Relevant bibliographies by topics / Protein hormone

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Protein hormone'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Protein hormone"

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Niessen, René W. L. M., Birgit A. Pfaffendorf, Augueste Sturk, Roy J. Lamping, Marianne C. L. Schaap, C. Erik Hack, and Marjolein Peters. "The Influence of Insulin, ß-Estradiol, Dexamethasone and Thyroid Hormone on the Secretion of Coagulant and Anticoagulant Proteins by HepG2 Cells." Thrombosis and Haemostasis 74, no. 02 (1995): 686–92. http://dx.doi.org/10.1055/s-0038-1649798.

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SummaryAs a basis for regulatory studies on the influence of hormones on (anti)coagulant protein production by hepatocytes, we examined the amounts of the plasma proteins antithrombin III (AT III), protein C, protein S, factor II, factor X, fibrinogen, and prealbumin produced by the hepatoma cell line HepG2, into the culture medium, in the absence and presence of insulin, β-estradiol, dexamethasone and thyroid hormone. Without hormones these cells produced large amounts of fibrinogen (2,452 ± 501 ng/mg cell protein), AT III (447 ± 16 ng/mg cell protein) and factor II (464 ± 31 ng/mg cell protein) and only small amounts of protein C (50 ± 7 ng/mg cell protein) and factor X (55 ± 5 ng/mg cell protein). Thyroid hormone had a slight but significant effect on the enrichment in the culture medium of the anticoagulant protein AT III (1.34-fold) but not on protein C (0.96-fold) and protein S (0.91-fold). This hormone also significantly increased the amounts of the coagulant proteins factor II (1.28-fold), factor X (1.45-fold) and fibrinogen (2.17-fold). Insulin had an overall stimulating effect on the amounts of all the proteins that were investigated. Neither dexamethasone nor ß-estradiol administration did substantially change the amounts of these proteins.We conclude that the HepG2 cell is a useful tool to study the hormonal regulation of the production of (anti)coagulant proteins. We studied the overall process of protein production, i.e., the amounts of proteins produced into the culture medium. Detailed studies have to be performed to establish the specific hormonal effects on the underlying processes, e.g., transcription, translation, cellular processing and transport, and secretion.
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Richardson, Samantha J., Julie A. Monk, Caroline A. Shepherdley, Lars O. E. Ebbesson, Frank Sin, Deborah M. Power, Peter B. Frappell, Josef Köhrle, and Marilyn B. Renfree. "Developmentally regulated thyroid hormone distributor proteins in marsupials, a reptile, and fish." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 288, no. 5 (May 2005): R1264—R1272. http://dx.doi.org/10.1152/ajpregu.00793.2004.

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Thyroid hormones are essential for vertebrate development. There is a characteristic rise in thyroid hormone levels in blood during critical periods of thyroid hormone-regulated development. Thyroid hormones are lipophilic compounds, which readily partition from an aqueous environment into a lipid environment. Thyroid hormone distributor proteins are required to ensure adequate distribution of thyroid hormones, throughout the aqueous environment of the blood, and to counteract the avid partitioning of thyroid hormones into the lipid environment of cell membranes. In human blood, these proteins are albumin, transthyretin and thyroxine-binding globulin. We analyzed the developmental profile of thyroid hormone distributor proteins in serum from a representative of each order of marsupials ( M. eugenii; S.crassicaudata), a reptile ( C. porosus), in two species of salmonoid fishes ( S. salar; O. tshawytsch), and throughout a calendar year for sea bream ( S. aurata). We demonstrated that during development, these animals have a thyroid hormone distributor protein present in their blood which is not present in the adult blood. At least in mammals, this additional protein has higher affinity for thyroid hormones than the thyroid hormone distributor proteins in the blood of the adult. In fish, reptile and polyprotodont marsupial, this protein was transthyretin. In a diprotodont marsupial, it was thyroxine-binding globulin. We propose an hypothesis that an augmented thyroid hormone distributor protein network contributes to the rise in total thyroid hormone levels in the blood during development.
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De Feo, Pierpaolo. "Hormonal regulation of human protein metabolism." European Journal of Endocrinology 135, no. 1 (July 1996): 7–18. http://dx.doi.org/10.1530/eje.0.1350007.

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De Feo P. Hormonal regulation of human protein metabolism. Eur J Endocrinol 1996:135:7–18. ISSN 0804–4643 This review focuses on the effects of hormones on protein kinetics in humans. Most of the recent knowledge on the regulation of protein metabolism in humans has been obtained by tracing protein kinetics in vivo, using labelled isotopes of essential or non-essential amino acids. This technique allows the rates of the whole-body protein synthesis and breakdown to be estimated together with amino acid oxidation and the fractional synthetic rates of mixed muscle proteins or of single plasma proteins. Changes induced within these parameters by hormonal administration or endocrine diseases are also discussed. Hormones, on the basis of their net effect on protein balance (protein synthesis minus protein breakdown), are divided into two categories: those provided with an anabolic action and those with a prevalent catabolic action. The effects on protein metabolism of the following hormones are reviewed: insulin, growth hormone, IGF-I, adrenaline, androgens, estrogens, progesterone, glucagon, glucocorticosteroids, thyroid hormones. The review concludes with a report on the effects of multiple hormonal infusions on whole-body protein kinetics and a discussion on the potential role played by the concomitant increase of several hormones in the pathogenesis of protein wasting that complicates stress diseases. Pierpaolo De Feo, DIMISEM, Via E. Dal Pozzo, 06126 Perugia, Italy
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Engels, J. W., J. Glauder, H. Müllner, D. Tripier, E. Uhlmann, and W. Wetekam. "Enzymatic amidation of recombinant (Leu27) growth hormone releasing hormone-Gly45." "Protein Engineering, Design and Selection" 1, no. 3 (1987): 195–99. http://dx.doi.org/10.1093/protein/1.3.195.

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Campbell, Kenneth L., Nurit Haspel, Cassandra Gath, Nuzulul Kurniatash, Indira (Nouduri) Akkiraju, Naomi Stuffers, and Uma Vadher. "Protein hormone fragmentation in intercellular signaling: hormones as nested information systems." Biology of Reproduction 104, no. 4 (January 5, 2021): 887–901. http://dx.doi.org/10.1093/biolre/ioaa234.

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Abstract This study explores the hypothesis that protein hormones are nested information systems in which initial products of gene transcription, and their subsequent protein fragments, before and after secretion and initial target cell action, play additional physiological regulatory roles. The study produced four tools and key results: (1) a problem approach that proceeds, with examples and suggestions for in vivo organismal functional tests for peptide–protein interactions, from proteolytic breakdown prediction to models of hormone fragment modulation of protein–protein binding motifs in unrelated proteins; (2) a catalog of 461 known soluble human protein hormones and their predicted fragmentation patterns; (3) an analysis of the predicted proteolytic patterns of the canonical protein hormone transcripts demonstrating near-universal persistence of 9 ± 7 peptides of 8 ± 8 amino acids even after cleavage with 24 proteases from four protease classes; and (4) a coincidence analysis of the predicted proteolysis locations and the 1939 exon junctions within the transcripts that shows an excess (P < 0.001) of predicted proteolysis within 10 residues, especially at the exonal junction (P < 0.01). It appears all protein hormone transcripts generate multiple fragments the size of peptide hormones or protein–protein binding domains that may alter intracellular or extracellular functions by acting as modulators of metabolic enzymes, transduction factors, protein binding proteins, or hormone receptors. High proteolytic frequency at exonal junctions suggests proteolysis has evolved, as a complement to gene exon fusion, to extract structures or functions within single exons or protein segments to simplify the genome by discarding archaic one-exon genes.
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Pradhananga, Sarbendra, and Jon R. Sayers. "Natural synthesis: Biologics, biosimilars and biobetters in protein hormone therapy." Biochemist 34, no. 1 (February 1, 2012): 10–15. http://dx.doi.org/10.1042/bio03401010.

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Hormone therapies have been used since the early 20th Century and belong to a group of drugs that has recently become known as ‘biologics’. Biologics are medicinal products that have been produced by biological processes as opposed to chemically synthesized drugs. The term biologics spans a wide range of products that include therapeutics such as organs, tissue, cells, blood or blood components, vaccines and proteins. This ‘proteins’ subgroup can be further subdivided into therapeutics such as antibodies, enzymes and hormones. The first hormone therapeutics were extracted from human or animal sources; however, with the advent and development of cloning and protein production technologies from the late-20th Century onwards, protein hormone therapeutics are now produced by recombinant DNA technology.
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Fetissov, Sergueï O., Romain Legrand, and Nicolas Lucas. "Bacterial Protein Mimetic of Peptide Hormone as a New Class of Protein- based Drugs." Current Medicinal Chemistry 26, no. 3 (March 26, 2019): 546–53. http://dx.doi.org/10.2174/0929867324666171005110620.

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Specific peptide molecules classified as hormones, neuropeptides and cytokines are involved in intercellular signaling regulating various physiological processes in all organs and tissues. This justifies the peptidergic signaling as an attractive pharmacological target. Recently, a protein mimetic of a peptide hormone has been identified in Escherichia coli suggesting the potential use of specific bacterial proteins as a new type of peptide-like drugs. We review the scientific rational and technological approaches leading to the identification of the E. coli caseinolytic protease B (ClpB) homologue protein as a conformational mimetic of α-melanocyte-stimulating hormone (α-MSH), a melanocortin peptide critically involved in the regulation of energy homeostasis in humans and animals. Theoretical and experimental backgrounds for the validation of bacterial ClpB as a potential drug are discussed based on the known E. coli ClpB amino acid sequence homology with α-MSH. Using in silico analysis, we show that other protein sources containing similar to E. coli ClpB α-MSH-like epitopes with potential biological activity may exist in Enterobacteriaceae and in some Brassicaceae. Thus, the original approach leading to the identification of E. coli ClpB as an α-MSH mimetic protein can be applied for the identification of mimetic proteins of other peptide hormones and development of a new type of peptide-like protein-based drugs.
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Clapp, Carmen, Stéphanie Thebault, Michael C. Jeziorski, and Gonzalo Martínez De La Escalera. "Peptide Hormone Regulation of Angiogenesis." Physiological Reviews 89, no. 4 (October 2009): 1177–215. http://dx.doi.org/10.1152/physrev.00024.2009.

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It is now apparent that regulation of blood vessel growth contributes to the classical actions of hormones on development, growth, and reproduction. Endothelial cells are ideally positioned to respond to hormones, which act in concert with locally produced chemical mediators to regulate their growth, motility, function, and survival. Hormones affect angiogenesis either directly through actions on endothelial cells or indirectly by regulating proangiogenic factors like vascular endothelial growth factor. Importantly, the local microenvironment of endothelial cells can determine the outcome of hormone action on angiogenesis. Members of the growth hormone/prolactin/placental lactogen, the renin-angiotensin, and the kallikrein-kinin systems that exert stimulatory effects on angiogenesis can acquire antiangiogenic properties after undergoing proteolytic cleavage. In view of the opposing effects of hormonal fragments and precursor molecules, the regulation of the proteases responsible for specific protein cleavage represents an efficient mechanism for balancing angiogenesis. This review presents an overview of the actions on angiogenesis of the above-mentioned peptide hormonal families and addresses how specific proteolysis alters the final outcome of these actions in the context of health and disease.
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Toth, Michael J., Cynthia K. Sites, Dwight E. Matthews, and Peter R. Casson. "Ovarian suppression with gonadotropin-releasing hormone agonist reduces whole body protein turnover in women." American Journal of Physiology-Endocrinology and Metabolism 291, no. 3 (September 2006): E483—E490. http://dx.doi.org/10.1152/ajpendo.00600.2005.

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The age-related decline in fat-free mass is accelerated in women after menopause. The role of ovarian hormone deficiency in the regulation of fat-free mass, however, has not been clearly defined. To address this question, we examined the effect of ovarian hormone suppression on whole body protein metabolism. Whole body protein breakdown, oxidation, and synthesis were measured using [13C]leucine in young, healthy women with regular menstrual patterns before and after 2 mo of treatment with gonadotropin-releasing hormone agonist (GnRHa; n = 6) or placebo ( n = 7). Protein metabolism was measured under postabsorptive and euglycemic-hyperinsulinemic-hyperaminoacidemic conditions. Ovarian suppression did not alter whole body or regional fat-free mass or adiposity. In the postabsorptive state, GnRHa administration was associated with reductions in protein breakdown and synthesis ( P < 0.05), whereas no change in protein oxidation was noted. Under euglycemic-hyperinsulinemic-hyperaminoacidemic conditions, a similar reduction ( P < 0.05) in protein synthesis and breakdown was noted, whereas, protein oxidation increased ( P < 0.05) in the placebo group. Testosterone, steroid hormone precursors, insulin-like growth factor I, and their respective binding proteins were not altered by GnRHa administration, and changes in these hormones over time were not associated with GnRHa-induced alterations in protein metabolism, suggesting that changes in protein turnover are not due to an effect of ovarian suppression on other endocrine systems. Our findings provide evidence that endogenous ovarian hormones participate in the regulation of protein turnover in women.
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Moseley, Jane M., Matthew T. Gillespie, and Mark A. Thiede. "Parathyroid Hormone-Related Protein." Critical Reviews in Clinical Laboratory Sciences 32, no. 3 (January 1995): 299–343. http://dx.doi.org/10.3109/10408369509084687.

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Dissertations / Theses on the topic "Protein hormone"

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Stevens, Jeffrey David. "LHRH fusion protein vaccines in beef heifers and bovine ectopic ovarian xenografting." Online access for everyone, 2004. http://www.dissertations.wsu.edu/Dissertations/Fall2004/J%5FStevens%5F092204.pdf.

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Deb, Joyita. "Protein-hormone interactions patterning the gynoecium." Thesis, University of East Anglia, 2015. https://ueaeprints.uea.ac.uk/54301/.

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The gynoecium is among the most intricately patterned organs of the plant, comprisingdifferent tissue sub-structures, all with the purpose of facilitating propagation to the next generation. It is therefore representative of the complexity involved in the initiation and establishment of organ patterning and presents a unique model to study the mechanisms coordinating development. As with all other organs, the interplay between genetic and hormonal factors specifies carpel development. However, although much is known about the genetic components involved in carpel development, our understanding of hormonal regulation and the cross-talk between these two pathways is limited. Thus, the aim of this thesis has been to address this issue by obtaining an integrated view of the genetic and hormonal regulatory mechanisms which act to coordinate gynoecium development. It has done so using broadly two approaches: first, by characterising the transcription factor interactions which pattern the carpel, and second, by elucidating the cross-talk between these interactions and the plant hormone auxin. Further, it has also studied the role of auxin in carpel morphogenesis. Observations from this research have uncovered a novel auxin co-receptor complex formed by the transcription factors IND and ETT. The co-receptor binds the IAA molecule directly and exhibits specificity for IAA over the synthetic analogues NAA and 2,4-D. This coreceptor functions to coordinate the development of the style and stigmatic tissues of the carpel, possibly via the regulation of PID kinase. Further, this work has also identified novel roles in protein-protein dimerisation for the domains involved in this interaction. Analyses also indicate that this novel auxin signalling pathway may also be conserved in the Brassicaceae through the ETT orthologues in this family. Finally, this project has analysed how ETT’s role as an auxin receptor could be translated into precise spatiotemporal regulation of its target genes to specify the boundaries necessary for gynoecium patterning. Together, the results from this work have posed new questions as to the signalling mechanisms through which auxin coordinates its varied and numerous functions in plants.
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Wood, Steven Leslie. "The protein phosphatases acting on hormone-sensitive lipase." Thesis, University of Newcastle Upon Tyne, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282920.

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Moss, Catherine Elizabeth. "G-protein coupled receptors modulating incretin hormone secretion." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648611.

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Smith, Gabriele Mary. "Structural and functional characterisation of hormone-sensitive lipase." Thesis, University of Newcastle Upon Tyne, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.357089.

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Ng, Kwong-man. "Sex hormone-binding globulin protein-protein interactions and identification of a novel isoform /." Click to view the E-thesis via HKUTO, 2006. http://sunzi.lib.hku.hk/hkuto/record/B37640677.

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Sim, Pauline J. "Activation of mitogen-activated protein (MAP) kinase by the luteinising hormone-releasing hormone (LHRH) receptor." Thesis, University of Edinburgh, 1996. http://hdl.handle.net/1842/21530.

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The ability of the luteinising hormone-releasing hormone (LHRH) receptor to activate multiple signal transduction pathways (additional to its conventional activation of phospholipase C, PLC) was investigated. In particular the potential activation of the mitogen-activated protein (MAP) kinases was explored using an in vitro kinase activity assay, establishing that LHRH induces a marked and sustained increase in MAP kinase activity. Experiments with the Ca2+ ionophore, ionomycin and the phorbol ester, phorbol 12, 13-dibutyrate (PDBu) were performed to assess whether the consequences of phosphoinositide hydrolysis evoked by the LHRH receptor such as Ca2+ mobilisation or PCK activation could mimic the LHRH-induced activation. This effect could be partially mimicked by PDBu, but not by ionomycin. The role of PKC in LHRH-induced MAP kinase activation was further examined. The PKC inhibitors GF109203X, rRo-31 8220 and H7 or the downregulation of phorbol ester-sensitive PKC isoforms prevented the LHRH- and PDBu-induced responses. The LHRH- induced response was relatively resistant to H7, consistent with the possibility that the LHRH receptor may differentially activate one or more PKC species in gonadotrophs. The LHRH-induced response was additionally prevented by the tyrosine kinase inhibitors genistein and MDC or was partially mimicked by the tyrosine phosphatase inhibitor pervanadate. In order to confirm these results with an independent technique, the phosphorylation-induced gel mobility shift in immunoreactive p42 and p44 MAP kinases was determined. Both p42 and (to a lesser extent) p44 species displayed a reduced electrophoretic mobility after a 10-60 min stimulation with LHRH in a concentration-dependent manner. Pertussis toxin (PTx) also prevented the majority of the LHRH-induced MAP kinase activation (or gel mobility shift), providing the first indication of Gαi/o -mediated signal transduction by the LHRH-receptor. Mastoparan (which activates Gαi/o proteins) partially mimicked the effect of LHRH in a manner which was also sensitive to PTx.
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Ng, Kwong-man, and 吳廣文. "Sex hormone-binding globulin: protein-proteininteractions and identification of a novel isoform." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2006. http://hub.hku.hk/bib/B37640677.

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Dhananjayan, Sarath Chandran. "Receptor Selective Coactivators: Characterization of a Novel Protein-Protein Interaction Module in Steroid Hormone Receptor Signaling." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_dissertations/67.

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WW-domain binding protein-2 (WBP-2) was cloned as an E6-associated protein (E6-AP) interacting protein and its role in steroid hormone receptor (SHR) function was investigated. We show that WBP-2 differs from other SHR coactivators, as it specifically enhanced the transactivation functions of progesterone receptor (PR) and estrogen receptor (ER alpha), whereas it had no significant effect on the androgen receptor, glucocorticoid receptor or the activation functions of p53 or VP-16. We also demonstrated that, like other well characterized coactivators, WBP-2 contains an intrinsic activation domain. Depletion of endogenous WBP-2 with small interfering RNAs indicated that normal physiological protein level of WBP-2 was required for the proper functioning of ER alpha and PR. Moreover, chromatin immunoprecipitation (ChIP) assays demonstrate the hormone-dependent recruitment of WBP-2 onto an estrogen-responsive promoter. As we initially identified WBP-2 as an E6-AP interacting protein, we investigated whether WBP-2 and E6-AP function in concert. Our data shows that WBP-2 and E6-AP each enhance PR function and when co-expressed they additively enhance the transactivation functions of PR. However, WBP-2 was also able to enhance the transactivation functions of ER alpha and PR in mouse embryonic fibroblast cells generated from E6-AP knockout mice lines, suggesting that the coactivation functions of WBP-2 was not dependent on E6-AP. The further elucidate the molecular mechanism of action of WBP-2; we dissected the functional importance of the polyproline (PY) motifs contained within the WBP-2 protein. Mutational analysis suggests that one of three PY motifs, PY3 of WBP-2 was essential for its coactivation and intrinsic activation functions. In this study, we also demonstrate that the WBP-2 binding protein, Yes-kinase associated protein 1 (YAP1) acts as a secondary coactivator of ER alpha and PR. However, the coactivation function of YAP1 is revealed only in the presence of wild-type WBP-2 and not with the PY motif 3 mutant WBP-2. This is consistent with our observations that, unlike the wild-type WBP-2, the PY motif 3 mutant WBP-2 does not interact with YAP1. Our quantitative reChIP assays demonstrates an estrogen-dependent recruitment and association of ER alpha with both WBP-2 and YAP1. The hormone-dependent recruitment of YAP1 to ER alpha responsive promoter is dependent on the physiological expression levels of WBP-2. This is consistent with, our observation that the coactivation functions of YAP1 is dependent on WBP-2, and is also in agreement with other known secondary coactivators that get recruited to SHR responsive promoter via their interaction with primary coactivators. Surprisingly, the association of WBP-2 with ER alpha and its recruitment to the ER alpha target promoter was abrogated by YAP1 knock-down, suggesting that WBP-2 and YAP1 may stabilize each other at the promoter, and consequently, are functionally interdependent. Taken together our data establish the role of WBP-2 and YAP1 as selective coactivators for ER alpha and PR transactivation pathways.
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Cziko, Paul. "Molecular Physiological Evolution: Steroid Hormone Receptors and Antifreeze Proteins." Thesis, University of Oregon, 2015. http://hdl.handle.net/1794/18733.

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For my dissertation research I explored the diversity and functional evolution of steroid hormone receptors (SRs) in animals and the physiological implications of the evolution of antifreeze proteins in Antarctic notothenioid fishes. For the former, I discovered multiple new SRs from the vast and under-sampled swath of animal diversity known as invertebrates. I used the sequences of these and other newly discovered related receptors in combination with genomic data and molecular phylogenetic techniques to revise the understanding of the evolutionary history of this important gene family. While previous studies have suggested that vertebrate SR diversity arose from a gene duplication in an ancestor of all bilaterian animals, my work presents strong evidence that this duplication occurred much later, at the base of the chordates. Furthermore, to determine the implications of added diversity and a revised phylogeny on inferences of the functional evolution of SRs, I functionally characterized heretofore-unknown SRs from hemichordates, an acoelomate flatworm, and a chaetognath and statistically reconstructed and functionally characterized ancestral SRs. My results expand the known sequence and functional repertoire of SRs in animals while reinforcing the previous inference that all SRs evolved from an estrogen-sensitive ancestral receptor. I also explored the consequences of the evolution of antifreeze proteins in Antarctic notothenioid fishes, a crucial adaptation to their icy, polar environment. These special proteins adsorb to ice crystals that enter a fish's body and prevent further growth, thereby averting death. I discovered that, in addition to their lifesaving growth-inhibiting ability, AFPs also prevent the melting of internal ice crystals at temperatures above the expected equilibrium melting point. Together with a decade-long temperature record of one of the coldest fish habitats on earth, my experimental results show that the evolution and expression of antifreeze proteins is accompanied by a potentially detrimental consequence: the lifelong accumulation of ice inside these fishes' bodies. This dissertation includes previously published co-authored material as well as unpublished co-authored material.
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Books on the topic "Protein hormone"

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Rotheim, Philip. Bioengineered protein drugs: Antibodies, blood proteins. Norwalk, CT: Business Communications Co., 1995.

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Edwards, Robert Charles. Parathyroid hormone-related protein (PTHrP) in breast tissue. Birmingham: University of Birmingham, 1993.

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Bowden, Sarah Jane. Studies on the pathophysiology of parathyroid hormone-related protein. Birmingham: University of Birmingham, 1994.

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Rotheim, Philip. Bioengineered protein drugs: Enzymes. Norwalk, CT: Business Communications Co., 1995.

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Li, Xin. Growth factor-like activity and oncogene regulation of parathyroid hormone-related protein. Ottawa: National Library of Canada, 1993.

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Rotheim, Philip. Bioengineered protein drugs: Cytokines/growth factors, peptide hormones. Norwalk, CT: Business Communications Co., 1995.

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Whitfield, James F. The parathyroid hormone: An unexpected bone builder for treating osteoporosis. Austin: R.G. Landes, 1998.

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Kong, Adrienne. An investigation of actin transcript and protein levels during steroid hormone-induced branching in Achlya ambisexualis. Ottawa: National Library of Canada, 2000.

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Dunne, Fidelma Patricia Maria. Parathyroid hormone-related protein (PTHrP) gene expression in malignant tumours and in early human fetal development. Birmingham: University of Birmingham, 1994.

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Wolfgang, König. Peptide and protein hormones: Structure, regulation, activity :a reference manual. Weinheim: VCH, 1993.

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Book chapters on the topic "Protein hormone"

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Goffin, Vincent, and Paul A. Kelly. "Protein Phosphorylation and Protein-Protein Interactions." In Hormone Signaling, 3–19. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-3600-7_1.

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Shetzline, Michael A., and Marc G. Caron. "G Proteins and G Protein-Coupled Receptors." In Hormone Signaling, 181–97. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-3600-7_9.

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Nussdorfer, Gastone G., and Gian Paolo Rossi. "Endothelin G Protein-Coupled Receptors." In Hormone Signaling, 221–37. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4757-3600-7_11.

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Rivier, J., S. Koerber, J. Porter, C. Rivier, C. Hoeger, S. Struthers, M. Perrin, et al. "Characterization of Gonadotropin Hormone-Releasing Hormone Analogs." In Methods in Protein Sequence Analysis, 329–36. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73834-0_44.

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Wysolmerski, John J. "Parathyroid Hormone-Related Protein." In Primer on the Metabolic Bone Diseases and Disorders of Mineral Metabolism, 215–23. Ames, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118453926.ch27.

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Dittmer, Juergen. "Parathyroid Hormone-Related Protein." In Encyclopedia of Cancer, 2785–88. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_4389.

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Ratcliffe, W. A., and J. G. Ratcliffe. "Parathyroid Hormone-Related Protein." In Calcium Regulating Hormones, Vitamin D Metabolites, and Cyclic AMP Assays and Their Clinical Application, 213–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-662-00406-7_16.

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Dittmer, Jürgen. "Parathyroid Hormone-Related Protein." In Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_4389-2.

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Dittmer, Jürgen. "Parathyroid Hormone-Related Protein." In Encyclopedia of Cancer, 3435–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_4389.

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Russell-Jones, D. L., and A. M. Umpleby. "The Effects of Growth Hormone on Glucose & Protein Metabolism." In Growth Hormone, 163–72. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5163-8_11.

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Conference papers on the topic "Protein hormone"

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Ohlsson, M., A. J. W. Hsueh, and T. Ny. "HORMONE REGULATION OF THE FIBRINOLYTIC SYSTEM IN THE OVARY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644389.

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In the ovary, the release of oocytes from graafian follicles during hormone-induced ovulation has been found to be associated with substantial increases in follicular plasminogen activator (PA) activity. Most of the PA activity comes from the granulosa cells that have been shown to produce tPA, uPA as well as the type-1 PA-inhibitor,(PAI-1).We have studied the molecular mechanism of follicle stimulating hormone (FSH) and gonadotropin releasing hormone (GnRH) on the synthesis of tPA in primary cultures of rat granulosa cells. FSH and GnRH were both found to induce tPA in granulosa cells in a time and dose dependent manner. The effect of FSH and GnRH on the levels of tPA mRNA was also studied by northern and slot blot hybridizations. FSH and GnRH were both found to increase the level of tPA mRNA. The stimulation was up to 18 -fold compared to untreated cells.The induction of tPA mRNA by FSH and GnRH was additive and the time courses of the stimulation by the hormones differed, suggesting that different cellular mechanisms are involved. Consistent with the ability of FSH to activate the cAMP dependent protein kinase A pathway, the phosphodiesterase inhibitor 1-methyl-3-isobutylxanthine further enhanced the FSH induction of tPA mRNA.GnRH is known to activate the phospholipid-dependent protein kinase C pathway. Likewise the effect of GnRH can be mimicked by the kinase C activator, phorbol myristate acetate.It is concluded that FSH and GnRH regulates tPA production by differnt molecular mechanisms, and that the increase in tPA activity is mediated via an increase in the levels tPA mRNA. Since both gonadotropins and GnRH cause ovulation in hyposectomized animals, similar stimulatory actions of these hormones on the tPA activity suggest a correlative relationship between this enzyme and the ovulatory process.
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Montgrain, Philippe R., Rick Quintana, Leonard J. Deftos, and Randolph H. Hastings. "Akt Regulates Parathyroid Hormone-Related Protein Expression In Lung Cancer." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2066.

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Quintana, R., D. Arenberg, PR Montgrain, S. Carskadon, LJ Deftos, and RH Hastings. "Parathyroid Hormone-Related Protein Expression in NSCLC Predicts Improved Survival." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a2678.

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Wang, Di. "G-protein-coupled receptor controls steroid hormone signaling in cell membrane." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.107278.

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Fernández-Fígares, I., M. Lachica, I. Seiquer, L. Lara, A. Haro, and R. Nieto. "Effect of immunocastration and dietary protein on plasma metabolites and hormone concentrations of Iberian pigs." In 6th EAAP International Symposium on Energy and Protein Metabolism and Nutrition. The Netherlands: Wageningen Academic Publishers, 2019. http://dx.doi.org/10.3920/978-90-8686-891-9_109.

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Choi, Hee Jun, Hong Won Lee, Sangmin Kim, Tae-Young Yoon, Hyunwoo Kim, Seul Lee, Seok Jin Nam, et al. "Abstract P4-10-26: Protein-protein interaction of HER2 predicts the prognosis of hormone receptor-positive HER2-negative breast cancer." In Abstracts: 2019 San Antonio Breast Cancer Symposium; December 10-14, 2019; San Antonio, Texas. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.sabcs19-p4-10-26.

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Hastings, Randolph H., Ryan Vander Werff, Philippe R. Montgrain, and Rick Quintana. "Parathyroid Hormone-Related Protein (PTHrP) Inhibits Lung Cancer Proliferation Through The Classic PTHrP Receptor." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5080.

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Hastings, RH, R. Quintana, E. Healy, LJ Deftos, Y. Rascon, and PR Montgrain. "Cell Cycle Actions of Parathyroid Hormone-Related Protein in Non-Small Cell Lung Carcinoma." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5010.

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Melissari, E., M. F. Scully, C. Parker, R. Hedges, and V. V. Kakkar. "PLASMA FREE PROTEIN S AND OESTROGEN ADMINISTRATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644295.

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It has been shown that protein S has a cofactor role for the anticoagulant and fibrinolytic activity of activated protein C (APC) and that the free protein S fraction is the main cofactor for the APC. Here we report free protein S levels from three groups of women on oral oestrogen. Group A: Five post menopausal women (36-48 years), on oestradiol valerate (as hormone replacement therapy after hysterectomy-oophorectomy) mean free protein S was 62.8% ( 2SD below normal adult mean). Group B: Seven young women (20-25 years) on the contraceptive pill. Two had normal levels of free protein S (100% and 125%), whereas the other five were 30%, 29%, 50%, 60% and 64% of normal. Group C: Two young women. The first, a 25 year old, insulin-dependent diabetic woman developed severe thromboembolic disease shortly after initiation of oral contraception. The second, a 21 year old woman with congenital, moderately decreased plasminogen (PLG) (activity and antigen 45% of normal), had a severe ileofemoral deep venous thrombosis about 8 months after initiation of oral contraceptive (her free protein S levels were twice found to be 60% of normal). In both cases, family members with reduced levels of PK and PLG respectively were free from any thromboembolic disease and had normal protein S levels. Since an association between oral contraceptive use and incidence of venous thromboembolism without predisposition has been consistently observed in case-control and cohort Studies, we conclude that oestrogen may reduce the plasma free protein S concentration and increase thrombophilia.
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Edenbrandt, C.-M., S. Gershagen, P. Femlund, R. Wydro, J. Stenflo, and Å. Lundwall. "GENE STRUCTURE OF VITAMIN K-DEPENDENT PROTEIN S; A REGION HOMOLOGOUS TO SEX HORMONE BINDING GLOBULIN (SHBG) REPLACES THE SERINE PROTEASE REGION OF FACTORS IX, X AND PROTEIN C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644640.

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It has recently been shown that the similarity between coagulation factors IX, X and protein C in the protein sequence is also evident in the organization of their genes. To further elucidate the relation of protein S to the other vitamin K-dependent clotting factors, we are now characterizing the human protein S gene. The size of the gene was estimated to be more than 45 kb, by hybridization of a cDNA for human protein S with chromosomal DNA in a Southern blot.We have isolated three overlapping clones from a human genomic DNA library in bacteriophage λ Charon 4A, which cover approximately 40 kb of the gene. The clones have been mapped by single- and double restriction enzyme digestion. Genomic subclones in pUC 18 which hybridize with cDNA probes for protein S have been isolated and sequenced to establish the intron/exon structure of the gene. The 5’- part of the human protein S gene closely resembles the corresponding part of the genes for factors IX, X and protein C. However, the thrombin sensitive region (amino acids 46-75), which is unique for protein S among the vitamin K-dependent clotting factors, is coded for by a separate exon. The 3'- end of the protein S gene, coding for amino acids 247-635, is not homologous to the catalytic region of the vitamin K-dependent serine proteases but shows a significant homology to human sex hormone binding globulin (SHBG).
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Reports on the topic "Protein hormone"

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Gruise, Theresa. The Role of Parathyroid Hormone-Related Protein in Breast Cancer Mediated Osteolysis. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada383256.

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Niu, Gang. Imaging Heat Shock Protein 90 (Hsp90) Activity in Hormone-Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2009. http://dx.doi.org/10.21236/ada506361.

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Srinivasan, Sathish. Involvement of Novel Multifunction Steroid Hormone Receptor Coactivator, E6-Associated Protein, in Prostate Gland Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, January 2009. http://dx.doi.org/10.21236/ada500946.

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Srinivasan, Sathish. Involvement of Novel Multifunction Steroid Hormone Receptor Coactivator, E6-Associated Protein, in Prostate Gland Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, January 2010. http://dx.doi.org/10.21236/ada524513.

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Srinvasan, Sathish. Involvement of Novel Multifunctional Steroid Hormone Receptor Coactivator, E6-Associated Protein, in Prostate Gland Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, January 2008. http://dx.doi.org/10.21236/ada481370.

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Conrad, Susan E. A Role for MEK-Interacting Protein 1 in Hormone Responsiveness of ER Positive Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2010. http://dx.doi.org/10.21236/ada540806.

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Conrad, Susan E. A Role for MEK-Interacting Protein 1 in Hormone Responsiveness of ER Positive Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2009. http://dx.doi.org/10.21236/ada514031.

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Conrad, Susan E. A Role for MEK-Interacting Protein 1 In Hormone Responsiveness of ER Positive Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, October 2011. http://dx.doi.org/10.21236/ada560599.

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Conrad, Susan E. A Role for MEK-Interacting Protein 1 (MP1) in Hormone Responsiveness of Estrogen Receptor-Positive Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2008. http://dx.doi.org/10.21236/ada491116.

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Chirgwin, John M. PSA Converts Parathyroid Hormone Related Protein (PTHrP) from an Osteolytic to an Osteoblastic Factor: Role in Bone Metastasis. Fort Belvoir, VA: Defense Technical Information Center, December 2002. http://dx.doi.org/10.21236/ada413569.

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