Littérature scientifique sur le sujet « Calpain system »
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Articles de revues sur le sujet "Calpain system"
GOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI et JINYANG CONG. « The Calpain System ». Physiological Reviews 83, no 3 (juillet 2003) : 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.
Texte intégralTheopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässel et D. Hultmark. « CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells. » Molecular and Cellular Biology 15, no 2 (février 1995) : 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.
Texte intégralFontenele, Marcio, Bomyi Lim, Danielle Oliveira, Márcio Buffolo, David H. Perlman, Trudi Schupbach et Helena Araujo. « Calpain A modulates Toll responses by limited Cactus/IκB proteolysis ». Molecular Biology of the Cell 24, no 18 (15 septembre 2013) : 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.
Texte intégralGoll, Darrel E., Valery F. Thompson, Richard G. Taylor et Ahmed Ouali. « The calpain system and skeletal muscle growth ». Canadian Journal of Animal Science 78, no 4 (1 décembre 1998) : 503–12. http://dx.doi.org/10.4141/a98-081.
Texte intégralIlian, M. A., et N. E. Forsberg. « Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits ». Biochemical Journal 287, no 1 (1 octobre 1992) : 163–71. http://dx.doi.org/10.1042/bj2870163.
Texte intégralPánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman et Ana María Salazar. « TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes ». Journal of Molecular Endocrinology 65, no 3 (octobre 2020) : 45–57. http://dx.doi.org/10.1530/jme-19-0253.
Texte intégralMiller, John A., Domenica E. Drouet, Leonid M. Yermakov, Mahmoud S. Elbasiouny, Fatima Z. Bensabeur, Michael Bottomley et Keiichiro Susuki. « Distinct Changes in Calpain and Calpastatin during PNS Myelination and Demyelination in Rodent Models ». International Journal of Molecular Sciences 23, no 23 (6 décembre 2022) : 15443. http://dx.doi.org/10.3390/ijms232315443.
Texte intégralWeber, Jonasz J., Eva Haas, Yacine Maringer, Stefan Hauser, Nicolas L. P. Casadei, Athar H. Chishti, Olaf Riess et Jeannette Hübener-Schmid. « Calpain-1 ablation partially rescues disease-associated hallmarks in models of Machado-Joseph disease ». Human Molecular Genetics 29, no 6 (21 janvier 2020) : 892–906. http://dx.doi.org/10.1093/hmg/ddaa010.
Texte intégralMellgren, Ronald L., et Xinhua Huang. « Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair ». Journal of Biological Chemistry 282, no 49 (17 octobre 2007) : 35868–77. http://dx.doi.org/10.1074/jbc.m706929200.
Texte intégralBevers, Matthew B., et Robert W. Neumar. « Mechanistic Role of Calpains in Postischemic Neurodegeneration ». Journal of Cerebral Blood Flow & ; Metabolism 28, no 4 (12 décembre 2007) : 655–73. http://dx.doi.org/10.1038/sj.jcbfm.9600595.
Texte intégralThèses sur le sujet "Calpain system"
Janardhanan, Anitha C. « Gene expression of components of the calpain system m-calpain, [mu]-calpain and calpastatin in male and female broiler skeletal muscle / ». Morgantown, W. Va. : [West Virginia University Libraries], 1999. http://etd.wvu.edu/templates/showETD.cfm?recnum=895.
Texte intégralTitle from document title page. Document formatted into pages; contains vii, 93 p. : ill. (some col.) Includes abstract. Includes bibliographical references (p. 72-80).
Drouet, Saltos Domenica Elizabeth. « Calpain-Calpastatin System in Peripheral Nerve Myelination and Demyelination ». Wright State University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=wright1559220437439116.
Texte intégralJones, Simon W. « Fibre-type specific expression of the calpain proteolytic system in skeletal muscle ». Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312237.
Texte intégralDelgado, Eduardo Francisquine. « The calpain system and postmortem tenderization in ovine meat from callipyge and normal phenotypes ». Diss., The University of Arizona, 1998. http://hdl.handle.net/10150/288910.
Texte intégralCataldo, Francesca. « Role of calpain in USP1 stability regulation and genome integrity maintenance ». Doctoral thesis, Università degli studi di Trieste, 2012. http://hdl.handle.net/10077/7860.
Texte intégralThe calpains are a family of intracellular cysteine proteases, among which the best studied isoforms, micro- (CAPN1) and milli-calpain (CAPN2), are heterodimers consisting of a catalytic subunit and a common regulatory subunit, CAPNS1, required for function. Calpain is involved in many processes important for cancer biology, such as autophagy, indeed in calpain-depleted cells autophagy is impaired, with a subsequent increase in apoptosis sensitivity. Calpain is also important in all the stages of the stress response. A proteomic approach was employed for the identification of novel CAPNS1 interacting proteins. Proteins immunoprecipitating with endogenous CAPNS1 in HT1080 cell lysates were analyzed by Mass Spectrometry. We identified novel partners among which the deubiquitinating enzyme USP1, a key regulator of the DNA damage response and genome integrity maintenance via its specific action on FANCD2, involved in DNA repair and protection from chromosome instability, and PCNA, involved in the regulation of translesion DNA synthesis (TLS), that bypasses DNA lesions with low stringency basepairing requirements. We performed co-IP assays in lysates of 293T cells and confirmed that the interaction was specific. Furhermore, we observed that calpain is able to bind a USP1 C-terminal deleted mutant, suggesting that USP1 first 523 aminoacids were sufficient for the binding. To understand what is the effect exerted by calpain upon USP1, we depleted calpain activity in a series of cell lines, and followed the fate of endogenous USP1. We transfected CAPNS1 specific siRNAs, or treated cells with a specific inhibitor of calpain, and we observed a strong decrease in USP1 protein levels. This effect should be at a post-transcriptional level, since any significant change in USP1 mRNA levels is detected. We also obtained the same result by transfecting a siRNA specific for CAPN1, the gene encoding for the catalytic subunit micro-calpain. Moreover, we studied the role of calpain in the PCNA-mediated switch between high fidelity replication and TLS upon UV irradiation. In mouse embryonic fibroblasts knockout for CAPNS1, USP1 downregulation is coupled to an increase in PCNA monoubiquitination. Moreover, CAPNS1-depleted U2OS cells showed an increase in the percentage of nuclei containing PCNA-induced foci upon UV irradiation. Since we demonstrated that calpain can modulate an important regulator of DNA damage response such as USP1, we investigated if calpain could have a role in genome integrity maintenance. CAPNS1 depleted cells showed a reduced rescue in DNA repair compared to control cells, suggesting that increased levels in PCNA monoubiquitination could lead to an increased amount of errore-prone TLS. Calpain plays an important role in autophagy, so we asked if USP1 degradation in absence of calpain activity could involve autophagic pathways. We first blocked macroautophagy by silencing ATG5, and we observed that USP1 was downregulated, suggesting that the depletion of ATG5 could lead to an increased activity of other degradation pathways. To impaire chaperone-mediated autophagy (CMA), we silenced a protein important for autophagosome formation, LAMP-2A. Also in this case we observed a decrease in USP1 protein levels, thus suggesting that USP1 is alternatively degraded by different pathways. However, we observed that USP1 is stabilized upon inhibition of lysosomal enzymes, suggesting that USP1 may be degraded in the lysosome. To better understand the mechanism by which calpain affect USP1 stability we search for an effect of calpain upon USP1 co-factor and activator UAF1/WDR48. CAPNS1-depleted cells showed WDR48 downregulation, but WDR48 overexpression only partially rescue USP1 protein levels in this cells. Furthermore, we provided evidences that calpain regulation of p35/p25 activator of Cdk5 can affect Cdh1 phosphorylation and thus APC/Cdh1 activity, leading to a regulation of USP1 stabilization. In conclusion, we identified USP1 as a novel interactor of calpain, and we found that calpain is important for USP1 stability, since in its absence USP1 is downregulated. The importance of this novel regulation is strengthened by the recent findings that unveiled a role of USP1 in maintenance of a mesenchymal stem cell program in osteosarcoma, and thus placing calpain in a crucial regulatory position for cancer development.
XXIV Ciclo
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Li, Liang. « The role of calpain-calpastatin system in in the SOD1G93A mouse model of amyotrophic lateral sclerosis ». Thesis, University of Brighton, 2009. https://research.brighton.ac.uk/en/studentTheses/e0f03b52-5ddc-42cc-b769-ccde3e69e709.
Texte intégralAmini, Mandana. « Analysis of Conditional Knock-out of Calpain Small Subunit, capns1, in Central Nervous System Development and Function ». Thesis, Université d'Ottawa / University of Ottawa, 2014. http://hdl.handle.net/10393/31360.
Texte intégralKloock, Simon Johannes [Verfasser]. « Einfluss von VDAC1 auf das Calpain-System als mögliche therapeutische Option für Morbus Huntington / Simon Johannes Kloock ». Tübingen : Universitätsbibliothek Tübingen, 2020. http://d-nb.info/1224882385/34.
Texte intégralHoward, Benjamin. « Effects of Implanting Strategy and Zilpaterol Hydrochloride on the Calpain Proteolytic System in Sectioned Beef Steaks for Two Time Periods ». Thesis, North Dakota State University, 2016. https://hdl.handle.net/10365/28128.
Texte intégralLee, Hannah Yun Young. « Calcium homeostasis in lens transparency and the involmement of calpains in cataract ». Lincoln University, 2006. http://hdl.handle.net/10182/1897.
Texte intégralLivres sur le sujet "Calpain system"
Purintrapiban, Juntipa. Coordination of protease systems on muscle protein degradation and identification of calpain substrates using the yeast two-hybrid system. 1999.
Trouver le texte intégralChapitres de livres sur le sujet "Calpain system"
Samanta, Krishna, Pulak Kar, Tapati Chakraborti et Sajal Chakraborti. « An Overview of Endoplasmic Reticulum Calpain System ». Dans Proteases in Health and Disease, 3–19. New York, NY : Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9233-7_1.
Texte intégralMurachi, Takashi, Toshio Murakami, Michiko Ueda, Ichiro Fukui, Takao Hamakubo, Yoshifumi Adachi et Masakazu Hatanaka. « The Calpain-Calpastatin System in Hematopoietic Cells ». Dans Calcium Protein Signaling, 445–54. Boston, MA : Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_47.
Texte intégralWitkowski, Jacek M., Anna Mikosik, Ewa Bryl et Tamas Fulop. « Calpain-Calpastatin System in Lymphoid Neoplasm of the Aged ». Dans Geriatric Oncology, 1–12. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-44870-1_70-1.
Texte intégralWitkowski, Jacek M., Anna Mikosik, Ewa Bryl et Tamas Fulop. « Calpain-Calpastatin System in Lymphoid Neoplasm of the Aged ». Dans Geriatric Oncology, 129–40. Cham : Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-319-57415-8_70.
Texte intégralAshraf, Javaria, Jamil Ahmad et Zaheer Ul-Haq. « Deciphering the Role of PKC in Calpain-CAST System Through Formal Modeling Approach ». Dans Bioinformatics and Biomedical Engineering, 60–71. Cham : Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-17938-0_6.
Texte intégralRay, S. K., M. K. Guyton, E. A. Sribnick et N. L. Banik. « Calpain as a Target for Prevention of Neuronal Death in Injuries and Diseases of the Central Nervous System ». Dans Handbook of Neurochemistry and Molecular Neurobiology, 445–67. Boston, MA : Springer US, 2007. http://dx.doi.org/10.1007/978-0-387-30379-6_15.
Texte intégralLiang, Zhe, et Hilde-Gunn Opsahl-Sorteberg. « Use of the β-Glucuronidase (GUS) Reporter System to Localize Promoter Activities of the Endogenous Plant Calpain DEFECTIVE KERNEL1 (DEK1) ». Dans Methods in Molecular Biology, 103–8. New York, NY : Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8988-1_9.
Texte intégralParameswaran, Sreejit, Sujeet Kumar et Rajendra K. Sharma. « Role of Calpains in Calmodulin Regulated Systems ». Dans Proteases in Health and Disease, 33–48. New York, NY : Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-9233-7_3.
Texte intégralLuo, Y., D. F. Sellitti et K. Suzuki. « The Calpain Proteolytic System ». Dans Encyclopedia of Cell Biology, 670–80. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-12-394447-4.10075-6.
Texte intégralBaudry, Michel, Wenyue Su et Xiaoning Bi. « The Calpain Proteolytic System ». Dans Reference Module in Life Sciences. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-821618-7.00223-6.
Texte intégralActes de conférences sur le sujet "Calpain system"
Kajiwara, Y., M. Sakon, T. Tsujinaka, J. Kambayashi, T. Mori et T. Murachi. « STUDIES ON ROLE OF CALPAIN IN PLATELET REACTION, UTILIZING NEWLY SYNTHETIZED PEPTIDE ANTAGONISTS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642823.
Texte intégralverhallen, P. F. J., E. M. Bevers, P. Comfurius, W. M. A. Linkskens et R. F. A. Zwaal. « CALPAIN-MEDIATED CYTOSKELETAL DEGRADATION CORRELATES WITH STIMULATION OF PLATELET PROCOAGULANT ACTIVITY ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642821.
Texte intégralduVERLE, DAVID, ICHIGAKU TAKIGAWA, YASUKO ONO, HIROYUKI SORIMACHI et HIROSHI MAMITSUKA. « CaMPDB : A RESOURCE FOR CALPAIN AND MODULATORY PROTEOLYSIS ». Dans Proceedings of the 9th Annual International Workshop on Bioinformatics and Systems Biology (IBSB 2009). IMPERIAL COLLEGE PRESS, 2010. http://dx.doi.org/10.1142/9781848165786_0017.
Texte intégralVerhaagen, Don, Katie Hausman et Emily Saopraseuth. « Calpine Improves Accuracy of Steam Flow Measurement With Top-Mounted Annubar Flowmeter ». Dans ASME 2013 Power Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/power2013-98176.
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