Academic literature on the topic 'Propeptide de la sortiline'
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Journal articles on the topic "Propeptide de la sortiline":
Hivelin, C., J. Mazella, and T. Coppola. "CA-143: Le propeptide de la sortiline module l'entrée de glucose dans les adipocytes et les myocytes." Diabetes & Metabolism 42 (March 2016): A74. http://dx.doi.org/10.1016/s1262-3636(16)30275-0.
Hivelin, Céline, Jean Mazella, and Thierry Coppola. "Sortilin derived propeptide regulation during adipocyte differentiation and inflammation." Biochemical and Biophysical Research Communications 482, no. 1 (January 2017): 87–92. http://dx.doi.org/10.1016/j.bbrc.2016.10.139.
Petersen, C. M. "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding." EMBO Journal 18, no. 3 (February 1, 1999): 595–604. http://dx.doi.org/10.1093/emboj/18.3.595.
Mazella, J., C. Devader, M. Roulot, M. Borsotto, and C. Heurteaux. "Regulation of serum spadin propeptide: An antidepressant response probe." European Psychiatry 33, S1 (March 2016): S417. http://dx.doi.org/10.1016/j.eurpsy.2016.01.1507.
Roulot, Morgane, Alessandra Minelli, Marco Bortolomasi, Elisabetta Maffioletti, Massimo Gennarelli, Marc Borsotto, Catherine Heurteaux, and Jean Mazella. "Increased serum levels of sortilin-derived propeptide after electroconvulsive therapy in treatment-resistant depressed patients." Neuropsychiatric Disease and Treatment Volume 14 (September 2018): 2307–12. http://dx.doi.org/10.2147/ndt.s170165.
Devader, Christelle, Morgane Roulot, Sébastien Moréno, Alessandra Minelli, Marco Bortolomasi, Chiara Congiu, Massimo Gennarelli, Marc Borsotto, Catherine Heurteaux, and Jean Mazella. "Serum sortilin-derived propeptides concentrations are decreased in major depressive disorder patients." Journal of Affective Disorders 208 (January 2017): 443–47. http://dx.doi.org/10.1016/j.jad.2016.10.049.
Mazella, Jean, and Jean-Pierre Vincent. "La sortiline : une protéine associée à de multiples fonctions." médecine/sciences 20, no. 6-7 (June 2004): 629–31. http://dx.doi.org/10.1051/medsci/2004206-7629.
Kaufman, Beth D., Nancy Videon, Xuemei Zhang, Matthew A. Harris, Robert E. Shaddy, and Elizabeth Goldmuntz. "Procollagen type III amino-terminal propeptide: a serum biomarker of left ventricular remodelling in paediatric dilated cardiomyopathy." Cardiology in the Young 25, no. 2 (November 6, 2013): 228–36. http://dx.doi.org/10.1017/s1047951113001820.
Meiring, S. M., B. D. P. Setlai, C. Theron, and R. Bragg. "The Use of Phage Display and Yeast Based Expression System for the Development of a Von Willebrand Factor Propeptide Assay: Development of a Von Willebrand Factor Propeptide Assay." BioMed Research International 2018 (2018): 1–7. http://dx.doi.org/10.1155/2018/6232091.
Emeis, Jef, Henk Bilo, Coen Stehouwer, Claus Thomsen, Ole Rasmussen, Kjeld Hermansen, Claes Wollheim, Jørgen Ingerslev, and Ulrich Vischer. "von Willebrand Factor (vWf) as a Plasma Marker of Endothelial Activation in Diabetes: Improved Reliability with Parallel Determination of the vWf Propeptide (vWf:AgII)." Thrombosis and Haemostasis 80, no. 12 (1998): 1002–7. http://dx.doi.org/10.1055/s-0037-1615401.
Dissertations / Theses on the topic "Propeptide de la sortiline":
Hivelin, Céline. "Étude des mécanismes de libération du propeptide de la sortiline et de ses effets sur l’homéostasie glucidique." Thesis, Université Côte d'Azur (ComUE), 2016. http://www.theses.fr/2016AZUR4109/document.
In France, approximately 15% of the population is obese and this number keeps rising up every year. Obesity is a major cause of diabetes, inducing an increase of the number of fat-filled cells, called the adipocytes, and a peripheral insulin resistance. This increase of the number of adipocytes is associated with a decrease of sortilin expression, a transmembrane protein which is involved in the release of a propeptide (PE) in the blood circulation. Spadin, a synthetic PE analog, is known to modulate the potassium TREK-1 channel activity. Since, this channel is expressed in pancreatic beta cells which secrete insulin, a hormone involved in blood glucose regulation, spadin may play a role in glucose homeostasis. Consistent with this hypothesis, spadin improves glucose tolerance in mice, by stimulating insulin release. Spadin is a natural peptide derived from sortilin, which is known to control the glucose transporter Glut4 trafficking to the plasma membrane of adipocytes. This suggests that spadin may regulate glucose storage in adipocytes by affecting the sortilin function. However, my results show that spadin has no effect on glucose storage. In summary, spadin is involved in insulin secretion and glucose homeostasis and may be an alternative treatment against obesity and diabetes
Hivelin, Céline. "Étude des mécanismes de libération du propeptide de la sortiline et de ses effets sur l’homéostasie glucidique." Electronic Thesis or Diss., Université Côte d'Azur (ComUE), 2016. http://www.theses.fr/2016AZUR4109.
In France, approximately 15% of the population is obese and this number keeps rising up every year. Obesity is a major cause of diabetes, inducing an increase of the number of fat-filled cells, called the adipocytes, and a peripheral insulin resistance. This increase of the number of adipocytes is associated with a decrease of sortilin expression, a transmembrane protein which is involved in the release of a propeptide (PE) in the blood circulation. Spadin, a synthetic PE analog, is known to modulate the potassium TREK-1 channel activity. Since, this channel is expressed in pancreatic beta cells which secrete insulin, a hormone involved in blood glucose regulation, spadin may play a role in glucose homeostasis. Consistent with this hypothesis, spadin improves glucose tolerance in mice, by stimulating insulin release. Spadin is a natural peptide derived from sortilin, which is known to control the glucose transporter Glut4 trafficking to the plasma membrane of adipocytes. This suggests that spadin may regulate glucose storage in adipocytes by affecting the sortilin function. However, my results show that spadin has no effect on glucose storage. In summary, spadin is involved in insulin secretion and glucose homeostasis and may be an alternative treatment against obesity and diabetes
Daziano, Guillaume. "Rôle du propeptide de la sortiline et de ses dérivés dans les mécanismes de survie de la cellule bêta pancréatique." Electronic Thesis or Diss., Université Côte d'Azur, 2021. http://www.theses.fr/2021COAZ6025.
In 2019, the International Diabetes Federation revealed that nearly 500 million people have diabetes worldwide. It is estimated that this incidence will reach 700 million people by 2045. In addition to the financial aspect of treatment, diabetes is a real public health issue. Indeed, the deleterious hyperglycemic environment associated with diabetes is could induce serious complications, leading to a functional alteration of many organs such as the heart, the brain or the kidney. Insulin resistance associated with the deterioration of insulin secretion and the loss of pancreatic beta cell mass are the main characteristics of type 2 diabetes. Thus, in order to improve the management of diabetic patients, the identification of a controlled therapeutic approach to protect beta cell mass and promote insulin secretion only in response to glucose and without side effects, appears ideal.The laboratory has identified the endogenous PE and its synthetic derivatives Spadin and Mini-Spadin as selective inhibitors of TREK-1 potassium channels. By this mechanism, the peptides showed also a strong antidepressant potential by modulating serotonin secretion, neuronal proliferation and survival. At the peripheral level, Spadin has been described in vitro and in vivo as a peptide with an incretin effect comparable to that of exendin-4, an antidiabetic commonly used in the clinic. Thus, following this study and by analogy to the protective effects observed on the neuron, we hypothesized that PE and its derivatives may have a beneficial role in the survival mechanisms in the pancreatic beta-cell.In this thesis, we demonstrate that endogenous PE and its derivatives protect beta cells from apoptosis induced by the chronic presence of the pro-inflammatory and diabetogenic interleukin IL-1β, as well as from an acute toxic shock induced by staurosporine. Furthermore, analysis of intracellular mechanisms reveals that these peptides cause an increase in intracellular calcium concentration, activate the ERK and Akt proliferative and survival pathways, and maintain CREB transcriptional factor activity in a deleterious environment via a calmodulin kinase-dependent pathway.Thus, this work shows that PE and its synthetic derivatives protect the pancreatic beta-cell and initiate virtuous cellular processes through an original PKA-independent signaling pathway, where membrane potential and calcium play a crucial role. This suggests the sortilin-derived peptides as a new class of pancreatic beta-cell protective molecules
Moreno, Sébastien. "Le récepteur 3 de la neurotensine/Sortiline dans la régulation de l’état dépressif." Thesis, Université Côte d'Azur (ComUE), 2017. http://www.theses.fr/2017AZUR4136/document.
Major depressive disorder is a condition that affects 20% of the population and is the leading cause of morbidity and disability worldwide. Recently, the TREK-1 potassium channel has been shown to be a potential target in the treatment of depression. The deletion of this channel or its blocking by a derived peptide resulting from the maturation of Sortilin, propeptide (PE), or its synthetic analogue Spadin, results in a phenotype of resistance to depression in mice. Sortilin is a protein able to bind with TREK-1 but also with the neurotrophic factor BDNF, an important factor for neuronal viability and depressive state regulation. Sortilin is therefore involved in regulating the intracellular addressing of TREK-1 and BDNF. Initially, my work focused on the consequences of the deletion of the Sortilin gene (sort1-/-) on the TREK-1 and BDNF addressing, and the neurotensinergic system. The results showed a decrease in TREK-1 membrane expression at the cerebral level and an increase in BDNF. All of these changes lead the Sort1-/- mice to develop a phenotype of resistance to depression. In addition, these mice show an increase in brain neurotensin concentration and its receptor 2, leading to increased resistance to pain perception. In a second phase, I was interested in whether PE, a potential antidepressant, showed serum variations in depressed patients and could be an indicator of depressive syndrome. We showed that the serum PE level is significantly reduced in depressed people, a level restored after treatment with antidepressants. In conclusion, Sortilin plays a major key in the regulation of depressive disorder and also in nociception
Moreno, Sébastien. "Le récepteur 3 de la neurotensine/Sortiline dans la régulation de l’état dépressif." Electronic Thesis or Diss., Université Côte d'Azur (ComUE), 2017. http://www.theses.fr/2017AZUR4136.
Major depressive disorder is a condition that affects 20% of the population and is the leading cause of morbidity and disability worldwide. Recently, the TREK-1 potassium channel has been shown to be a potential target in the treatment of depression. The deletion of this channel or its blocking by a derived peptide resulting from the maturation of Sortilin, propeptide (PE), or its synthetic analogue Spadin, results in a phenotype of resistance to depression in mice. Sortilin is a protein able to bind with TREK-1 but also with the neurotrophic factor BDNF, an important factor for neuronal viability and depressive state regulation. Sortilin is therefore involved in regulating the intracellular addressing of TREK-1 and BDNF. Initially, my work focused on the consequences of the deletion of the Sortilin gene (sort1-/-) on the TREK-1 and BDNF addressing, and the neurotensinergic system. The results showed a decrease in TREK-1 membrane expression at the cerebral level and an increase in BDNF. All of these changes lead the Sort1-/- mice to develop a phenotype of resistance to depression. In addition, these mice show an increase in brain neurotensin concentration and its receptor 2, leading to increased resistance to pain perception. In a second phase, I was interested in whether PE, a potential antidepressant, showed serum variations in depressed patients and could be an indicator of depressive syndrome. We showed that the serum PE level is significantly reduced in depressed people, a level restored after treatment with antidepressants. In conclusion, Sortilin plays a major key in the regulation of depressive disorder and also in nociception
Massa, Fabienne. "Rôle du système neurotensinergique dans la prolifération et l'adhésion des cellules cancéreuses de colon." Nice, 2011. http://www.theses.fr/2011NICE4055.
Neurotensin (NT) can act in periphery and in the central nervous system. Two of this receptors are G protein coupled receptors (NTSR1 and NTSR2) and the third, is a type I receptor with one transmembrane domain (NTSR3 or sortilin). NT and NTSR1 are both implicated in tumoral progression and there are overexpressed in a lot of cancer. NT induces proliferation of cancerous cells which are mediated by NTSR1 which may transactivate the Epidermal Growth Factor Receptor (EGFR). We demonstrated that NT doesn’t transactivate the EGFR in HT29 cell line, a human adenocarcinoma of colon. NTSR3 is a multifunctional protein, is implicated in sorting of proteins, proliferation, differenciation… Moreover, once at the plasma membrane, NTSR3 can be hydrolysed and freed in a soluble form, in the extracellular medium (sNTSR3). During my PhD, I demonstrated that the sNTSR3 is an active molecule with a biological activity, as it induces the release of intracellular calcium. The sNTSR3 activates intracellular signaling like the complex FAK-Src, PKCα and Pi3K pathway, leading to an increase in cancerous cell adhesion. Furthermore, sNTSR3 increases E-Cadherin expression, space between cells and enhances the proliferation induced by EGF. Taken together, these results indicate that the soluble form of NTSR3 can be implicated in tumoral progression
Hassan, Noor. "Characterization and engineering of carbohydrate-active enzymes for biotechnological applications." Doctoral thesis, KTH, Industriell bioteknologi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-165613.
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Niemelä, Onni. "Aminoterminal propeptide of type III procollagen and basement related antigens in alcoholic liver disease." Oulu : University of Oulu, 1985. http://catalog.hathitrust.org/api/volumes/oclc/14472875.html.
Cacciatore, Angela [Verfasser], and Hans-Ruprecht [Akademischer Betreuer] Neuberger. "Prokollagen Propeptide : Marker für atriale Fibrose und Vorhofflimmern? / Angela Cacciatore. Betreuer: Hans-Ruprecht Neuberger." Saarbrücken : Saarländische Universitäts- und Landesbibliothek, 2013. http://d-nb.info/1052907148/34.
Iyappan, Saravanakumar. "The function of the beta6/Pre7 propeptide for 20S proteasome biogenesis in baker's yeast." [S.l. : s.n.], 2004. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB11612026.
Books on the topic "Propeptide de la sortiline":
Davies, Darryl. Interactions between integrins and the c-propeptide domain of fibrillar collagens. Manchester: University of Manchester, 1996.
Book chapters on the topic "Propeptide de la sortiline":
Shinde, Ujwal, and Masayori Inouye. "Propeptide-Mediated Folding in Subtilisin: The Intramolecular Chaperone Concept." In Advances in Experimental Medicine and Biology, 147–54. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0319-0_16.
Harris, Robert B., Jun ling You, Saskia C. F. Milton, Raymond C. DeLisle Milton, N. S. Rangaraju, and Christopher P. Baker. "The Role of Propeptide Hormone Protein Conformation in Limited Endoproteolysis." In Natural and Engineered Pest Management Agents, 230–48. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1994-0551.ch016.
McAlinden, Audrey, Naoshi Fukui, and Linda J. Sandell. "Type IIA procollagen NH2-propeptide functions as an antagonist of bone morphogenetic proteins." In The Many Faces of Osteoarthritis, 5–16. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8133-3_1.
Wu, Deguang, Yefu Chen, Jun Lu, Yanan Qi, Cuiying Zhang, and Dongguang Xiao. "Effect of Proteinase A Propeptide Deletion on its Enzyme Activity in Saccharomyces cerevisiae." In Proceedings of the 2012 International Conference on Applied Biotechnology (ICAB 2012), 1459–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37925-3_155.
Hartmann, D. J., J. C. Trinchet, B. Galet, P. Callard, B. Nusgens, Ch M. Lapiere, M. Beaugrand, and G. Ville. "MEASUREMENT OF SERLM PROCOLLAGEN TYPE III N-TERMINAL PROPEPTIDE IN PATIENTS WITH ALCOHOLIC LIVER DISEASE." In Proceedings of the Third Symposium, Lyon, France, June 26–28, 1985, edited by Jacques Bienvenu, J. A. Grimaud, and Philippe Laurent, 443–48. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110860757-057.
Bayer, Milan, and Vladimir Palicka. "Utilization and Reference Values of Bone Turnover Markers: Osteocalcin and Procollagen Type 1 N-Propeptide." In Biomarkers in Bone Disease, 239–52. Dordrecht: Springer Netherlands, 2017. http://dx.doi.org/10.1007/978-94-007-7693-7_37.
Bayer, Milan, and Vladimir Palicka. "Utilization and Reference Values of Bone Turnover Markers: Osteocalcin and Procollagen Type 1 N-Propeptide." In Biomarkers in Bone Disease, 1–15. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-7745-3_37-1.
Hamilton, Maureen A., and Timothy S. Charlebois. "Extracellular Propeptide Processing of Recombinant Human Factor Ix by a Secreted Form of the Endoprotease, Pace." In Animal Cell Technology, 495–501. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5404-8_79.
Dodojacek, R., G. Höfler, B. Leschnik, and W. Muntean. "A Novel Type of Mutation at the Propeptide Cleavage Site (Ala+1Thr) Causing Symptomatic Protein C Type II Deficiency." In 30th Hemophilia Symposium Hamburg 1999, 126–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-18240-2_16.
Oldenburg, J., E. M. Quenzel, U. Harbrecht, A. Fregin, W. Kress, C. R. Müller, H. J. Hertfelder, R. Schwaab, H. H. Brackmann, and P. Hanfland. "Missense Mutations at ALA-10 in the Factor IX Propeptide: A Novel Mechanism for Severe Bleeding During Oral Anticoagulant Therapy." In 27. Hämophilie-Symposion Hamburg 1996, 285–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-80403-8_43.
Conference papers on the topic "Propeptide de la sortiline":
Busby, S., K. Berkner, L. Halfpap, J. Gambee, and A. Kumar. "ALTERATION OF PROPTIDE SEQUENCE IMPAIRS BIOLOGICAL ACTIVITY OF HUMAN FACTOR VII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643784.
Jorgensen, M. J., MJ Rabiet, A. B. Cantor, B. Furie, C. L. Brown, C. B. Shoemaker, and B. C. Furie. "VITAMIN K-DEPENDENT γ-CARBOXYLATION OF FACTOR IX REQUIRES A RECOGNITION SITE CONTAINED WITHIN THE PROPEPTIDE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643564.
Zhu, Anqi, Pinyao He, Haiyan Wang, and Yunfei Chen. "Detection of the C-terminal Propeptide of Proaerolysin by Aerolysin Nanopore." In 2022 IEEE International Conference on Manipulation, Manufacturing and Measurement on the Nanoscale (3M-NANO). IEEE, 2022. http://dx.doi.org/10.1109/3m-nano56083.2022.9941648.
Foster, D., B. Schach, M. Rudisky, K. Berkner, A. Kumar, A. Kumar, C. Sprecher, F. Hagen, and E. W. Davie. "The Effect of Changes in the Leader Sequence of Human Protein C on Biosynthetic Processing and Gamma-Carboxylation." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643993.
Wellhöfer, T., H. J. Kolde, O. Tiebel, B. Krammer-Steiner, M. Steiner, and J. Lüdemann. "A New Rapid, Specific, and Simple ELISA for von Willebrand Factor Propeptide." In 63rd Annual Meeting of the Society of Thrombosis and Haemostasis Research. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1680243.
Bañares-Hidalgo, A., E. J. Cabré, F. Gil, A. Bolaños, S. Aller, B. Amor, G. Castañer, et al. "Production of recombinant forms of the propeptide COOH-terminal and the saposin B-type domain of the propeptide NH2-terminal of the precursor of pulmonary surfactant protein B." In Proceedings of the II International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2007). WORLD SCIENTIFIC, 2009. http://dx.doi.org/10.1142/9789812837554_0148.
Furis, B. C., M. J. Jorgensem, M. J. Rabiet, A. B. Contor, C. L. Brown, C. B. Shoemaker, and B. Furie. "RECOGNITION SITE DIRECTING GAMMA-CARBOXYLATION RESIDES ON THE PROPEPTIDES OF FACTOR IX AND PROTRROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643992.
Salameh, Janelle W., Charles S. Umbaugh, and Marxa L. Figueiredo. "Abstract LB-260: Development and validation of propeptide therapeutics for treating bone metastatic prostate cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-260.
Simbrunner, B., I. Villesen, B. Scheiner, DJ Bauer, R. Paternostro, P. Schwabl, A. Stättermayer, et al. "Von Willebrand Factor (VWF) propeptide levels are similarly accurate for assessing portal hypertension as compared to VWF antigen." In 54. Jahrestagung & 31. Fortbildungskurs der Österreichischen Gesellschaft für Gastroenterologie & Hepatologie – ÖGGH (Hybrid Veranstaltung). Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1734276.
Syrkis, Joanna Patrycja, Katarzyna Aleksandra Kujawa, Patrycja Jakubowska, and Katarzyna Marta Lisowska. "#817 Overexpression of lysil oxidase propeptide (LOX-PP) results in decreased proliferation and improved chemosensitivity of ovarian cancer cells." In ESGO 2023 Congress. BMJ Publishing Group Ltd, 2023. http://dx.doi.org/10.1136/ijgc-2023-esgo.652.