8 results on '"Linda P. Hansen"'
Search Results
2. Upper- vs. Lower-Body Exercise Performance in Female and Male Cross-Country Skiers
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Linda Marie Hansen, Øyvind Sandbakk, Gertjan Ettema, and Julia Kathrin Baumgart
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oxygen uptake ,heart rate ,blood lactate ,running ,XC skiing ,XC skiers ,Sports ,GV557-1198.995 - Abstract
Purpose: To investigate the interaction between exercise modality (i.e., upper- and lower-body exercise) and sex in physiological responses and power output (PO) across the entire intensity spectrum (i.e., from low to maximal intensity).Methods: Ten male and 10 female cross-country (XC) skiers performed a stepwise incremental test to exhaustion consisting of 5 min stages with increasing workload employing upper-body poling (UP) and running (RUN) on two separate days. Mixed measures ANOVA were performed to investigate the interactions between exercise modalities (i.e., UP and RUN) and sex in physiological responses and PO across the entire exercise intensity spectrum.Results: The difference between UP and RUN (ΔUP−RUN), was not different in the female compared with the male XC skiers for peak oxygen uptake (18 ± 6 vs. 18 ± 6 mL·kg−1·min−1, p = 0.843) and peak PO (84 ± 18 vs. 91 ± 22 W, p = 0.207). At most given blood lactate and rating of perceived exertion values, ΔUP−RUN was larger in the male compared with the female skiers for oxygen uptake and PO, but these differences disappeared when the responses were expressed as % of the modality-specific peak.Conclusion: Modality-differences (i.e., ΔUP−RUN) in peak physiological responses and PO did not differ between the female and male XC skiers. This indicates that increased focus on upper-body strength and endurance training in female skiers in recent years may have closed the gap between upper- and lower-body endurance capacity compared with male XC skiers. In addition, no sex-related considerations need to be made when using relative physiological responses for intensity regulation within a specific exercise modality.
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- 2021
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3. Development and validation of a vitamin D status prediction model in Danish pregnant women: a study of the Danish National Birth Cohort.
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Camilla Bjørn Jensen, Andrew L Thorne-Lyman, Linda Vadgård Hansen, Marin Strøm, Nina Odgaard Nielsen, Arieh Cohen, and Sjurdur Frodi Olsen
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Medicine ,Science - Abstract
Vitamin D has been hypothesized to reduce risk of pregnancy complications such as preeclampsia, gestational diabetes mellitus, and preterm delivery. However, many of these outcomes are rare and require a large sample size to study, representing a challenge for cohorts with a limited number of preserved samples. The aims of this study were to (1) identify predictors of serum 25-hydroxy-vitamin D (25(OH)D) among pregnant women in a subsample (N = 1494) of the Danish National Birth Cohort (DNBC) and (2) develop and validate a score predicting 25(OH)D-status in order to explore associations between vitamin D and maternal and offspring health outcomes in the DNBC. In our study sample, 42.3% of the population had deficient levels of vitamin D (
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- 2013
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4. The immune system strikes back: cellular immune responses against indoleamine 2,3-dioxygenase.
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Rikke Baek Sørensen, Linda Berge-Hansen, Niels Junker, Christina Aaen Hansen, Sine Reker Hadrup, Ton N M Schumacher, Inge Marie Svane, Jürgen C Becker, Per thor Straten, and Mads Hald Andersen
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Medicine ,Science - Abstract
BackgroundThe enzyme indoleamine 2,3-dioxygenase (IDO) exerts an well established immunosuppressive function in cancer. IDO is expressed within the tumor itself as well as in antigen-presenting cells in tumor-draining lymph nodes, where it promotes the establishment of peripheral immune tolerance to tumor antigens. In the present study, we tested the notion whether IDO itself may be subject to immune responses.Methods and findingsThe presence of naturally occurring IDO-specific CD8 T cells in cancer patients was determined by MHC/peptide stainings as well as ELISPOT. Antigen specific cytotoxic T lymphocytes (CTL) from the peripheral blood of cancer patients were cloned and expanded. The functional capacity of the established CTL clones was examined by chrome release assays. The study unveiled spontaneous cytotoxic T-cell reactivity against IDO in peripheral blood as well as in the tumor microenvironment of different cancer patients. We demonstrate that these IDO reactive T cells are indeed peptide specific, cytotoxic effector cells. Hence, IDO reactive T cells are able to recognize and kill tumor cells including directly isolated AML blasts as well as IDO-expressing dendritic cells, i.e. one of the major immune suppressive cell populations.ConclusionIDO may serve as an important and widely applicable target for anti-cancer immunotherapeutic strategies. Furthermore, as emerging evidence suggests that IDO constitutes a significant counter-regulatory mechanism induced by pro-inflammatory signals, IDO-based immunotherapy holds the promise to boost anti-cancer immunotherapy in general.
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- 2009
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5. Regulation of the HNF-1 homeodomain proteins by DCoH
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Gerald R. Crabtree and Linda P. Hansen
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Transcriptional Activation ,Transcription, Genetic ,Protein Conformation ,Recombinant Fusion Proteins ,Molecular Sequence Data ,Biology ,Models, Biological ,In vivo ,Genetics ,Animals ,Humans ,Hepatocyte Nuclear Factor 1-alpha ,Hydro-Lyases ,Hepatocyte Nuclear Factor 1-beta ,Transcriptional activity ,Base Sequence ,Nuclear Proteins ,DNA ,NKX-homeodomain factor ,Cell biology ,DNA-Binding Proteins ,Hepatocyte nuclear factors ,Gene Expression Regulation ,Hepatocyte Nuclear Factor 1 ,Homeobox ,Function (biology) ,Protein Binding ,Transcription Factors ,Developmental Biology - Abstract
The pattern of expression of homeodomain proteins often exceeds their apparent domain of activity. Tissue-specific proteins that modulate the in vivo activity of homeodomain proteins have been proposed to account for this functional restriction. The first identified example of such an accessory protein is DCoH, which confers transcriptional activity to the hepatocyte nuclear factor 1 and provides a model of how other accessory factors might modulate the function of homeodomain proteins.
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- 1993
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6. Characterization of a Cofactor That Regulates Dimerization of a Mammalian Homeodomain Protein
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Arie Admon, Linda P. Hansen, Pamela B. Conley, Dirk B. Mendel, Paul A. Khavari, Gerald R. Crabtree, and Mary K. Graves
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Reticulocytes ,Transcription, Genetic ,HMG-box ,Macromolecular Substances ,Molecular Sequence Data ,Alpha (ethology) ,Biology ,digestive system ,DNA-binding protein ,Mice ,chemistry.chemical_compound ,Animals ,Humans ,Amino Acid Sequence ,Hepatocyte Nuclear Factor 1-alpha ,RNA, Messenger ,Nuclear protein ,Transcription factor ,Hydro-Lyases ,Gene Library ,Hepatocyte Nuclear Factor 1-beta ,Cell Nucleus ,Multidisciplinary ,Nuclear Proteins ,DNA-binding domain ,Rats ,DNA-Binding Proteins ,Liver ,Biochemistry ,chemistry ,Protein Biosynthesis ,Hepatocyte Nuclear Factor 1 ,embryonic structures ,Hepatocyte Nuclear Factor 1-Beta ,Rabbits ,Chromosome Deletion ,DNA ,Transcription Factors - Abstract
Dimerization among transcription factors has become a recurrent theme in the regulation of eukaryotic gene expression. Hepatocyte nuclear factor-1 alpha (HNF-1 alpha) is a homeodomain-containing protein that functions as a dimer. A dimerization cofactor of HNF-1 alpha (DCoH) was identified that displayed a restricted tissue distribution and did not bind to DNA, but, rather, selectively stabilized HNF-1 alpha dimers. The formation of a stable tetrameric DCoH-HNF-1 alpha complex, which required the dimerization domain of HNF-1 alpha, did not change the DNA binding characteristics of HNF-1 alpha, but enhanced its transcriptional activity. However, DCoH did not confer transcriptional activation to the GAL4 DNA binding domain. These results indicate that DCoH regulates formation of transcriptionally active tetrameric complexes and may contribute to the developmental specificity of the complex.
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- 1991
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7. HNF-1 alpha and HNF-1 beta (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro
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Linda P. Hansen, Gerald R. Crabtree, Mary K. Graves, Pamela B. Conley, and Dirk B. Mendel
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Molecular Sequence Data ,Biology ,digestive system ,Jurkat cells ,DNA-binding protein ,Mice ,Sequence Homology, Nucleic Acid ,Genetics ,Animals ,Amino Acid Sequence ,Hepatocyte Nuclear Factor 1-alpha ,Cloning, Molecular ,Gene ,Transcription factor ,Peptide sequence ,Hepatocyte Nuclear Factor 1-beta ,Regulation of gene expression ,Base Sequence ,Nuclear Proteins ,DNA ,Transfection ,Molecular biology ,Rats ,DNA-Binding Proteins ,Gene Expression Regulation ,Liver ,Organ Specificity ,Hepatocyte Nuclear Factor 1 ,embryonic structures ,Hepatocyte Nuclear Factor 1-Beta ,Transcription Factors ,Developmental Biology - Abstract
HNF-1 alpha (previously referred to as HNF-1, LPB1, and APF) is a vertebrate transcription factor that contains a divergent homeo domain and plays a prominent role in regulating genes that have the common characteristic of being expressed in hepatocytes and a complex group of endodermally and mesodermally derived tissues. HNF-1 alpha is unique among the vertebrate homeo domain-containing proteins in that it dimerizes in the absence of its DNA recognition sequence, suggesting the possibility that the function of HNF-1 alpha may be diversified by forming heterodimers with other related proteins. We report the initial characterization of HNF-1 beta, which is closely related to HNF-1 alpha and is able to form heterodimers with HNF-1 alpha in vitro. Although HNF-1 alpha, but not HNF-1 beta, is expressed in the liver, HNF-1 alpha and HNF-1 beta are coexpressed in the murine Hepa1A cell line and in the mammalian kidney where a subset of hepatocyte genes are expressed. In contrast, exclusive expression of HNF-1 beta is associated with repression of a subset of hepatocyte-specific genes in the dedifferentiated hepatocyte cell line C2, differentiated F9 cells, in somatic hybrids between hepatocytes and fibroblasts, and in the lung. The extent of heterodimerization may be regulated in a tissue-specific way because freely exchangeable heterodimers are formed in Jurkat T cells transfected with HNF-1 alpha and HNF-1 beta, whereas in liver cells stable homodimers are present. These studies define a pair of homeo domain proteins that have the potential to interact to produce an embryologically complex pattern of gene expression.
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- 1991
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8. Independent regulation of HNF-1 alpha and HNF-1 beta by retinoic acid in F9 teratocarcinoma cells
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Dirk B. Mendel, Gerald R. Crabtree, Linda P. Hansen, and Calvin J. Kuo
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Embryonal Carcinoma Stem Cells ,Transcription, Genetic ,Molecular Sequence Data ,Retinoic acid ,Biology ,DNA-binding protein ,digestive system ,General Biochemistry, Genetics and Molecular Biology ,Embryonal carcinoma ,chemistry.chemical_compound ,medicine ,Tumor Cells, Cultured ,Animals ,RNA, Messenger ,Promoter Regions, Genetic ,Molecular Biology ,Transcription factor ,Hepatocyte Nuclear Factor 1-beta ,Regulation of gene expression ,General Immunology and Microbiology ,Base Sequence ,General Neuroscience ,Nuclear Proteins ,Promoter ,DNA ,medicine.disease ,Molecular biology ,DNA Fingerprinting ,DNA-Binding Proteins ,chemistry ,Gene Expression Regulation ,Retinoic acid receptor alpha ,embryonic structures ,Hepatocyte Nuclear Factor 1 ,Hepatocyte Nuclear Factor 1-Beta ,Neoplastic Stem Cells ,Transcription Factors ,Research Article - Abstract
Hepatocyte Nuclear Factor-1 alpha (HNF-1 alpha) and HNF-1 beta are homeodomain-containing transcription factors which interact with the GTTAATNATTAAC motif essential to the function of more than 15 promoters selectively expressed in the liver. These homeoproteins can form homo- and heterodimers in solution and share identical DNA-binding domains but have different transcriptional activation properties. During retinoic acid (RA) induced differentiation of F9 embryonal carcinoma (EC) cells, which stimulates aspects of pre-implantation embryogenesis, both HNF-1 beta mRNA and immunoreactive DNA-binding activity are strongly induced approximately 24 h post RA-treatment. In contrast, HNF-1 alpha mRNA increases approximately 4-fold after 5 days, concomitant with elevation of HNF-1 alpha DNA-binding activity and expression of the HNF-1 target gene alpha-fetoprotein. These results indicate that HNF-1 alpha and -1 beta expression can be controlled by regulatory hierarchies downstream of primary RA-response genes, and suggest that independent regulatory mechanisms for these factors can confer distinct and interactive developmental functions.
- Published
- 1991
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