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Relevant bibliographies by topics / Hormone proteine

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Academic literature on the topic 'Hormone proteine'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Hormone proteine"

1

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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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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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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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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Corbacho, AM, G. Martinez De La Escalera, and C. Clapp. "Roles of prolactin and related members of the prolactin/growth hormone/placental lactogen family in angiogenesis." Journal of Endocrinology 173, no. 2 (May 1, 2002): 219–38. http://dx.doi.org/10.1677/joe.0.1730219.

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Prolactin, growth hormone and placental lactogen are members of a family of polypeptide hormones which share structural similarities and biological activities. Numerous functions have been attributed to these hormones, among which stand out their recently discovered effects on angiogenesis, the process by which new blood vessels are formed from the pre-existing microvasculature. Prolactin, growth hormone and placental lactogen, along with two non-classical members of the family, proliferin and proliferin-related protein, can act both as circulating hormones and as paracrine/autocrine factors to either stimulate or inhibit various stages of the formation and remodeling of new blood vessels, including endothelial cell proliferation, migration, protease production and apoptosis. Such opposing actions can reside in similar but independent molecules, as is the case of proliferin and proliferin-related protein, which stimulate and inhibit angiogenesis respectively. The potential to exert opposing effects on angiogenesis can also reside within the same molecule as the parent protein can promote angiogenesis (i.e. prolactin, growth hormone and placental lactogen), but after proteolytic processing the resulting peptide fragment acquires anti-angiogenic properties (i.e. 16 kDa prolactin, 16 kDa growth hormone and 16 kDa placental lactogen). The unique properties of the peptide fragments versus the full-length molecules, the regulation of the protease responsible for specific protein cleavage, the selective expression of specific receptors and their associated signal transduction pathways are issues that are being investigated to further establish the precise contribution of these hormones to angiogenesis under both physiological and pathological situations. In this review article, we summarize the known and speculative issues underlying the effects of the prolactin, growth hormone and placental lactogen family of proteins on angiogenesis, and address important remaining enigmas in this field of research.

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Puzianowska-Kuznicka, Monika, Eliza Pawlik-Pachucka, Magdalena Owczarz, Monika Budzińska, and Jacek Polosak. "Small-Molecule Hormones: Molecular Mechanisms of Action." International Journal of Endocrinology 2013 (2013): 1–21. http://dx.doi.org/10.1155/2013/601246.

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Small-molecule hormones play crucial roles in the development and in the maintenance of an adult mammalian organism. On the molecular level, they regulate a plethora of biological pathways. Part of their actions depends on their transcription-regulating properties, exerted by highly specific nuclear receptors which are hormone-dependent transcription factors. Nuclear hormone receptors interact with coactivators, corepressors, basal transcription factors, and other transcription factors in order to modulate the activity of target genes in a manner that is dependent on tissue, age and developmental and pathophysiological states. The biological effect of this mechanism becomes apparent not earlier than 30–60 minutes after hormonal stimulus. In addition, small-molecule hormones modify the function of the cell by a number of nongenomic mechanisms, involving interaction with proteins localized in the plasma membrane, in the cytoplasm, as well as with proteins localized in other cellular membranes and in nonnuclear cellular compartments. The identity of such proteins is still under investigation; however, it seems that extranuclear fractions of nuclear hormone receptors commonly serve this function. A direct interaction of small-molecule hormones with membrane phospholipids and with mRNA is also postulated. In these mechanisms, the reaction to hormonal stimulus appears within seconds or minutes.

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Borsellino, Giovanni, Arturo Buonaguidi, Mario Baroni, Gaetano Elli, Augusta Sonato, Silvano Poma, Stefania Rescalli, and Roberto Mondina. "Plasma Steroid Transport in Subjects with Tumors of Hormonal Target Organs: A Review." Tumori Journal 78, no. 3 (June 1992): 155–58. http://dx.doi.org/10.1177/030089169207800302.

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Tumors derived from a hormonal target organ are assumed to be stimulated by the same hormone that stimulates the normal target tissue. In spite of attempts to acquire direct indications of a correlation between hormones and cancer, none have been definitive because studies of total and free hormone levels have given contradictory results. For this reason, attention has shifted to the study of plasma binding and transport of hormones, that is, of the proteins responsible for modulation of the hormone effect and thus of hormone bioavailability. The data reviewed indicate that in-depth study of the transport and binding system of sex steroids would give new information about the endocrine characteristics of cancer patients.

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8

Cordeiro, Aline, Luana Lopes Souza, Marcelo Einicker-Lamas, and Carmen Cabanelas Pazos-Moura. "Non-classic thyroid hormone signalling involved in hepatic lipid metabolism." Journal of Endocrinology 216, no. 3 (January 7, 2013): R47—R57. http://dx.doi.org/10.1530/joe-12-0542.

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Thyroid hormones are important modulators of lipid metabolism because the liver is a primary hormonal target. The hypolipidaemic effects of thyroid hormones result from the balance between direct and indirect actions resulting in stimulation of lipid synthesis and lipid oxidation, which favours degradation pathways. Originally, it was believed that thyroid hormone activity was only transduced by alteration of gene transcription mediated by the nuclear receptor thyroid hormone receptors, comprising the classic action of thyroid hormone. However, the discovery of other effects independent of this classic mechanism characterised a new model of thyroid hormone action, the non-classic mechanism that involves other signalling pathways. To date, this mechanism and its relevance have been intensively described. Considering the increasing evidence for non-classic signalling of thyroid hormones and the major influence of these hormones in the regulation of lipid metabolism, we reviewed the role of thyroid hormone in cytosolic signalling cascades, focusing on the regulation of second messengers, and the activity of effector proteins and the implication of these mechanisms on the control of hepatic lipid metabolism.

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Meier, V. S., and B. Groner. "The nuclear factor YY1 participates in repression of the beta-casein gene promoter in mammary epithelial cells and is counteracted by mammary gland factor during lactogenic hormone induction." Molecular and Cellular Biology 14, no. 1 (January 1994): 128–37. http://dx.doi.org/10.1128/mcb.14.1.128.

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Expression of the beta-casein milk protein gene in the mammary epithelial cell line HC11 is primarily regulated at the transcriptional level. A 338-bp segment of promoter sequence 5' of the transcription start site is sufficient to confer inducibility by the lactogenic hormones insulin, glucocorticoid hormone, and prolactin. Positively and negatively acting promoter elements and specific DNA binding proteins have been identified. The binding of the mammary gland factor MGF to a site between -80 and -100 is indispensable for hormonal induction of transcription. Binding of MGF activity to DNA is greatly enhanced by the action of the lactogenic hormones. Repression of transcription in the uninduced state is mediated by a promoter element located adjacent to the MGF binding site at positions -110 to -150. This repressor element consists of two interacting protein binding sites. A nuclear factor that binds specifically to the proximal site between positions -110 and -120 has been characterized and found to be identical with the nuclear factor YY1 (delta, NF-E1). YY1 does not bind to the distal site. The simultaneous mutation in the proximal and the distal sites results in high, hormone-independent transcription. This finding suggests that YY1 plays a functional role in the repression and acts in conjunction with a second DNA binding protein. Comparison of YY1 DNA binding activity in uninduced and hormone-induced cells showed that relief of repression is not mediated by changes in the concentration or binding affinity of YY1. Infection of HC11 cells with a YY1-expressing recombinant retrovirus resulted in overexpression of YY1 but did not suppress hormonal induction. The addition of purified MGF decreased YY1 binding to its DNA recognition site in vitro. This finding indicates that MGF regulates the DNA binding activity of YY1 and thereby may cause the relief of transcriptional repression.

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Meier, V. S., and B. Groner. "The nuclear factor YY1 participates in repression of the beta-casein gene promoter in mammary epithelial cells and is counteracted by mammary gland factor during lactogenic hormone induction." Molecular and Cellular Biology 14, no. 1 (January 1994): 128–37. http://dx.doi.org/10.1128/mcb.14.1.128-137.1994.

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Expression of the beta-casein milk protein gene in the mammary epithelial cell line HC11 is primarily regulated at the transcriptional level. A 338-bp segment of promoter sequence 5' of the transcription start site is sufficient to confer inducibility by the lactogenic hormones insulin, glucocorticoid hormone, and prolactin. Positively and negatively acting promoter elements and specific DNA binding proteins have been identified. The binding of the mammary gland factor MGF to a site between -80 and -100 is indispensable for hormonal induction of transcription. Binding of MGF activity to DNA is greatly enhanced by the action of the lactogenic hormones. Repression of transcription in the uninduced state is mediated by a promoter element located adjacent to the MGF binding site at positions -110 to -150. This repressor element consists of two interacting protein binding sites. A nuclear factor that binds specifically to the proximal site between positions -110 and -120 has been characterized and found to be identical with the nuclear factor YY1 (delta, NF-E1). YY1 does not bind to the distal site. The simultaneous mutation in the proximal and the distal sites results in high, hormone-independent transcription. This finding suggests that YY1 plays a functional role in the repression and acts in conjunction with a second DNA binding protein. Comparison of YY1 DNA binding activity in uninduced and hormone-induced cells showed that relief of repression is not mediated by changes in the concentration or binding affinity of YY1. Infection of HC11 cells with a YY1-expressing recombinant retrovirus resulted in overexpression of YY1 but did not suppress hormonal induction. The addition of purified MGF decreased YY1 binding to its DNA recognition site in vitro. This finding indicates that MGF regulates the DNA binding activity of YY1 and thereby may cause the relief of transcriptional repression.

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Dissertations / Theses on the topic "Hormone proteine"

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Aina, E. M. "Regulation du metabolisme du glucose et des acides amines par l'insuline et le glucagon chez la chevre en lactation." Clermont-Ferrand 2, 1988. http://www.theses.fr/1988CLF21126.

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Beau, Isabelle. "Etude de la polarisation des récepteurs de la FSH de la LH et de la TSH dans les cellules MDCK." Paris 11, 1995. http://www.theses.fr/1995PA11T035.

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Pascalon, Annette. "Influence des deficits energetiques et proteiques sur l'evolution de la gestation et le taux des acides amines libres chez la ratte : effets sur les concentrations de progesterone et de prolactine aux periodes critiques de la mortalite embryonnaire." Clermont-Ferrand 2, 1988. http://www.theses.fr/1988CLF21092.

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Samson, Michel. "Le transport membranaire des hormones thyroïdiennes : caractérisation, identification et purification partielle des protéines de transport de l'érythracyte." Paris 11, 1993. http://www.theses.fr/1993PA11T035.

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Crave, Jean-Charles. "Proteine de liaison des hormones steroides sexuelles ; role des facteurs metaboliques et nutritonnels." Lyon 1, 1990. http://www.theses.fr/1990LYO1M182.

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Cousin, Patrice. "Étude des formes circulantes de la Sex Hormone-Binding Globulin (SHBG) humaine, protéine de liaison des hormones stéroïdes sexuelles : mesure des clairances métaboliques." Lyon 1, 2000. http://www.theses.fr/2000LYO1T006.

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Desvergne, Béatrice. "Regulation transcriptionnelle par les hormones thyroidiennes : caracterisation des elements de reponse presents au sein des promoteurs des genes de l'enzyme malique et de la proteine basique de la myeline." Paris 11, 1993. http://www.theses.fr/1993PA11T033.

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David, Jean-Pierre. "Régulation hormonale du promoteur de la HSP90 de poulet : modulation de la réponse hormonale par le choc thermique." Paris 11, 1992. http://www.theses.fr/1992PA11T016.

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Dinerstein-Cali, Hélène. "Etude des molecules impliquees dans la transduction du signal du recepteur de l'hormone de croissance (doctorat : endocrinologie et interactions cellulaires)." Paris 11, 2000. http://www.theses.fr/2000PA11T005.

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Le, Bihan Stéphane. "Role des immunophilines dans le mecanisme d'action des recepteurs des glucocorticosteroides et des progestagenes." Paris 11, 1996. http://www.theses.fr/1996PA11T025.

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Books on the topic "Hormone proteine"

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

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

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3

G, Forest Maguelone, Pugeat M, and Institut national de la santé et de la recherche médicale (France), eds. Binding proteins of steroid hormones =: Protéines de liaison des hormones stéroïds : proceedings of the First International Symposium on Binding Proteins: Steroid Hormones held in Lyon 26-30 April 1986. Paris: INSERM, 1986.

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4

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

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Steroid-protein interactions II. Berlin: Springer-Verlag, 1986.

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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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Matsuto, Mochizuki, and Hussa Robert O, eds. Placental protein hormones: Proceedings of the Satellite Symposium on Placental Protein Hormones, Kobe, Japan, 14-15 July 1988. Amsterdam: Excerpta Medica, 1988.

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9

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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Book chapters on the topic "Hormone proteine"

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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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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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Baumann, Gerhard. "Growth Hormone Binding Proteins." In Growth Hormone, 37–57. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-5163-8_3.

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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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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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Walsh, Gary. "Hormones and Growth Factors Used Therapeutically." In Proteins, 233–55. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2015. http://dx.doi.org/10.1002/9781119117599.ch8.

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Hintz, Raymond L. "The Somatomedin Binding Proteins." In Human Growth Hormone, 553–61. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4615-7201-5_44.

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Brinegar, A. Chris, and J. E. Fox. "Immunocytological Localization of a Wheat Embryo Cytokinin Binding Protein and its Homology with Proteins in other Cereals." In Plant Hormone Receptors, 177–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72779-5_17.

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Hai, Huang, Lu Jia-ling, Jian Zhi-ying, and Tang Yu-wei. "Studies on Cytokinin Binding Proteins." In Plant Hormone Receptors, 185–97. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72779-5_18.

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Thomas, P. J. "Protein and Peptide Hormones." In Characterization of Proteins, 233–43. Totowa, NJ: Humana Press, 1988. http://dx.doi.org/10.1007/978-1-59259-437-5_9.

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Conference papers on the topic "Hormone proteine"

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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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Stenflo, J., A.-K. öhlin, Å. Lundvall, and B. Dahlback. "β-HYDROXY ASPARTIC ACID AND ft-HYDROXYASPARAGINE IN THEEGF-HOMOLOGY REGIONS OF PROTEIN C AND PROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643995.

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The amino acid sequence has been determined for all of the vitamin K-dependent proteins and the gene structure is known for some of them. These findings have shown the proteins to consist of four clearly discernible domains, except protein S which has six domains. The protein domains seem to be coded on separate exons (Foster, D. C. et. al. 1985 Proc. Natl. Acad. Sci. USA 82,4673). The vitamin K-dependent γ-carboxyglutamic acid (Gla) containing domain isthe common structural denominator of the members of this protein family. In addition, all of these proteins except prothrombin contain domains that are homologous to the precursor of the epidermal growth factor (EGF). Such domains arealso found in proteins that are not vitamin K-dependent, such as the low density lipoprotein receptor, thrombomodulin, factor XII, plasminogen, the tissue type plasminogen activator, urokinase and the complement protein Clr. The vitamin K-dependent proteins can be dividedinto three groups. Factors VII, IX, X, protein C and protein Z form one group, which in addition to the Gla-region have two EGF-homology regions and one domain that is homologous to the serine proteases. Prothrombin has two 'kringle' structures and a serine protease domain and constitutes a group of its own. Protein S is also unique in that it has four EGF-homology regions and a COOH-terminal region that is homologous to the sexual hormone binding globulin (see poster by Edenbrand et. al.).Recently a posttranslationally modified amino acid, B-hydroxyaspatic acid (Hya), was identified in position 71 in the NH2-terminal EGF-homology region ofbovine protein C. The amino acid is formed by hydroxylation of aspartic acid. It has also been identified in the corresponding positions in factors VII, IX,X and protein Z (i. e. proteins which like protein C have two EGF-homology regions each). In protein S the N2-terminal of four EGF-homology regions has hydroxy lated aspartic acid .whereas the following three EGF-like domains have B-hydroxyasparagine. The nucleotide sequence codes for asparagine in the three latter positions. Neither vitamin K nor vitamin C seem to be involvedin the formation of the two hydroxylated amino acids. Recently, Hya was identified in acid hydrolysates of the complement protein Clr. Hya and Hyn have onlybeen found in domains that are homologous to the EGF precursor. In an attempt to identify the structural requirement of the hydroxylating enzyme, we have compared the sequences of EGF-homology regions that contain Hya or Hyn with the corresponding sequences that have been shown not to contain the modified amino acids. The domains that have Hya or Hyn have the consensus sequence Cx xxxx xCxC. This sequence has been found in three EGF-like domains in the EGF-precursor, in two in the LDL-receptor and in two in thrombomodulin. Furthermore, the neurogenic Notch locus in Drosophila melanogaster codes for 36 EGF-homolgy regions, 22 of which contain the consensussequence, whereas the Lin-12 locus in Caenorhabditis elegans codes for at least 11 EGF-like repeats, two of which comply with the consensus sequence. Whether any of these proteins contain Hya orHyn is not yet known with certainty.It has been hypothesized that Hya isinvolved in the Gla independent Ca2+binding of factors IX, X and protein C. In an attempt to resolve this issue, we have isolated the EGF-homology region from human protein C and been able to demonstrate that it binds Ca2+ (see poster by öhlin and Stenflo). However, we do not yet know whether Hya is directly involved in the Ca2+binding.

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Yanoso, Laura, Justin Jacobson, Tulin Dadali, David Reynolds, and Hani Awad. "Evaluation of Polylactic Acid/Beta-Tricalcium Phosphate Scaffolds as Segmental Bone Graft Substitutes." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192978.

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The use of processed structural allografts for treatment of massive segmental defects in long bones can be complicated by poor incorporation and remodeling of the devitalized graft, foreign-body reaction and micro-damage accumulation which often leads to catastrophic graft failure [1]. It is therefore useful to develop a bioengineered, biodegradable scaffold that is able to stimulate healing of the defect region. The use of bioengineered scaffolds has been limited due to their poor mechanical strength that does not permit withstanding large in vivo loads and due to their poor osteoinductive properties. We therefore investigated the use of rigid polylactic acid/beta-tricalcium phosphate (PLA/βTCP) composites used in conjunction with osteoinductive factors such as growth hormones (parathyroid hormone (PTH)) and growth factors (bone morphogenic protein-2 (BMP-2) & vascular endothelial growth factor (VEGF)) to stimulate bone formation and vessel ingrowth in the segmental defect region. We examined the physical characteristics of the scaffolds, and evaluated their osteoinductive potential in a clinically-relevant mouse model of a femoral segmental defect with or without PTH treatment. Finally, we used an ectopic bone formation model to assess the efficacy of the scaffold in site-specific delivery of bone anabolic factors.

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Elbashir, Israa, Heba Al Khatib, and Hadi Yassine. "Replication Dynamics, Pathogenicity, and Evolution of Influenza Viruses in Intestinal Caco-2 Cells." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0166.

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Background: Influenza virus is a major cause of respiratory infections worldwide. Besides the common respiratory symptoms, namouras cases with gastrointestinal symptoms have been reported. Moreover, influenza virus has been detected in feces of up to 20.6 % of influenza-infected patients. Therefore, direct infection of intestinal cells with influenza virus is suspected; however, the mechanism of this infection has not been explored. AIM: To investigate influenza virus replication, cellular responses to infection, and virus evolution following serial infection in human Caucasian colon adenocarcinoma cells (Caco-2 cells). Method: Two influenza A subtypes (A/H3N2 and A/H1N1pdm 09) and one influenza B virus (B/Yamagata) were serially passaged in Caco-2. Quantitative PCR was used to study hormones and cytokines expression following infection. Deep sequencing analysis of viral genome was used to assess the virus evolution. Results: The replication capacity of the three viruses was maintained throughout 12 passages, with H3N2 virus being the fastest in adaptation. The expression of hormone and cytokines in Caco-2 cells was considerably different between the viruses and among the passages, however, a pattern of induction was observed at the late phase of infection. Deep sequencing analysis revealed a few amino acid substitutions in the HA protein of H3N2 and H1N1 viruses, mostly in the antigenic site. Moreover, virus evolution at the quasispecies level based on HA protein revealed that H3N2 and H1N1 harbored more diverse virus populations when compared to IBV, indicating their higher evolution within Caco-2 cells. Conclusion: The findings of this study indicate the possibility of influenza virus replication in intestinal cells. To further explain the gastrointestinal complications of influenza infections in-vivo experiments with different influenza viruses are needed.

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Mohbeddin, Abeer, Nawar Haj Ahmed, and Layla Kamareddine. "The use of Drosophila Melanogaster as a Model Organism to study the effect of Innate Immunity on Metabolism." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0224.

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Apart from its traditional role in disease control, recent body of evidence has implicated a role of the immune system in regulating metabolic homeostasis. Owing to the importance of this “immune-metabolic alignment” in dictating a state of health or disease, a proper mechanistic understanding of this alignment is crucial in opening up for promising therapeutic approaches against a broad range of chronic, metabolic, and inflammatory disorders like obesity, diabetes, and inflammatory bowel syndrome. In this project, we addressed the role of the Janus kinase/signal transducer and activator of transcription (JAK/STAT) innate immune pathway in regulating different metabolic parameters using the Drosophila melanogaster (DM) fruit fly model organism. Mutant JAK/STAT pathway flies with a systemic knockdown of either Domeless (Dome) [domeG0282], the receptor that activates JAK/STAT signaling, or the signal-transducer and activator of transcription protein at 92E (Stat92E) [stat92EEY10528], were used. The results of the study revealed that blocking JAK/STAT signaling alters the metabolic profile of mutant flies. Both domeG0282 and stat92EEY10528 mutants had an increase in body weight, lipid deprivation from their fat body (lipid storage organ in flies), irregular accumulation of lipid droplets in the gut, systemic elevation of glucose and triglyceride levels, and differential down-regulation in the relative gene expression of different peptide hormones (Tachykinin, Allatostatin C, and Diuretic hormone 31) known to regulate metabolic homeostasis in flies. Because the JAK/STAT pathway is evolutionary conserved between invertebrates and vertebrates, our potential findings in the fruit fly serves as a platform for further immune-metabolic translational studies in more complex mammalian systems including humans.

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Bojovic, Biljana, Milica Kanjevac, and Dragana Jakovljevic. "EFEKAT PRAJMIRANJA SEMENA PŠENICE (Triticum aestivum L.) NA SADRŽAJ FOTOSINTETSKIH PIGMENATA I UKUPNIH SOLUBILNIH PROTEINA." In XXVI savetovanje o biotehnologiji sa međunarodnim učešćem. University of Kragujevac, Faculty of Agronomy, 2021. http://dx.doi.org/10.46793/sbt26.401b.

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In this paper, effect of different priming treatments in the pregerminative phase of wheat seeds (Triticum aestivum L.) on the concentration of photosynthetic pigments and total soluble proteins in the leaf of seedling was investigated. Seeds were treated with solutions of the phytohormones gibberellin and auxin (hormone priming), salts of potassium and magnesium (halo priming), ascorbic acid and hydrogen peroxide (chemo priming) and water (hydro priming). Based on the obtained results, it was determined that the content of pigments and total soluble proteins can be increased by applying the appropriate priming treatment. The most favorable effect on the examined parameters was observed in the treatment with potassium nitrate.

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Comp, P. C., and C. T. Esmon. "Defects in the protein C pathway." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643715.

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Activated protein C functions as an anticoagulant by enzymatically degrading factors Va and Villa in the clotting cascade. Protein C may be converted to its enzymatically active form bythrombin. The rate at which thrombin cleavage of the zymogen occurs is greatly enhanced when thrombin is bound to an endothelial cell receptor protein, thrombomodulin. Activated proteinC has a relatively long half-life in vivo and the formation of activated protein C in response to low level thrombin infusion suggests that the protein C system may provide a feedback mechanism to limit blood clotting. Clinical support for such a physiologic role for activated protein C includes an increased incidence of thrombophlebitis and pulmonary emboli in heterozygous deficient individuals, and severe, often fatal, cutaneous thrombosis in homozygous deficient newborns. A third thrombotic condition associated with protein C deficiency is coumarin induced skin (tissue) necrosis. This localized skin necrosis occurs shortly after the initiation of coumarin therapy and is hypothesized to bedue to the rapid disappearance of protein C activity in the plasma beforean adequate intensity of anticoagulation is achieved. Recent estimates of heterozygous protein C deficiency range as high as 1 in 300 individuals in the general population. Since coumarin compounds are in routine clinical use throughout the world and skin necrosis remains a relatively rare clinical finding, this suggests that factors other than protein C deficiency alone may be involved in the pathogenesis of the skin necrosis.The anticoagulant properties of activated protein C are greatly enhanced by another vitamin K-dependent plasma protein, protein S. Protein S functions by increasing the affinity of activated protein C for cell surfaces.Protein S is found in two forms in plasma: free and in complex with C4b-binding protein, "an inhibitor of the complement system. Free protein S is functionally active and the complexed protein S is not active. Individuals congenitally deficient in protein S ae subject to recurrent thromboembolicevents. At least two classes of protin S deficiency occur.Some patienshavedecreased levels of protein S antigen and reduced protein S functional activity. A second group of deficient individuals have normal levels of protein S antigen but most or all their protein S is complexed to C4b-binding protein and they have little or no functional protein S activity. Such a protein S distribution could result from abnormal forms of protein S or C4b-binding protein or some other abnormal plasma or cellular component. Patients with functionally inactive forms of protein S have yet to be identified. Identification of protein S deficient individuals is complicated by thepossible effect of sex hormones on plasma protein S levels. Total protein S antigen is reduced during pregnancyand during oral contraceptive administration. This finding is of practicalclinical importance since the decrease in protein S which occurs during pregnancy may be an added risk factor for congenitally protein S deficient women and may explain why some proteinS deficient women experience their first episode of thrombosis during pregnancy.In addition to having anticoagulant properties, activated protein C enhances fibrinolysis, at least in part,by inhibiting the inhibitor of tissueplasminogen activator. This profibrinolytic effect is enhanced by protein S and cell surfaces. This protection of plasminogen activator activity suggests that the combination of tissue plasminogen activator and activated protein C may be useful in the treatment of coronary artery thrombi. Tissueplasminogen activator would promote clot lysis while activated protein C protected the plasminogen activatorfrom inhibition and also prevented further clot deposition. There is no evidence at present that fibrinolytic activity is reduced in protein C deficient individuals. The possible clinical relevance of this aspect of protein Cfunction in the predisposition of protein C deficient individuals to thrombosis remains to be defined.

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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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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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Medcalf, R. L., E. van den Berg, and W.-D. Schleuning. "THE INFLUENCE OF GLUCOCORTICOID HORMONES ON THE GENE TRANSCRIPTION OF POUR COMPONENTS OF THE FIBRINOLYTIC SYSTEM." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644611.

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The hormonal regulation of plasminogen activator (urokinase type (u-PA) and tissue-type (t-PA)) biosynthesis plays an important role in fibrinolysis and extracellular matrix turnover during invasive growth and cell migration. Recently, two genetically distinct inhibitors of both PA's (PA inhibitor 1 (PAI-1) and PA inhibitor 2 (PAI-2)) have been described which may contribute to the modulation of matrix stability. We have employed cloned cDNA probes to study the regulation of biosynthesis of these proteins in the human fibrosarcoma line HT1080. These cells constitutively express high levels of pro-u-PA. PAI-1, PAI-2 and t-PA are also present at relatively low levels. Treatment of the cells with the glucocorticoid dexamethasone (Dex; 10−7 M), almost completely suppresses u-PA gene transcription, as determined by measurement of in vitro elongation of initiated u-PA transcripts in isolated nuclei ("run-on" transcription assay). Concomitantly, Dex also induces PAI-1 and t-PA gene transcription, whereas PAI-2 gene transcription appeared to remain ' unaffected. These changes in transcription rates are also reflected at the level of mRNA: u-PA mRNA is decreased, whereas PAI-1 and t-PA mRNA are simultaneously induced. PAI-2 mRNA is apparently unchanged. These results demonstrate that glucocorticoid hormones reprogramne the expression of components of the fibrinolytic system, and are of possible relevance in the context of inflammatory disease and malignancy.

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Reports on the topic "Hormone proteine"

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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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Wainberg, Zev. Development of Antibodies Against Novel Cell Surface Proteins in Hormone Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2007. http://dx.doi.org/10.21236/ada475475.

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Wainberg, Zev A. Development of Antibodies Against Novel Cell Surface Proteins in Hormone Refractory Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2009. http://dx.doi.org/10.21236/ada523982.

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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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Callis, Judy. The Role of RUB (related to ubiquitin) Family of Proteins in the Hormone Response. Final Report. Office of Scientific and Technical Information (OSTI), March 2013. http://dx.doi.org/10.2172/1070042.

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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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