42 results on '"Powell, Barry C."'
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2. Clustered Arrangement of Keratin Intermediate Filament Genes
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Powell, Barry C., Cam, Graham R., Fietz, Michael J., and Rogers, George E.
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- 1986
3. Retinol-binding protein 4 is expressed in chondrocytes of developing mouse long bones: implications for a local role in formation of the secondary ossification center
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Hatfield, Jodie T., Anderson, Peter J., and Powell, Barry C.
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- 2013
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4. Retinol-binding protein 4 downregulation during osteogenesis and its localization to non-endocytic vesicles in human cranial suture mesenchymal cells suggest a novel tissue function
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Leitch, Victoria D., Dwivedi, Prem P., Anderson, Peter J., and Powell, Barry C.
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- 2013
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5. Decreased expression of Flightless I, a gelsolin family member and developmental regulator, in early-gestation fetal wounds improves healing
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Lin, Cheng-Hung, Waters, James M., Powell, Barry C., Arkell, Ruth M., and Cowin, Allison J.
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- 2011
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6. Δ6 Desaturase mRNA Abundance in HepG2 Cells Is Suppressed by Unsaturated Fatty Acids
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Portolesi, Roxanne, Powell, Barry C., and Gibson, Robert A.
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- 2008
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7. Identification of genes differentially expressed by prematurely fused human sutures using a novel in vivo–in vitro approach
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Coussens, Anna K., Hughes, Ian P., Wilkinson, Christopher R., Morris, C. Phillip, Anderson, Peter J., Powell, Barry C., and van Daal, Angela
- Published
- 2008
8. An ultrahigh-sulphur keratin gene of the human hair cuticle is located at 11q13 and cross-hybridizes with sequences at 11p15
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MacKinnon, Philip J., Powell, Barry C., Rogers, George E., Baker, Elizabeth G., MacKinnon, Ruth N., Hyland, Valentine J., Callen, David F., and Sutherland, Grant R.
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- 1991
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9. Development of an efficient, non-viral transfection method for studying gene function and bone growth in human primary cranial suture mesenchymal cells reveals that the cells respond to BMP2 and BMP3
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Dwivedi Prem P, Anderson Peter J, and Powell Barry C
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Transfection ,Nucleofection ,Skull ,Bone ,Primary cell culture ,Mesenchymal ,BMP2 ,luciferase ,Biotechnology ,TP248.13-248.65 - Abstract
Abstract Background Achieving efficient introduction of plasmid DNA into primary cultures of mammalian cells is a common problem in biomedical research. Human primary cranial suture cells are derived from the connective mesenchymal tissue between the bone forming regions at the edges of the calvarial plates of the skull. Typically they are referred to as suture mesenchymal cells and are a heterogeneous population responsible for driving the rapid skull growth that occurs in utero and postnatally. To better understand the molecular mechanisms involved in skull growth, and in abnormal growth conditions, such as craniosynostosis, caused by premature bony fusion, it is essential to be able to easily introduce genes into primary bone forming cells to study their function. Results A comparison of several lipid-based techniques with two electroporation-based techniques demonstrated that the electroporation method known as nucleofection produced the best transfection efficiency. The parameters of nucleofection, including cell number, amount of DNA and nucleofection program, were optimized for transfection efficiency and cell survival. Two different genes and two promoter reporter vectors were used to validate the nucleofection method and the responses of human primary suture mesenchymal cells by fluorescence microscopy, RT-PCR and the dual luciferase assay. Quantification of bone morphogenetic protein (BMP) signalling using luciferase reporters demonstrated robust responses of the cells to both osteogenic BMP2 and to the anti-osteogenic BMP3. Conclusions A nucleofection protocol has been developed that provides a simple and efficient, non-viral alternative method for in vitro studies of gene and protein function in human skull growth. Human primary suture mesenchymal cells exhibit robust responses to BMP2 and BMP3, and thus nucleofection can be a valuable method for studying the potential competing action of these two bone growth factors in a model system of cranial bone growth.
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- 2012
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10. Expression of the Homeobox Gene, Barx2, in Wool Follicle Development
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Sander, Guy, Bawden, C. Simon, Hynd, Philip I., Nesci, Antonietta, Rogers, George, and Powell, Barry C.
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- 2000
11. Bone to pick: the importance of evaluating reference genes for RT-qPCR quantification of gene expression in craniosynostosis and bone-related tissues and cells
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Yang Xianxian, Hatfield Jodie T, Hinze Susan J, Mu Xiongzheng, Anderson Peter J, and Powell Barry C
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Osteocalcin ,Alkaline phosphatase ,18 S RNA ,Gapdh ,β-actin ,geNorm ,Normfinder ,Craniosynostosis ,Bone ,Mineralization ,Medicine ,Biology (General) ,QH301-705.5 ,Science (General) ,Q1-390 - Abstract
Abstract Background RT-qPCR is a common tool for quantification of gene expression, but its accuracy is dependent on the choice and stability (steady state expression levels) of the reference gene/s used for normalization. To date, in the bone field, there have been few studies to determine the most stable reference genes and, usually, RT-qPCR data is normalised to non-validated reference genes, most commonly GAPDH, ACTB and 18 S rRNA. Here we draw attention to the potential deleterious impact of using classical reference genes to normalise expression data for bone studies without prior validation of their stability. Results Using the geNorm and Normfinder programs, panels of mouse and human genes were assessed for their stability under three different experimental conditions: 1) disease progression of Crouzon syndrome (craniosynostosis) in a mouse model, 2) proliferative culture of cranial suture cells isolated from craniosynostosis patients and 3) osteogenesis of a mouse bone marrow stromal cell line. We demonstrate that classical reference genes are not always the most ‘stable’ genes and that gene ‘stability’ is highly dependent on experimental conditions. Selected stable genes, individually or in combination, were then used to normalise osteocalcin and alkaline phosphatase gene expression data during cranial suture fusion in the craniosynostosis mouse model and strategies compared. Strikingly, the expression trends of alkaline phosphatase and osteocalcin varied significantly when normalised to the least stable, the most stable or the three most stable genes. Conclusion To minimise errors in evaluating gene expression levels, analysis of a reference panel and subsequent normalization to several stable genes is strongly recommended over normalization to a single gene. In particular, we conclude that use of single, non-validated “housekeeping” genes such as GAPDH, ACTB and 18 S rRNA, currently a widespread practice by researchers in the bone field, is likely to produce data of questionable reliability when changes are 2 fold or less, and such data should be interpreted with due caution.
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- 2012
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12. Unravelling the molecular control of calvarial suture fusion in children with craniosynostosis
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Morris C Phillip, Hughes Ian P, Wilkinson Christopher R, Coussens Anna K, van Daal Angela, Anderson Peter J, and Powell Barry C
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Biotechnology ,TP248.13-248.65 ,Genetics ,QH426-470 - Abstract
Abstract Background Craniosynostosis, the premature fusion of calvarial sutures, is a common craniofacial abnormality. Causative mutations in more than 10 genes have been identified, involving fibroblast growth factor, transforming growth factor beta, and Eph/ephrin signalling pathways. Mutations affect each human calvarial suture (coronal, sagittal, metopic, and lambdoid) differently, suggesting different gene expression patterns exist in each human suture. To better understand the molecular control of human suture morphogenesis we used microarray analysis to identify genes differentially expressed during suture fusion in children with craniosynostosis. Expression differences were also analysed between each unfused suture type, between sutures from syndromic and non-syndromic craniosynostosis patients, and between unfused sutures from individuals with and without craniosynostosis. Results We identified genes with increased expression in unfused sutures compared to fusing/fused sutures that may be pivotal to the maintenance of suture patency or in controlling early osteoblast differentiation (i.e. RBP4, GPC3, C1QTNF3, IL11RA, PTN, POSTN). In addition, we have identified genes with increased expression in fusing/fused suture tissue that we suggest could have a role in premature suture fusion (i.e. WIF1, ANXA3, CYFIP2). Proteins of two of these genes, glypican 3 and retinol binding protein 4, were investigated by immunohistochemistry and localised to the suture mesenchyme and osteogenic fronts of developing human calvaria, respectively, suggesting novel roles for these proteins in the maintenance of suture patency or in controlling early osteoblast differentiation. We show that there is limited difference in whole genome expression between sutures isolated from patients with syndromic and non-syndromic craniosynostosis and confirmed this by quantitative RT-PCR. Furthermore, distinct expression profiles for each unfused suture type were noted, with the metopic suture being most disparate. Finally, although calvarial bones are generally thought to grow without a cartilage precursor, we show histologically and by identification of cartilage-specific gene expression that cartilage may be involved in the morphogenesis of lambdoid and posterior sagittal sutures. Conclusion This study has provided further insight into the complex signalling network which controls human calvarial suture morphogenesis and craniosynostosis. Identified genes are candidates for targeted therapeutic development and to screen for craniosynostosis-causing mutations.
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- 2007
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13. Studying Permeability in a Commonly Used Epithelial Cell Line: T84 Intestinal Epithelial Cells.
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Donato, Rino P., El-Merhibi, Adaweyah, Gundsambuu, Batjargal, Mak, Kai Yan, Formosa, Emma R., Wang, Xian, Abbott, Catherine A., and Powell, Barry C.
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- 2011
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14. Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins
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Sander, Guy R., Cummins, Adrian G., and Powell, Barry C.
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- 2005
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15. Decreased expression of Flightless I, a gelsolin family member and developmental regulator, in early-gestation fetal wounds improves healing.
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Cheng-Hung Lin, Waters, James, Powell, Barry C., Arkell, Ruth M., and Cowin, Allison J.
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PREGNANCY ,IMMUNOFLUORESCENCE ,KERATINOCYTES ,WOUND healing ,FETUS ,ACTIN ,LABORATORY rats - Abstract
Up until late in the third trimester of gestation and through to adulthood, the healing response acts more to regenerate than to repair a wound. The mechanisms underlying this 'scar-free' healing remain unknown although the actin cytoskeleton has a major role. Flightless I (Flii), an actin-remodelling protein and essential developmental regulator, negatively affects wound repair but its effect on scar-free fetal healing is unknown. Using fetal skin explants from E17 (regenerate) and E19 (repair) rats, the function of Flii in fetal wound repair was determined. Expression of Flii increased between E17 and E19 days of gestation and wounding transiently increased Flii expression in E17 but not E19 wounds. However, both confocal and immunofluorescent analysis showed E17 keratinocytes immediately adjacent to the wounds downregulated Flii. As a nuclear coactivator and inhibitor of proliferation and migration, the absence of Flii in cells at the edge of the wound could be instrumental in allowing these cells to proliferate and migrate into the wound deficit. In contrast, Flii was strongly expressed within the cytoplasm and nucleus of keratinocytes within epidermal cells at the leading edge of E19 wounded fetal skin explants. This increase in Flii expression in E19 wounds could affect the way these cells migrate into the wound space and contribute to impaired wound healing. Neutralising Flii protein improved healing of early- but not late-gestation wounds. Flii did not colocalise with actin cables formed around E17 wounds suggesting an independent mechanism of action distinct from its actin-binding function in scar-free wound repair. [ABSTRACT FROM AUTHOR]
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- 2011
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16. In vitro differentiation of human calvarial suture derived cells with and without dexamethasone does not induce in vivo-like expression.
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Coussens, Anna K., Hughes, Ian P., Morris, C. Phillip, Powell, Barry C., and Anderson, Peter J.
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VITAMIN C ,SUTURES ,PHOSPHATES ,CELLS ,GENE expression ,CELL culture - Abstract
Osteogenic supplements are a requirement for osteoblastic cell differentiation during in vitro culture of human calvarial suture-derived cell populations. We investigated the ability of ascorbic acid and β-glycerophosphate with and without the addition of dexamethasone to stimulate in vivo-like osteoblastic differentiation. Cells were isolated from unfused and prematurely fused suture tissue from patients with syndromic and non-syndromic craniosynostosis and cultured in each osteogenic medium for varying lengths of time. The effect of media supplementation was investigated with respect to the ability of cells to form mineralised bone nodules and the expression of five osteodifferentiation marker genes (COL1A1, ALP, BSP, OC and RUNX2), and five genes that are differentially expressed during human premature suture fusion (GPC3, RBP4, C1QTNF3, WIF1 and FGF2). Cells from unfused sutures responded more slowly to osteogenic media but formed comparable bone nodules to fused suture-derived cells after 16 days of culture in either osteogenic media. However, gene expression differed between unfused and fused suture-derived cells, as did expression in each osteogenic medium. When compared to expression in the explant tissue of origin, neither medium induced a level or profile of gene expression similar to that seen in vivo. Overall, our results demonstrate that cells from the same suture that are isolated during different stages of morphogenesis in vivo, despite being de-differentiated to a similar level in vitro, respond uniquely and differently to each osteogenic medium. Further, we suggest that neither cell culture medium recapitulates differentiation via activation of the same genetic cascades as occurs in vivo. J. Cell. Physiol. 218: 183–191, 2009. © 2008 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]
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- 2009
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17. Identification of a novel FcγRIII receptor that is up-regulated in fetal wound healing.
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Teusner, Jacqueline T., Goddard, Chris, Belford, David A., Dunaiski, Vera, and Powell, Barry C.
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FETUS ,SKIN injuries ,ANIMAL models of wound healing ,SCARS ,REGENERATION (Biology) ,LABORATORY rats - Abstract
The mid-gestation fetus is able to heal skin wounds rapidly and without scarring, an ability that is lost as development proceeds. The aim of this study was to identify novel genes involved in this process. We established an ex vivo wound model from embryonic rats and showed that over 72 hours, embryonic day 17 wounds reepithelialized and closed whereas day 19 wounds did not. To investigate the molecular basis of this phenomenon we analyzed changes in gene expression using differential display polymerase chain reaction. We characterized one transcript that was strongly up-regulated in the healing response of wounded, day 17 skin. It encodes a protein of 249 amino acids with striking similarity to the human low-affinity receptor for the Fc portion of IgG (FcγRIII), suggesting that it is a novel member of the FcγR family, which we named FcγRIII-X. A wound-healing timecourse shows that FcγRIII-X was up-regulated in healing, wounded day 17 skin but not in nonhealing, wounded day 19 skin and that its up-regulation was accelerated in skin with multiple wounds. We suggest that up-regulation of FcγRIII-X may contribute to scarless healing of fetal skin. [ABSTRACT FROM AUTHOR]
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- 2006
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18. Differential Expression of Genes Encoding a Cysteine-Rich Keratin Family in the Hair Cuticle.
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Jenkins, Brendan J. and Powell, Barry C.
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CUTICLE , *GENES , *KERATIN , *GLYCINE , *HAIR follicles , *WOOL , *IN situ hybridization , *AMINO acids - Abstract
In the hair follicle the cuticle develops as a thin layer of cells between the hair shaft cortex and the inner root sheath. Once the cuticle cells begin to differentiate they accumulate cysteine-rich granules in their cytoplasm but the identity of their constituent proteins has remained largely an enigma. In this report we show differential expression of a family of genes encoding cysteine-rich, glycine-rich keratins in the cuticle. Two clones of the sheep KAP5 gene family were isolated: the KAP5.4 cDNA encodes a protein of 190 amino acids (Mr = 16,936) containing 32 mol% cysteine, 26 mol% glycine and the partial KAP5.5 cDNA encodes a protein of at least 197 amino acids (Mr ≥ 17,474) containing 29 mol% cysteine, 28 mol% glycine. The predicted amino acid sequences of the KAP5 family show extensive sequence conservation and all the proteins are composed almost entirely of cysteine-rich and glycine-rich repeats. Each KAP5 gene produces an ∼ 1.5- kb mRNA species but the KAP5.4 and KAP5.5 mRNA levels appear to be severalfold greater than the KAP5.1 mRNA. Comparative tissue in situ hybridizations reveal a positive correlation between the onset of expression and follicle depth. For a given KAP5 gene two widely different cuticle expression patterns were noted amongst the follicle populations, and on the basis of follicle bulb cell kinetics they are consistent with expression in either sheep primary or secondary follicle types. [ABSTRACT FROM AUTHOR]
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- 1994
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19. Dietary Cysteine Regulates the Levels of mRNAs Encoding a Family of Cysteine-Rich Proteins of Wool.
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Fratini, Antonio, Powell, Barry C., Hynd, Philip I., Keough, Rebecca A., and Rogers, George E.
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KERATIN , *WOOL , *NUTRITION , *GENE expression , *AMINO acids , *RNA - Abstract
The abomasal or intravenous infusion of sulphur-containing amino acids such as cysteine or methionine into sheep on low-quality diets increases the sulphur content of the wool by increasing the synthesis of proteins containing a cysteine content of ∼ 30 mol %. To investigate the molecular and cellular basis of this nutritional effect, quantitative analyses of wool keratin mRNA and protein levels, and follicle cortical cell type, were undertaken in sheep intravenously infused with cysteine. Northern blot analyses revealed that the mRNA levels of one gene family encoding cysteine-rich keratin-associated proteins (KAP4 family) expressed in the wool follicle cortex, increased ∼ 5-6 times. Furthermore, the response was rapid as the mRNA levels increased ∼ 3.5 times after 1 d of the cysteine infusion and, by 1 d post-infusion, they had fallen, approaching their basal level. No changes in the mRNA levels encoding the intermediate filament or the other keratin-associated protein families of lower cysteine content were observed. Concomitantly, two-dimensional polyacrylamide gel electrophoresis analysis of wool proteins showed a striking increase in the abundance of a group of cysteine-rich keratin-associated proteins in the wool by the end of the infusion period, returning to basal levels by 3 weeks later. At the cellular level, KAP4 expression was localized to the follicle paracortical cells, and the proportion of paracortical cells and the extent of KAP4 expression paralleled the changes in the cysteine infusion status of the sheep. [ABSTRACT FROM AUTHOR]
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- 1994
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20. Characterization of a Hair (Wool) Keratin Intermediate Filament Gene Domain.
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Powell, Barry C. and Beltrame, Juliana S.
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KERATIN , *GENES , *HAIR follicles , *CHROMOSOMES , *WOOL , *DNA - Abstract
In epithelial differentiation keratin intermediate filament genes are expressed in multifarious tissue-specific and stage-specific patterns. Pairs of type I and type II intermediate filament genes, belonging to multigene families, are coordinately regulated, and 4 - 5 genes of each type are expressed in the hair follicle. Accumulating chromosomal mapping data points to a major locus for each intermediate filament multigene family on separate chromosomes. In this report we describe the isolation of a sheep hair keratin cosmid by chromosome walking that overlaps two previously described cosmids and establishes a continuous 100-kb segment of cloned DNA containing three hair and three hair-like type II intermediate filament keratin genes. A new hair keratin type II intermediate filament gene, KRT2.11, is located in the middle of the cluster, and partial sequence data reveal a striking conservation of its predicted N-terminal region with other sheep hair keratin type II intermediate filament proteins. Expression analyses demonstrate the presence of a 2.4-kb KRT2.11 transcript in wool follicle RNA and show that expression occurs in the follicle cortical keratinocytes above the dermal papilla. The three hair genes are clustered within about 40 kb and flanked by hair-like genes that are not expressed in the hair follicle, thereby demarcating a hair keratin gene domain. [ABSTRACT FROM AUTHOR]
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- 1994
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21. Organization and Expression of Hair Follicle Genes.
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Rogers, George E. and Powell, Barry C.
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HAIR growth stimulants , *PROTEINS , *KERATIN , *DERMATOLOGIC agents , *GENES , *HAIR care products , *AMINO acids - Abstract
Several families of proteins are expressed in the growth of hair and an estimated 50-100 proteins constitute the final hair fiber. The cumbersome nomenclature for naming these different proteins has led to a proposal to modify that which is currently used for epidermal keratins. Investigations of the organization of hair genes indicate that the members of each family are clustered in the genome and their expression could be under some general control. Interestingly, the protein called trichohyalin, markedly distinct from the hair proteins, is produced in the inner root sheath cells and the gene for it has been found to be located at the same human chromosome locus as the genes for profilaggrin, involucrin, and loricrin. A mainstream objective is to identify controls responsible for the production in the hair cortex of keratin intermediate filaments (IFs) and two large groups of keratin-associated proteins (KAPs) rich in the amino acids cysteine or glycine/tyrosine. A specific family of cysteine-rich proteins is expressed in the hair cuticle. Comparisons of promoter regions of IF genes and KAP genes, including a recently characterized gene for a glycine/tyrosine-rich protein, have revealed putative hair-specific motifs in addition to known elements that regulate gene expression. In the sheep, the patterns of expression in hair differentiation are particularly interesting insofar as there are distinct segments of para- and orthocortical type cells that have significantly different pathways of expression. The testing of candidate hair-specific regulatory sequences by mouse transgenesis has produced several interesting hair phenotypes. Transgenic sheep over-expressing keratin genes but showing no hair growth change have been obtained and compared with the equivalent transgenic hair-loss mice. Studies of the effects of amino acid supply on the rate of hair growth have demonstrated that with cysteine supplementation of sheep a perturbation occurs in which there is a markedly increased level of only one type of mRNA and the ration of para- to orthocortical cells is increased. A molecular explanation of this phenomenon is being sought. [ABSTRACT FROM AUTHOR]
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- 1993
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22. Complete sequence of a hair-like intermediate filament type II keratin gene.
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Powell, Barry C., Crocker, Lesley A., and Rogers, George E.
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- 1993
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23. Isolation and characterization of a sheep cysteine-rich cuticle keratin pseudogene.
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Jenkins, Brendan J. and Powell, Barry C.
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- 1992
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24. Regulation of Keratin Gene Expression in Hair Follicle Differentiationa.
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POWELL, BARRY C., NESCI, ANTONIETTA, and ROGERS, GEORGE E.
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- 1991
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25. Isolation of messenger RNA coding for the “fast” protein of embryonic chick feathers.
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Powell, Barry C. and Rogers, George E.
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- 1979
26. Corrigendum to “Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins FEBS (29865)” [FEBS Letters 579 (2005) 4851–4855]
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Sander, Guy R., Cummins, Adrian G., Henshall, Tanya, and Powell, Barry C.
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- 2005
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27. T1270 Gliadin Induced Increase in Intestinal Epithelial Permeability Is Independent of MEK.
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Staudacher, Alex, Powell, Barry C., and Sander, Guy R.
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- 2008
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28. Flightless I Regulates Hemidesmosome Formation and Integrin-Mediated Cellular Adhesion and Migration during Wound Repair.
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Kopecki, Zlatko, Arkell, Ruth, Powell, Barry C., and Cowin, Allison J.
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HEMIDESMOSOMES , *EPITHELIAL cells , *CELL junctions , *CELL adhesion molecules , *CELL communication , *MEMBRANE fusion , *CELL membranes - Abstract
Flightless I (Flii), a highly conserved member of the gelsolin family of actin-remodelling proteins associates with actin structures and is involved in cellular motility and adhesion. Our previous studies have shown that Flii is an important negative regulator of wound repair. Here, we show that Flii affects hemidesmosome formation and integrin-mediated keratinocyte adhesion and migration. Impaired hemidesmosome formation and sparse arrangements of keratin cytoskeleton tonofilaments and actin cytoskeleton anchoring fibrils were observed in FliiTg/+ and FliiTg/Tg mice with their skin being significantly more fragile than Flii+/− and WT mice. Flii+/− primary keratinocytes showed increased adhesion on laminin and collagen I than WT and FliiTg/Tg primary keratinocytes. Decreased expression of CD151 and laminin-binding integrins α3, β1, α6 and β4 were observed in Flii overexpressing wounds, which could contribute to the impaired wound re-epithelialization observed in these mice. Flii interacts with proteins directly linked to the cytoplasmic domain of integrin receptors suggesting that it may be a mechanical link between ligand-bound integrin receptors and the actin cytoskeleton driving adhesion-signaling pathways. Therefore Flii may regulate wound repair through its effect on hemidesmosome formation and integrin-mediated cellular adhesion and migration.Journal of Investigative Dermatology (2009) 129, 2031–2045; doi:10.1038/jid.2008.461; published online 12 February 2009 [ABSTRACT FROM AUTHOR]
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- 2009
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29. Chapter 10 - Developmental Signaling Networks: The Notch Pathway
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Sander, Guy R., Krysinska, Hanna, and Powell, Barry C.
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30. Regulation of epithelial apical junctions and barrier function by Gα13
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Donato, Rino, Wood, Stephen A., Saunders, Ian, Gundsambuu, Batjargal, Yan Mak, Kai, Abbott, Catherine A., and Powell, Barry C.
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CELLULAR control mechanisms , *TIGHT junctions , *CELL physiology , *EPITHELIAL cells , *G proteins , *CELL permeability , *CELL lines , *CYTOGENETICS , *GENE expression - Abstract
Abstract: The epithelial tight junction forms a barrier to paracellular solute movement. In this study we show that the heterotrimeric G-protein Gα13 regulates the epithelial tight junction barrier. We generated MDCKII kidney epithelial cell lines in which the expression of an active Gα13 mutant (Gα13Q226L) could be induced. We demonstrated that Gα13Q226L expression increased paracellular permeability and caused the disruption and redistribution of proteins comprising the tight junction and the adherens junction away from sites of cell contact and the appearance of basal stress fibers. The effects on the junctional proteins and the actin cytoskeleton were abrogated by the Rho kinase inhibitor Y27632 but not by the Src kinase inhibitor PP2. The Gα13 mediated increase in permeability was also Src kinase independent but was partly dependent on Rho kinase signalling. Our data establish a link between Gα13, Rho kinase signaling and epithelial barrier function and not only demonstrate that Gα13 regulates epithelial apical junction properties but that it does so via signaling pathways that are distinct from the closely related protein Gα12. [Copyright &y& Elsevier]
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- 2009
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31. Gender specific effects on the actin-remodelling protein Flightless I and TGF-β1 contribute to impaired wound healing in aged skin
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Adams, Damian H., Strudwick, Xanthe L., Kopecki, Zlatko, Hooper-Jones, Jane A., Matthaei, Klaus I., Campbell, Hugh D., Powell, Barry C., and Cowin, Allison J.
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GERIATRICS , *REGENERATION (Biology) , *DEVELOPMENTAL biology , *ESTROGEN - Abstract
Abstract: Impaired wound healing in the elderly presents a major clinical challenge. Understanding the cellular mechanisms behind age-related impaired healing is vital for developing new wound therapies. Here we show that the actin-remodelling protein, Flightless I (FliI) is a contributing factor to the poor healing observed in elderly skin and that gender plays a major role in this process. Using young and aged, wild-type and FliI overexpressing mice we found that aging significantly elevated FliI expression in the epidermis and wound matrix. Aging exacerbated the negative effect of FliI on wound repair and wounds in aged FliI transgenic mice were larger with delayed reepithelialisation. When the effect of gender was further analysed, despite increased FliI expression in young and aged male and female mice, female FliI transgenic mice had the most severe wound healing phenotype suggesting that male mice were refractory to FliI gene expression. Of potential importance, males, but not females, up-regulated transforming growth factor-β1 and this was most pronounced in aged male FliI overexpressing wounds. As FliI also functions as a co-activator of the estrogen nuclear receptor, increasing concentrations of β-estradiol were added to skin fibroblasts and keratinocytes and significantly enhanced FliI expression and translocation of FliI from the cytoplasm to the nucleus was observed. FliI further inhibited estrogen-mediated collagen I secretion suggesting a mechanism via which FliI may directly affect provisional matrix synthesis. In summary, FliI is a contributing factor to impaired healing and strategies aimed at decreasing FliI levels in elderly skin may improve wound repair. [Copyright &y& Elsevier]
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- 2008
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32. Retinol-binding protein 4 downregulation during osteogenesis and its localization to non-endocytic vesicles in human cranial suture mesenchymal cells suggest a novel tissue function
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Victoria D. Leitch, Barry C. Powell, Prem P. Dwivedi, Peter J. Anderson, Leitch, Victoria D, Dwivedi, Prem P, Anderson, Peter J, and Powell, Barry C
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Pathology ,medicine.medical_specialty ,Time Factors ,Histology ,Endosome ,Mesenchyme ,Primary Cell Culture ,Down-Regulation ,Biology ,mesenchymal ,retinol-binding protein 4 ,Craniosynostosis ,Craniosynostoses ,symbols.namesake ,Osteogenesis ,medicine ,Humans ,mineralization ,STRA6 ,Vitamin A ,Molecular Biology ,endosome ,Cells, Cultured ,vesicle ,Microscopy, Confocal ,Cytoplasmic Vesicles ,Mesenchymal stem cell ,Membrane Proteins ,Mesenchymal Stem Cells ,Cranial Sutures ,Cell Biology ,Golgi apparatus ,Flow Cytometry ,medicine.disease ,Cell biology ,Medical Laboratory Technology ,Retinol binding protein ,craniosynostosis ,medicine.anatomical_structure ,Endocytic vesicle ,Microscopy, Fluorescence ,Cell culture ,Organelle Size ,symbols ,calvarial ,Retinol-Binding Proteins, Plasma - Abstract
Craniosynostosis is a developmental disorder of the skull arising from premature bony fusion of cranial sutures, the sites of skull bone growth. In a recent gene microarray study, we demonstrated that retinol-binding protein ₄ (RBP₄) was the most highly downregulated gene in suture tissue during the pathological process of premature bony fusion. To gain insight into the function of RBP₄ in cranial sutures, we analysed primary cells cultured from human cranial suture mesenchyme. These cells express RBP₄ but not CRBP₁, cellular retinol-binding protein ₁, the typical cytoplasmic retinol storage protein. Using flow cytometry, we showed that suture mesenchymal cells express the RBP₄ receptor, STRA6, on the cell surface. In a cell culture model of cranial osteogenesis, we found that RBP₄ was significantly downregulated during mineralization, analogous to its decrease in pathological suture fusion. We found that cranial suture cells do not secrete detectable levels of RBP₄, suggesting that it acts in a cell-autonomous manner. High-resolution confocal microscopy with a panel of antibody markers of cytoplasmic organelles demonstrated that RBP₄ was present in several hundred cytoplasmic vesicles of about 300 nm in diameter which, in large part, were conspicuously distinct from the ER, the Golgi and endosomes of the endocytic pathway. We speculate that in suture mesenchymal cells, endogenous RBP₄ receives retinol from STRA6 and the RBP₄-retinol complex is stored in vesicles until needed for conversion to retinoic acid in the process of osteogenesis. This study extends the role of RBP₄ beyond that of a serum transporter of retinol and implicates a broader role in osteogenesis. Refereed/Peer-reviewed
- Published
- 2013
33. Boning up on glypicans-opportunities for new insights into bone biology
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Dwivedi, Prem, Lam, N, and Powell, Barry C
- Subjects
WNT ,hedgehog ,receptor ,chondrocyte ,endochondral ,BMP ,glypican ,bone - Abstract
Bone formation is remarkable for the convergence in the activity of four major signalling pathways, the bone morphogenetic protein (BMP), fibroblast growth factor (FGF), hedgehog (HH) and wingless-integrated (WNT) pathways. These pathways cooperate in morphogenetic, proliferative and differentiative processes that underpin the development, growth and repair of skeletal structures. They are regulated by pathway-specific modulators and by another class of molecules, the glypicans. Glypicans are proteoglycans located on the cell surface, where they act as coreceptors to promote or inhibit signalling by ligands of the BMP, FGF, HH and WNT pathways, through protein–protein and protein–carbohydrate interactions. In this review, we discuss glypican structure, expression and function in the context of bone development and growth, with emphasis on the long bone growth plate where five of the six glypicans are expressed in overlapping patterns in the chondrogenic zone. Analyses of gene knockout models and the human conditions of Simpson–Golabi–Behmel syndrome and omodysplasia, which arise from mutations in glypican 3 (GPC3) and GPC6, respectively, highlight both subtle and striking effects of glypicans on bone growth. We draw attention to challenges and areas of opportunity, where the actions of glypicans on BMP, FGF, HH and WNT signalling might be profitably studied to help illuminate the complex interplay of signalling that drives bone growth. Refereed/Peer-reviewed
- Published
- 2013
34. Somatic FGFR and TWIST mutations are not a common cause of isolated nonsyndromic single suture craniosynostosis
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Anderson, PJ, Cox, TC, Roscioli, T, Elakis, G, Smithers, Lisa Gaye, David, D, and Powell, Barry C
- Published
- 2007
35. Development of an efficient, non-viral transfection method for studying gene function and bone growth in human primary cranial suture mesenchymal cells reveals that the cells respond to BMP2 and BMP3
- Author
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Barry C. Powell, Peter J. Anderson, Prem P. Dwivedi, Dwivedi, Prem P, Anderson, Peter J, and Powell, Barry C
- Subjects
skull ,Mesenchymal ,Cell Survival ,lcsh:Biotechnology ,Green Fluorescent Proteins ,BMP2 ,Bone Morphogenetic Protein 2 ,Bone Morphogenetic Protein 3 ,Nucleofection ,mesenchymal ,Biology ,Bone morphogenetic protein ,Transfection ,bone ,Bone morphogenetic protein 2 ,Mice ,Glypicans ,Genes, Reporter ,lcsh:TP248.13-248.65 ,Animals ,Humans ,Primary cell culture ,nucleofection ,Bone ,Cells, Cultured ,Bone growth ,Methodology Article ,Electroporation ,Mesenchymal stem cell ,Skull ,Mesenchymal Stem Cells ,Cranial Sutures ,luciferase ,Molecular biology ,Cell biology ,transfection ,Liposomes ,Stem cell ,primary cell culture ,Plasmids ,Biotechnology - Abstract
Background Achieving efficient introduction of plasmid DNA into primary cultures of mammalian cells is a common problem in biomedical research. Human primary cranial suture cells are derived from the connective mesenchymal tissue between the bone forming regions at the edges of the calvarial plates of the skull. Typically they are referred to as suture mesenchymal cells and are a heterogeneous population responsible for driving the rapid skull growth that occurs in utero and postnatally. To better understand the molecular mechanisms involved in skull growth, and in abnormal growth conditions, such as craniosynostosis, caused by premature bony fusion, it is essential to be able to easily introduce genes into primary bone forming cells to study their function. Results A comparison of several lipid-based techniques with two electroporation-based techniques demonstrated that the electroporation method known as nucleofection produced the best transfection efficiency. The parameters of nucleofection, including cell number, amount of DNA and nucleofection program, were optimized for transfection efficiency and cell survival. Two different genes and two promoter reporter vectors were used to validate the nucleofection method and the responses of human primary suture mesenchymal cells by fluorescence microscopy, RT-PCR and the dual luciferase assay. Quantification of bone morphogenetic protein (BMP) signalling using luciferase reporters demonstrated robust responses of the cells to both osteogenic BMP2 and to the anti-osteogenic BMP3. Conclusions A nucleofection protocol has been developed that provides a simple and efficient, non-viral alternative method for in vitro studies of gene and protein function in human skull growth. Human primary suture mesenchymal cells exhibit robust responses to BMP2 and BMP3, and thus nucleofection can be a valuable method for studying the potential competing action of these two bone growth factors in a model system of cranial bone growth.
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36. Studying permeability in a commonly used epithelial cell line: T84 intestinal epithelial cells.
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Donato RP, El-Merhibi A, Gundsambuu B, Mak KY, Formosa ER, Wang X, Abbott CA, and Powell BC
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- Blotting, Western, Cell Line, Dextrans analysis, Diffusion Chambers, Culture, Electrophoresis, Polyacrylamide Gel, Epithelial Cells cytology, Fluorescein-5-isothiocyanate analogs & derivatives, Fluorescein-5-isothiocyanate analysis, Fluorescent Antibody Technique, Humans, Immunohistochemistry, Inflammation immunology, Inflammation metabolism, Interferon Regulatory Factor-1 genetics, Interferon Regulatory Factor-1 immunology, Interferon-gamma genetics, Interferon-gamma immunology, Intestinal Mucosa cytology, Intestines cytology, Membrane Proteins genetics, Occludin, Permeability, Plasmids, Tight Junctions genetics, Tight Junctions immunology, Transfection, Epithelial Cells metabolism, Interferon Regulatory Factor-1 metabolism, Interferon-gamma metabolism, Intestinal Mucosa metabolism, Membrane Proteins metabolism, Tight Junctions metabolism
- Abstract
The integrity, or barrier function, of the intestinal epithelium is of paramount importance in -maintaining good health. This is largely imparted by a single layer of epithelial cells linked by the transmembrane tight junction protein complex near their apical surface. Disruption of epithelial permeability via the tight junctions can contribute to disease progression. The cytokine IFNγ is involved in many inflammatory processes and has been shown to dramatically increase permeability via changes at the tight junction in experimental models. One of its key effectors is the transcription factor, -IRF-1. In our studies of the role of IRF-1 in barrier function using the human T84 intestinal epithelial cell monolayer model, we have found that induction of IRF-1 alone is insufficient to change permeability and that if IRF-1 is involved in mediating the permeability effects of IFNγ, then other factors must also be required.
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- 2011
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37. Delta6 desaturase mRNA abundance in HepG2 cells is suppressed by unsaturated fatty acids.
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Portolesi R, Powell BC, and Gibson RA
- Subjects
- Cell Line, Tumor, Fatty Acid Desaturases, Humans, RNA, Messenger metabolism, Stearoyl-CoA Desaturase metabolism, Carcinoma, Hepatocellular drug therapy, Carcinoma, Hepatocellular enzymology, Fatty Acids, Unsaturated pharmacology, RNA, Messenger drug effects, Stearoyl-CoA Desaturase genetics
- Abstract
The effect of unsaturated fatty acids on the abundance of Delta6 desaturase (D6D) mRNA and the fatty acid composition of HepG2 cell membranes was examined. Supplementation of HepG2 cells with oleic acid (18:1n-9, OA), linoleic acid (18:2n-6, LA), alpha-linolenic acid (18:3n-3, ALA), arachidonic acid (20:4n-6, AA) or eicosapentaenoic acid (20:5n-3, EPA) reduced D6D mRNA abundance by 39 +/- 6.6, 40 +/- 2.2, 31 +/- 5.2, 55 +/- 4.8, and 52 +/- 5.0%, respectively, compared with control cells. Despite the reduction in D6D mRNA abundance, the level of D6D conversion products (20:3n-9, EPA and AA) in OA, ALA and LA supplemented cells, respectively, was elevated above that in control cells. Our results suggest that although unsaturated fatty acids decrease the abundance of D6D mRNA by as much as 50%, the conversion of polyunsaturated fatty acids and accumulation of long chain polyunsaturated fatty acids (LCPUFA) in HepG2 cell phospholipids continues to occur.
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- 2008
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38. Unravelling the molecular control of calvarial suture fusion in children with craniosynostosis.
- Author
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Coussens AK, Wilkinson CR, Hughes IP, Morris CP, van Daal A, Anderson PJ, and Powell BC
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- Acrocephalosyndactylia genetics, Adolescent, Adult, Aged, 80 and over, Cell Fusion, Child, Child, Preschool, Female, Gene Expression Profiling, Gene Expression Regulation, Developmental, Humans, Infant, Newborn, Male, Middle Aged, Models, Biological, Oligonucleotide Array Sequence Analysis, Cranial Sutures growth & development, Craniosynostoses genetics, Skull growth & development
- Abstract
Background: Craniosynostosis, the premature fusion of calvarial sutures, is a common craniofacial abnormality. Causative mutations in more than 10 genes have been identified, involving fibroblast growth factor, transforming growth factor beta, and Eph/ephrin signalling pathways. Mutations affect each human calvarial suture (coronal, sagittal, metopic, and lambdoid) differently, suggesting different gene expression patterns exist in each human suture. To better understand the molecular control of human suture morphogenesis we used microarray analysis to identify genes differentially expressed during suture fusion in children with craniosynostosis. Expression differences were also analysed between each unfused suture type, between sutures from syndromic and non-syndromic craniosynostosis patients, and between unfused sutures from individuals with and without craniosynostosis., Results: We identified genes with increased expression in unfused sutures compared to fusing/fused sutures that may be pivotal to the maintenance of suture patency or in controlling early osteoblast differentiation (i.e. RBP4, GPC3, C1QTNF3, IL11RA, PTN, POSTN). In addition, we have identified genes with increased expression in fusing/fused suture tissue that we suggest could have a role in premature suture fusion (i.e. WIF1, ANXA3, CYFIP2). Proteins of two of these genes, glypican 3 and retinol binding protein 4, were investigated by immunohistochemistry and localised to the suture mesenchyme and osteogenic fronts of developing human calvaria, respectively, suggesting novel roles for these proteins in the maintenance of suture patency or in controlling early osteoblast differentiation. We show that there is limited difference in whole genome expression between sutures isolated from patients with syndromic and non-syndromic craniosynostosis and confirmed this by quantitative RT-PCR. Furthermore, distinct expression profiles for each unfused suture type were noted, with the metopic suture being most disparate. Finally, although calvarial bones are generally thought to grow without a cartilage precursor, we show histologically and by identification of cartilage-specific gene expression that cartilage may be involved in the morphogenesis of lambdoid and posterior sagittal sutures., Conclusion: This study has provided further insight into the complex signalling network which controls human calvarial suture morphogenesis and craniosynostosis. Identified genes are candidates for targeted therapeutic development and to screen for craniosynostosis-causing mutations.
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- 2007
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39. Competition between 24:5n-3 and ALA for Delta 6 desaturase may limit the accumulation of DHA in HepG2 cell membranes.
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Portolesi R, Powell BC, and Gibson RA
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- Cell Line, Tumor, Cell Membrane metabolism, Humans, Liver Neoplasms metabolism, Membrane Lipids biosynthesis, Carcinoma, Hepatocellular metabolism, Docosahexaenoic Acids metabolism, Linoleoyl-CoA Desaturase metabolism, alpha-Linolenic Acid metabolism
- Abstract
The use of Delta 6 desaturase (D6D) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA. We examined this using an in vitro model of fatty acid metabolism to measure the accumulation of the long-chain metabolites of ALA in HepG2 cell phospholipids. The accumulation of ALA, eicosapentaenoic acid (20:5n-3), docosapentaenoic acid (22:5n-3), and 24:5n-3 in cell phospholipids was linearly related to the concentration of supplemented ALA over the range tested (1.8-72 microM). The accumulation of the post-D6D products of 22:5n-3, 24:6n-3 and DHA, in cell phospholipids was saturated at concentrations of >18 microM ALA. Supplementation of HepG2 cells with preformed DHA revealed that, although the accumulation of DHA in cell phospholipids approached saturation, the level of DHA in cell phospholipids was significantly greater compared with the accumulation of DHA from ALA, indicating that the accumulation of DHA from ALA was not limited by incorporation. The parallel pattern of accumulation of 24:6n-3 and DHA in response to increasing concentrations of ALA suggests that the competition between 24:5n-3 and ALA for D6D may contribute to the limited accumulation of DHA in cell membranes.
- Published
- 2007
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40. Expression of notch receptors and ligands in the adult gut.
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Sander GR and Powell BC
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- Animals, Blotting, Northern, Calcium-Binding Proteins, Carrier Proteins biosynthesis, Carrier Proteins genetics, Digestive System cytology, Digestive System immunology, Endothelium metabolism, Esophagus metabolism, Female, In Situ Hybridization, Intercellular Signaling Peptides and Proteins, Intestinal Mucosa metabolism, Intestine, Large metabolism, Intestine, Small metabolism, Jagged-1 Protein, Jagged-2 Protein, Ligands, Organ Specificity, Protein Biosynthesis, Proteins genetics, Proto-Oncogene Proteins genetics, RNA, Messenger biosynthesis, Rats, Rats, Sprague-Dawley, Receptor, Notch1, Receptor, Notch2, Receptors, Cell Surface genetics, Serrate-Jagged Proteins, Digestive System metabolism, Membrane Proteins, Proto-Oncogene Proteins biosynthesis, Receptors, Cell Surface biosynthesis, Transcription Factors
- Abstract
The Notch signaling pathway has become recognized as a vitally important pathway in regulating proliferative/differentiative decisions and cell fate. To explore the involvement of the Notch pathway in adult gut, we investigated the expression of Notch receptors and their ligands by Northern blotting and in situ hybridization. Notch receptors and ligands were expressed in both proliferative and post-mitotic cells throughout adult rat gut, variously in epithelial, immune, and endothelial cells. Expression of Notch1, Jagged1, and Jagged2 frequently overlapped, whereas Notch2 expression was restricted to specific crypt cells, the lamina propria of the large intestine, and Peyer's patch lymphocytes. We propose that the expression of multiple Notch receptors and ligands in a range of different intestinal cell types indicates that this signaling pathway underpins many of the processes involved in the maintenance and function of the adult gut.
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- 2004
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41. Expression of the homeobox gene barx2 in the gut.
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Sander GR and Powell BC
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- Adenocarcinoma, Animals, Blotting, Northern, Cell Differentiation, Cell Division, Cell Line, Tumor, Colonic Neoplasms, Female, Gastric Mucosa cytology, Humans, In Situ Hybridization, Intestinal Mucosa cytology, Rats, Rats, Sprague-Dawley, Esophagus metabolism, Gastric Mucosa metabolism, Homeodomain Proteins biosynthesis, Intestinal Mucosa metabolism
- Abstract
Barx2 is a member of the Bar class of homeobox genes and has been shown to regulate specific cell adhesion molecules, L1, Ng-CAM, N-CAM, and cadherin 6. By Northern blotting and in situ hybridization, we show that Barx2 is expressed throughout the gut and is located in epithelial cells of the proliferative and differentiative regions of the stomach, esophagus, and intestine. Barx2 was expressed in muscle cells of the muscularis externa and also showed a graded pattern of expression in intestinal enterocytes, decreasing in a crypt-to-villous direction. We speculate that Barx2 may regulate cell adhesion molecules in epithelial cells of the gut.
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- 2004
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42. Expression of Notch1 and Jagged2 in the enteric nervous system.
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Sander GR, Brookes SJ, and Powell BC
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- Animals, Calbindin 2, Calcium-Binding Proteins, Enteric Nervous System anatomy & histology, Female, Fluorescent Antibody Technique, Immunohistochemistry, In Situ Hybridization, Intercellular Signaling Peptides and Proteins, Intestinal Mucosa innervation, Intestinal Mucosa metabolism, Jagged-2 Protein, Myenteric Plexus metabolism, Nitric Oxide Synthase metabolism, Proteins metabolism, Rats, Rats, Sprague-Dawley, Receptor, Notch1, Receptor, Notch2, Receptors, Cell Surface metabolism, S100 Calcium Binding Protein G metabolism, Serrate-Jagged Proteins, Submucous Plexus metabolism, Carrier Proteins metabolism, Enteric Nervous System metabolism, Membrane Proteins metabolism, Transcription Factors
- Abstract
The Notch signaling pathway is a vitally important pathway in regulating brain development. To explore the involvement of the Notch pathway in neuronal cells of adult rat gut, we investigated the expression of Notch1 and Jagged2 by in situ hybridization (ISH) and immunohistochemistry (IHC). In the enteric nervous system, Notch1 and Jagged2 were expressed in ganglia of the submucosal and myenteric plexus. Notch1 was preferentially expressed in cholinergic neurons lacking calretinin or nitric oxide synthase (NOS), whereas Jagged2 was present in most neuron subtypes. We propose that Notch1 and Jagged2 have a continuing role in the maintenance and function of neuronal cells in the adult enteric nervous system.
- Published
- 2003
- Full Text
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