16 results on '"Esko, Jeffrey D."'
Search Results
2. Multiplex genome editing of mammalian cells for producing recombinant heparin.
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Thacker, Bryan E., Thorne, Kristen J., Cartwright, Colin, Park, Jeeyoung, Glass, Kimberly, Chea, Annie, Kellman, Benjamin P., Lewis, Nathan E., Wang, Zhenping, Di Nardo, Anna, Sharfstein, Susan T., Jeske, Walter, Walenga, Jeanine, Hogwood, John, Gray, Elaine, Mulloy, Barbara, Esko, Jeffrey D., and Glass, Charles A.
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GENE expression profiling , *HEPARIN , *GENOME editing , *HEPARAN sulfate , *CHONDROITIN sulfates , *ANIMAL populations , *MAST cells - Abstract
Heparin is an essential anticoagulant used for treating and preventing thrombosis. However, the complexity of heparin has hindered the development of a recombinant source, making its supply dependent on a vulnerable animal population. In nature, heparin is produced exclusively in mast cells, which are not suitable for commercial production, but mastocytoma cells are readily grown in culture and make heparan sulfate, a closely related glycosaminoglycan that lacks anticoagulant activity. Using gene expression profiling of mast cells as a guide, a multiplex genome engineering strategy was devised to produce heparan sulfate with high anticoagulant potency and to eliminate contaminating chondroitin sulfate from mastocytoma cells. The heparan sulfate purified from engineered cells grown in chemically defined medium has anticoagulant potency that exceeds porcine-derived heparin and confers anticoagulant activity to the blood of healthy mice. This work demonstrates the feasibility of producing recombinant heparin from mammalian cell culture as an alternative to animal sources. • The mammalian glycosaminoglycan biosynthetic pathways have been genetically engineered. • The anticoagulant potency of engineered heparan sulfate exceeds that of unfractionated heparin. • This work demonstrates the feasibility of producing recombinant heparin from mammalian cells. [ABSTRACT FROM AUTHOR]
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- 2022
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3. Ndst1 is required for FGF signaling in early lens development
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Pan, Yi, Woodbury, Andrea, Esko, Jeffrey D., Grobe, Kay, and Zhang, Xin
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- 2006
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4. Intra-articular enzyme replacement therapy with rhIDUA is safe, well-tolerated, and reduces articular GAG storage in the canine model of mucopolysaccharidosis type I.
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Wang, Raymond Y., Aminian, Afshin, McEntee, Michael F., Shih-Hsin Kan, Simonaro, Calogera M., Lamanna, William C., Lawrence, Roger, Ellinwood, N. Matthew, Guerra, Catalina, Le, Steven Q., Dickson, Patricia I., and Esko, Jeffrey D.
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CARTILAGE cells , *HEMATOPOIETIC stem cells , *STEM cell transplantation , *IMMUNOGLOBULINS , *SPINAL cord , *LYSOSOMAL storage diseases - Abstract
Background: Treatment with intravenous enzyme replacement therapy and hematopoietic stem cell transplantation for mucopolysaccharidosis (MPS) type I does not address joint disease, resulting in persistent orthopedic complications and impaired quality of life. A proof-of-concept study was conducted to determine the safety, tolerability, and efficacy of intra-articular recombinant human iduronidase (IA-rhIDUA) enzyme replacement therapy in the canine MPS I model. Methods: Four MPS I dogs underwent monthly rhIDUA injections (0.58 mg/joint) into the right elbow and knee for 6 months. Contralateral elbows and knees concurrently received normal saline. No intravenous rhIDUA therapy was administered. Monthly blood counts, chemistries, anti-rhIDUA antibody titers, and synovial fluid cell counts were measured. Lysosomal storage of synoviocytes and chondrocytes, synovial macrophages and plasma cells were scored at baseline and 1 month following the final injection. Results: All injections were well-tolerated without adverse reactions. One animal required prednisone for spinal cord compression. There were no clinically significant abnormalities in blood counts or chemistries. Circulating anti-rhIDUA antibody titers gradually increased in all dogs except the prednisone-treated dog; plasma cells, which were absent in all baseline synovial specimens, were predominantly found in synovium of rhIDUA-treated joints at study-end. Lysosomal storage in synoviocytes and chondrocytes following 6 months of IA-rhIDUA demonstrated significant reduction compared to tissues at baseline, and saline-treated tissues at study-end. Mean joint synovial GAG levels in IA-rhIDUA joints were 8.62 ± 5.86 µg/mg dry weight and 21.6 ± 10.4 µg/mg dry weight in control joints (60% reduction). Cartilage heparan sulfate was also reduced in the IA-rhIDUA joints (113 ± 39.5 ng/g wet weight) compared to saline-treated joints (142 ± 56.4 ng/g wet weight). Synovial macrophage infiltration, which was present in all joints at baseline, was abolished in rhIDUA-treated joints only. Conclusions: Intra-articular rhIDUA is well-tolerated and safe in the canine MPS I animal model. Qualitative and quantitative assessments indicate that IA-rhIDUA successfully reduces tissue and cellular GAG storage in synovium and articular cartilage, including cartilage deep to the articular surface, and eliminates inflammatory macrophages from synovial tissue. Clinical relevance: The MPS I canine IA-rhIDUA results suggest that clinical studies should be performed to determine if IA-rhIDUA is a viable approach to ameliorating refractory orthopedic disease in human MPS I. [ABSTRACT FROM AUTHOR]
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- 2014
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5. Novel transporters for enzyme replacement therapy.
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Tong, Wenyong, Tor, Yitzhak, and Esko, Jeffrey D.
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- 2014
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6. Glycan-based biomarkers for mucopolysaccharidoses.
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Lawrence, Roger, Brown, Jillian R., Lorey, Fred, Dickson, Patricia I., Crawford, Brett E., and Esko, Jeffrey D.
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GLYCANS , *MUCOPOLYSACCHARIDOSIS , *BIOMARKERS , *ENZYME activation , *GLYCOSAMINOGLYCANS , *HEMATOPOIETIC stem cells , *DIAGNOSIS , *PATIENTS - Abstract
Abstract: The mucopolysaccharidoses (MPS) result from attenuation or loss of enzyme activities required for lysosomal degradation of the glycosaminoglycans, hyaluronan, heparan sulfate, chondroitin/dermatan sulfate, and keratan sulfate. This review provides a summary of glycan biomarkers that have been used to characterize animal models of MPS, for diagnosis of patients, and for monitoring therapy based on hematopoietic stem cell transplantation and enzyme replacement therapy. Recent advances have focused on the non-reducing terminus of the glycosaminoglycans that accumulate as biomarkers, using a combination of enzymatic digestion with bacterial enzymes followed by quantitative liquid chromatography/mass spectrometry. These new methods provide a simple, rapid diagnostic strategy that can be applied to samples of urine, blood, cerebrospinal fluid, cultured cells and dried blood spots from newborn infants. Analysis of the non-reducing end glycans provides a method for monitoring enzyme replacement and substrate reduction therapies and serves as a discovery tool for uncovering novel biomarkers and new forms of mucopolysaccharidoses. [Copyright &y& Elsevier]
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- 2014
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7. Metabolic engineering of Chinese hamster ovary cells: Towards a bioengineered heparin
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Baik, Jong Youn, Gasimli, Leyla, Yang, Bo, Datta, Payel, Zhang, Fuming, Glass, Charles A., Esko, Jeffrey D., Linhardt, Robert J., and Sharfstein, Susan T.
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BLOOD coagulation , *HEPARIN , *BIOENGINEERING , *CHINESE medicine , *BIOPHARMACEUTICS , *CELL metabolism , *CELL growth , *GENETIC engineering , *THERAPEUTICS - Abstract
Abstract: Heparin is the most widely used pharmaceutical to control blood coagulation in modern medicine. A health crisis that took place in 2008 led to a demand for production of heparin from non-animal sources. Chinese hamster ovary (CHO) cells, commonly used mammalian host cells for production of foreign pharmaceutical proteins in the biopharmaceutical industry, are capable of producing heparan sulfate (HS), a related polysaccharide naturally. Since heparin and HS share the same biosynthetic pathway, we hypothesized that heparin could be produced in CHO cells by metabolic engineering. Based on the expression of endogenous enzymes in the HS/heparin pathways of CHO-S cells, human N-deacetylase/N-sulfotransferase (NDST2) and mouse heparan sulfate 3-O-sulfotransferase 1 (Hs3st1) genes were transfected sequentially into CHO host cells growing in suspension culture. Transfectants were screened using quantitative RT-PCR and Western blotting. Out of 120 clones expressing NDST2 and Hs3st1, 2 clones, Dual-3 and Dual-29, were selected for further analysis. An antithrombin III (ATIII) binding assay using flow cytometry, designed to recognize a key sugar structure characteristic of heparin, indicated that Hs3st1 transfection was capable of increasing ATIII binding. An anti-factor Xa assay, which affords a measure of anticoagulant activity, showed a significant increase in activity in the dual-expressing cell lines. Disaccharide analysis of the engineered HS showed a substantial increase in N-sulfo groups, but did not show a pattern consistent with pharmacological heparin, suggesting that further balancing the expression of transgenes with the expression levels of endogenous enzymes involved in HS/heparin biosynthesis might be necessary. [Copyright &y& Elsevier]
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- 2012
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8. Growth factor-dependent branching of the ureteric bud is modulated by selective 6-O sulfation of heparan sulfate
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Shah, Mita M., Sakurai, Hiroyuki, Gallegos, Thomas F., Sweeney, Derina E., Bush, Kevin T., Esko, Jeffrey D., and Nigam, Sanjay K.
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GROWTH factors , *SOMATOMEDIN , *GLYCOSAMINOGLYCANS , *PROTEOGLYCANS , *BASAL lamina , *PROTEIN binding , *LABORATORY mice , *DEVELOPMENTAL biology , *MORPHOGENESIS - Abstract
Abstract: Heparan sulfate proteoglycans (HSPGs) are found in the basement membrane and at the cell-surface where they modulate the binding and activity of a variety of growth factors and other molecules. Most of the functions of HSPGs are mediated by the variable sulfated glycosaminoglycan (GAG) chains attached to a core protein. Sulfation of the GAG chain is key as evidenced by the renal agenesis phenotype in mice deficient in the HS biosynthetic enzyme, heparan sulfate 2-O sulfotransferase (Hs2st; an enzyme which catalyzes the 2-O-sulfation of uronic acids in heparan sulfate). We have recently demonstrated that this phenotype is likely due to a defect in induction of the metanephric mesenchyme (MM), which along with the ureteric bud (UB), is responsible for the mutually inductive interactions in the developing kidney (Shah et al., 2010). Here, we sought to elucidate the role of variable HS sulfation in UB branching morphogenesis, particularly the role of 6-O sulfation. Endogenous HS was localized along the length of the UB suggesting a role in limiting growth factors and other molecules to specific regions of the UB. Treatment of cultures of whole embryonic kidney with variably desulfated heparin compounds indicated a requirement of 6O-sulfation in the growth and branching of the UB. In support of this notion, branching morphogenesis of the isolated UB was found to be more sensitive to the HS 6-O sulfation modification when compared to the 2-O sulfation modification. In addition, a variety of known UB branching morphogens (i.e., pleiotrophin, heregulin, FGF1 and GDNF) were found to have a higher affinity for 6-O sulfated heparin providing additional support for the notion that this HS modification is important for robust UB branching morphogenesis. Taken together with earlier studies, these findings suggest a general mechanism for spatio-temporal HS regulation of growth factor activity along the branching UB and in the developing MM and support the view that specific growth factor-HSPG interactions establish morphogen gradients and function as developmental switches during the stages of epithelial organogenesis (Shah et al., 2004). [Copyright &y& Elsevier]
- Published
- 2011
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9. Stage-dependent regulation of mammary ductal branching by heparan sulfate and HGF-cMet signaling
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Garner, Omai B., Bush, Kevin T., Nigam, Kabir B., Yamaguchi, Yu, Xu, Ding, Esko, Jeffrey D., and Nigam, Sanjay K.
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CELLULAR signal transduction , *HEPATOCYTE growth factor , *POLYSACCHARIDES , *MORPHOGENESIS , *CELL culture , *SULFOTRANSFERASES , *PROTEOGLYCANS , *EPITHELIAL cells - Abstract
Abstract: Specific interactions of growth factors with heparan sulfate may function as "switches" to regulate stages of branching morphogenesis in developing mammalian organs, such as breast, lung, salivary gland and kidney, but the evidence derives mostly from studies of explanted tissues or cell culture (Shah et al., 2004). We recently provided in vivo evidence that inactivation of Ndst1, the predominant N-deacetylase/N-sulfotransferase gene essential for the formation of mature heparan sulfate, results in a highly specific defect in murine lobuloalveolar development (Crawford et al., 2010). Here, we demonstrate a highly penetrant dramatic defect in primary branching by mammary epithelial-specific inactivation of Ext1, a subunit of the copolymerase complex that catalyzes the formation of the heparan sulfate chain. In contrast to Ext1 deletion, inactivation of Hs2st (which encodes an enzyme required for 2-O-sulfation of uronic acids in heparan sulfate) did not inhibit ductal formation but displayed markedly decreased secondary and ductal side-branches as well as fewer bifurcated terminal end buds. Targeted conditional deletion of c-Met, the receptor for HGF, in mammary epithelial cells showed similar defects in secondary and ductal side-branching, but did not result in any apparent defect in bifurcation of terminal end buds. Although there is published evidence indicating a role for 2-O sulfation in HGF binding, primary epithelial cells isolated from Hs2st conditional deletions were able to activate Erk in the presence of HGF and there appeared to be only a slight reduction in HGF-mediated c-Met phosphorylation in these cells compared to control. Thus, both c-Met and Hs2st play important, but partly independent, roles in secondary and ductal side-branching. When considered together with previous studies of Ndst1-deficient glands, the data presented here raise the possibility of partially-independent regulation by heparan sulfate-dependent pathways of primary ductal branching, terminal end bud bifurcation, secondary branching, ductal side-branching and lobuloalveolar formation. [Copyright &y& Elsevier]
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- 2011
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10. Heparan sulfate Ndst1 regulates vascular smooth muscle cell proliferation, vessel size and vascular remodeling
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Adhikari, Neeta, Basi, David L., Townsend, DeWayne, Rusch, Melissa, Mariash, Ami, Mullegama, Sureni, Watson, Adrienne, Larson, Jon, Tan, Sara, Lerman, Ben, Esko, Jeffrey D., Selleck, Scott B., and Hall, Jennifer L.
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VASCULAR smooth muscle , *MUSCLE cells , *SULFOTRANSFERASES , *BLOOD-vessel abnormalities , *CELL proliferation , *PROTEOGLYCANS , *DISACCHARIDES , *EXTRACELLULAR matrix - Abstract
Abstract: Heparan sulfate proteoglycans are abundant molecules in the extracellular matrix and at the cell surface. Heparan sulfate chains are composed of groups of disaccharides whose side chains are modified through a series of enzymatic reactions. Deletion of these enzymes alters heparan sulfate fine structure and leads to changes in cell proliferation and tissue development. The role of heparan sulfate modification has not been explored in the vessel wall. The goal of this study was to test the hypothesis that altering heparan sulfate fine structure would impact vascular smooth muscle cell (VSMC) proliferation, vessel structure, and remodeling in response to injury. A heparan sulfate modifying enzyme, N-deacetylase N-sulfotransferase1 (Ndst1) was deleted in smooth muscle resulting in decreased N- and 2-O sulfation of the heparan sulfate chains. Smooth muscle specific deletion of Ndst1 led to a decrease in proliferating VSMCs and the circumference of the femoral artery in neonatal and adult mice. In response to vascular injury, mice lacking Ndst1 exhibited a significant reduction in lesion formation. Taken together, these data provide new evidence that modification of heparan sulfate fine structure through deletion of Ndst1 is sufficient to decrease VSMC proliferation and alter vascular remodeling. [Copyright &y& Elsevier]
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- 2010
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11. Hs2st mediated kidney mesenchyme induction regulates early ureteric bud branching
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Shah, Mita M., Sakurai, Hiroyuki, Sweeney, Derina E., Gallegos, Thomas F., Bush, Kevin T., Esko, Jeffrey D., and Nigam, Sanjay K.
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PROTEOGLYCANS , *EPIDERMAL growth factor , *MESENCHYME , *GENETIC regulation , *DEVELOPMENTAL biology , *CELL communication , *MORPHOGENESIS - Abstract
Abstract: Heparan sulfate proteoglycans (HSPGs) are central modulators of developmental processes likely through their interaction with growth factors, such as GDNF, members of the FGF and TGFβ superfamilies, EGF receptor ligands and HGF. Absence of the biosynthetic enzyme, heparan sulfate 2-O-sulfotransferase (Hs2st) leads to kidney agenesis. Using a novel combination of in vivo and in vitro approaches, we have reanalyzed the defect in morphogenesis of the Hs2st − / − kidney. Utilizing assays that separately model distinct stages of kidney branching morphogenesis, we found that the Hs2st −/− UB is able to undergo branching and induce mesenchymal-to-epithelial transformation when recombined with control MM, and the isolated Hs2st null UB is able to undergo branching morphogenesis in the presence of exogenous soluble pro-branching growth factors when embedded in an extracellular matrix, indicating that the UB is intrinsically competent. This is in contrast to the prevailing view that the defect underlying the renal agenesis phenotype is due to a primary role for 2-O sulfated HS in UB branching. Unexpectedly, the mutant MM was also fully capable of being induced in recombination experiments with wild-type tissue. Thus, both the mutant UB and mutant MM tissue appear competent in and of themselves, but the combination of mutant tissues fails in vivo and, as we show, in organ culture. We hypothesized a 2OS-dependent defect in the mutual inductive process, which could be on either the UB or MM side, since both progenitor tissues express Hs2st. In light of these observations, we specifically examined the role of the HS 2-O sulfation modification on the morphogenetic capacity of the UB and MM individually. We demonstrate that early UB branching morphogenesis is not primarily modulated by factors that depend on the HS 2-O sulfate modification; however, factors that contribute to MM induction are markedly sensitive to the 2-O sulfation modification. These data suggest that key defect in Hs2st null kidneys is the inability of MM to undergo induction either through a failure of mutual induction or a primary failure of MM morphogenesis. This results in normal UB formation but affects either T-shaped UB formation or iterative branching of the T-shaped UB (possibly two separate stages in collecting system development dependent upon HS). We discuss the possibility that a disruption in the interaction between HS and Wnts (e.g. Wnt 9b) may be an important aspect of the observed phenotype. This appears to be the first example of a defect in the MM preventing advancement of early UB branching past the first bifurcation stage, one of the limiting steps in early kidney development. [Copyright &y& Elsevier]
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- 2010
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12. Regulation of ureteric bud branching morphogenesis by sulfated proteoglycans in the developing kidney
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Steer, Dylan L., Shah, Mita M., Bush, Kevin T., Stuart, Robert O., Sampogna, Rosemary V., Meyer, Tobias N., Schwesinger, Catherine, Bai, Xaiomei, Esko, Jeffrey D., and Nigam, Sanjay K.
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PROTEOGLYCANS , *GLYCOPROTEINS , *PROTEINS , *EMBRYOLOGY - Abstract
Glycosaminoglycans in the form of heparan sulfate proteoglycans (HSPG) and chondroitin sulfate proteoglycans (CSPG) are required for normal kidney organogenesis. The specific roles of HSPGs and CSPGs on ureteric bud (UB) branching morphogenesis are unclear, and past reports have obtained differing results. Here we employ in vitro systems, including isolated UB culture, to clarify the roles of HSPGs and CSPGs on this process. Microarray analysis revealed that many proteoglycan core proteins change during kidney development (syndecan-1,2,4, glypican-1,2,3, versican, decorin, biglycan). Moreover, syndecan-1, syndecan-4, glypican-3, and versican are differentially expressed during isolated UB culture, while decorin is dynamically regulated in cultured isolated metanephric mesenchyme (MM). Biochemical analysis indicated that while both heparan sulfate (HS) and chondroitin sulfate (CS) are present, CS accounts for approximately 75% of the glycosaminoglycans (GAG) in the embryonic kidney. Selective perturbation of HS in whole kidney rudiments and in the isolated UB resulted in a significant reduction in the number of UB branch tips, while CS perturbation has much less impressive effects on branching morphogenesis. Disruption of endogenous HS sulfation with chlorate resulted in diminished FGF2 binding and proliferation, which markedly altered kidney area but did not have a statistically significant effect on patterning of the ureteric tree. Furthermore, perturbation of GAGs did not have a detectable effect on FGFR2 expression or epithelial marker localization, suggesting the expression of these molecules is largely independent of HS function. Taken together, the data suggests that nonselective perturbation of HSPG function results in a general proliferation defect; selective perturbation of specific core proteins and/or GAG microstructure may result in branching pattern defects. Despite CS being the major GAG synthesized in the whole developing kidney, it appears to play a lesser role in UB branching; however, CS is likely to be integral to other developmental processes during nephrogenesis, possibly involving the MM. A model is presented of how, together with growth factors, heterogeneity of proteoglycan core proteins and glycosaminoglycan sulfation act as a switching mechanism to regulate different stages of the branching process. In this model, specific growth factor–HSPG combinations play key roles in the transitioning between stages and their maintenance. [Copyright &y& Elsevier]
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- 2004
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13. Prion protein post-translational modifications modulate heparan sulfate binding and limit aggregate size in prion disease.
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Callender, Julia A., Sevillano, Alejandro M., Soldau, Katrin, Kurt, Timothy D., Schumann, Taylor, Pizzo, Donald P., Altmeppen, Hermann, Glatzel, Markus, Esko, Jeffrey D., and Sigurdson, Christina J.
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POST-translational modification , *PRION diseases , *HEPARAN sulfate , *BOVINE spongiform encephalopathy , *PRIONS , *GLYCANS , *GLYCAN structure - Abstract
Many aggregation-prone proteins linked to neurodegenerative disease are post-translationally modified during their biogenesis. In vivo pathogenesis studies have suggested that the presence of post-translational modifications can shift the aggregate assembly pathway and profoundly alter the disease phenotype. In prion disease, the N-linked glycans and GPI-anchor on the prion protein (PrP) impair fibril assembly. However, the relevance of the two glycans to aggregate structure and disease progression remains unclear. Here we show that prion-infected knockin mice expressing an additional PrP glycan (tri-glycosylated PrP) develop new plaque-like deposits on neuronal cell membranes, along the subarachnoid space, and periventricularly, suggestive of high prion mobility and transit through the interstitial fluid. These plaque-like deposits were largely non-congophilic and composed of full length, uncleaved PrP, indicating retention of the glycophosphatidylinositol (GPI) anchor. Prion aggregates sedimented in low density fractions following ultracentrifugation, consistent with oligomers, and bound low levels of heparan sulfate (HS) similar to other predominantly GPI-anchored prions. Collectively, these results suggest that highly glycosylated PrP primarily converts as a GPI-anchored glycoform, with low involvement of HS co-factors, limiting PrP assembly mainly to oligomers. Since PrPC is highly glycosylated, these findings may explain the high frequency of diffuse, synaptic, and plaque-like deposits in the brain as well as the rapid conversion commonly observed in human and animal prion disease. • Knockin mice expressing tri-glycosylated PrPC develop novel plaque-like deposits upon prion infection. • Tri-glycosylated PrPSc forms mobile oligomers that accumulate perineuronally, periventricularly, and adjacent to meninges. • Tri-glycosylated PrPSc binds low levels of heparan sulfate, unlike unglycosylated PrPSc. • PrP post-translational modifications profoundly alter prion aggregate assembly pathways. [ABSTRACT FROM AUTHOR]
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- 2020
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14. Intracerebroventricular sulfamidase delivery to the brain.
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Brown, Jillian R., Hussain, Farhan A., Le, Steven Q., Dickson, Patricia I., Thacker, Bryan E., Esko, Jeffrey D., and Glass, Charles A.
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BRAIN diseases , *GLYCOSAMINOGLYCANS - Published
- 2020
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15. The mucopolysaccharidosis type IIIA murine model demonstrates increased brown adipose activity and energy demand, resulting in postprandial hypertriglyceridemia.
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Wang, Raymond Y., Gordts, Phillip L.S.M., Lamanna, William C., Sarrazin, Stéphane, Gonzales, Jon C., Kan, Shih-hsin, Tong, Wenyong, Dickson, Patricia I., and Esko, Jeffrey D.
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SANFILIPPO syndrome , *LABORATORY mice , *BROWN adipose tissue , *HYPERTRIGLYCERIDEMIA , *AUTOPHAGY , *ENERGY metabolism - Published
- 2015
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16. Diagnosis and Monitoring of Mucopolysaccharidoses Using Disease-Specific Non-Reducing End Carbohydrate Biomarkers
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Brown, Jillian R., Lawrence, Roger, Al-Mafraji, Kanar, Lamanna, William C., Beitel, James R., Boons, Geert-Jan, Esko, Jeffrey D., and Crawford, Brett E.
- Published
- 2012
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