Relevant bibliographies by topics / Calpain

Academic literature on the topic 'Calpain'

Author: Grafiati
Published: 4 June 2021
Last updated: 22 June 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Calpain.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Calpain"

1

Chhabra, A., H. Fernando, R. E. Mansel, and W. G. Jiang. "Pattern of expression of calpain subunits (large and small) in human breast cancer and the prognostic significance." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 21078. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.21078.

Full text
Abstract:
21078 Background: Calpains belongs to family of non-lysosomal calcium dependent cysteine proteases which are known to regulate cellular migration, apoptosis and cell cycle progression in normal and tumour cells. Calpain has also been indicated in the metastatic process of certain tumours like RCC and identified as a potential tumor suppressor for gastric cancer. Little is known about the expression pattern of calpain in human breast cancer. The current study investigated the expression pattern of the large (calpainL) and small (calpainS) subunits of calpain which are encoded by different genes, in human breast cancer and attempted to correlate the expression with clinical outcome. Methods: RNA was extracted from frozen sections of breast tissue (n=120, median clinical follow up of the patients - 72 months) for gene amplification. The expression of both subunits of calpain was determined by using RT-PCR and quantitative RT-PCR. Statistical analysis was carried out using Mann- Whitney U test and the Kruskal- Wallis test. Results: We found significantly higher level of both calpain subunits in tumour tissue (n=120) as compared to normal non-neoplastic mammary tissues (calpainL, p=0.022 and calpainS, p=0.039). The expression of calpainL was significantly lower in patients with poor clinical outcome (with metastasis, p=0.024, with local recurrence, p=0.024 and who died of breast cancer, p=0.028), than those who were disease free. In contrast, the levels of calpainS were high in patients with poor prognosis, metastasis and who died of breast cancer but were statistically not significant. The expression of calpainL was marginally lower in node positive tumours than the node negative tumours. CalpainS transcripts were higher in node positive than node negative tumours (p=0.23). Similarly, calpainL showed a low level in high grade tumours whereas calpainS displayed a contrasting high level in these tumours. Conclusions: The large and small subunits of calpain have a distinct pattern of expression in human breast cancer. A decrease expression of calpainL but an increase expression of calpainS may be associated with poor prognostic tumours, thus indicating the intimate nature of the molecular pair in the disease progression of human breast cancer. No significant financial relationships to disclose.
APA, Harvard, Vancouver, ISO, and other styles
2

Upla, Paula, Varpu Marjomäki, Liisa Nissinen, Camilla Nylund, Matti Waris, Timo Hyypiä, and Jyrki Heino. "Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1." Journal of Virology 82, no. 3 (November 21, 2007): 1581–90. http://dx.doi.org/10.1128/jvi.01375-07.

Full text
Abstract:
ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in EV1 infection also was supported by the fact that EV1 increased calpain activity 3 h postinfection. Confocal microscopy and immunoelectron microscopy showed that the EV1/caveolin-1-positive vesicles also contain calpain 1 and 2. Our results indicate that calpains are not required for virus entry but that they are important at a later stage of infection. Calpain inhibitors blocked the production of EV1 particles after microinjection of EV1 RNA into the cells, and they effectively inhibited the synthesis of viral RNA in the host cells. Thus, both calpain 1 and calpain 2 are essential for the replication of EV1 RNA.
APA, Harvard, Vancouver, ISO, and other styles
3

Fontenele, Marcio, Bomyi Lim, Danielle Oliveira, Márcio Buffolo, David H. Perlman, Trudi Schupbach, and Helena Araujo. "Calpain A modulates Toll responses by limited Cactus/IκB proteolysis." Molecular Biology of the Cell 24, no. 18 (September 15, 2013): 2966–80. http://dx.doi.org/10.1091/mbc.e13-02-0113.

Full text
Abstract:
Calcium-dependent cysteine proteases of the calpain family are modulatory proteases that cleave their substrates in a limited manner. Among their substrates, calpains target vertebrate and invertebrate IκB proteins. Because proteolysis by calpains potentially generates novel protein functions, it is important to understand how this affects NFκB activity. We investigate the action of Calpain A (CalpA) on the Drosophila melanogaster IκB homologue Cactus in vivo. CalpA alters the absolute amounts of Cactus protein. Our data indicate, however, that CalpA uses additional mechanisms to regulate NFκB function. We provide evidence that CalpA interacts physically with Cactus, recognizing a Cactus pool that is not bound to Dorsal, a fly NFκB/Rel homologue. We show that proteolytic cleavage by CalpA generates Cactus fragments lacking an N-terminal region required for Toll responsiveness. These fragments are generated in vivo and display properties distinct from those of full-length Cactus. We propose that CalpA targets free Cactus, which is incorporated into and modulates Toll-responsive complexes in the embryo and immune system.
APA, Harvard, Vancouver, ISO, and other styles
4

SORIMACHI, Hiroyuki, Shoichi ISHIURA, and Koichi SUZUKI. "Structure and physiological function of calpains." Biochemical Journal 328, no. 3 (December 15, 1997): 721–32. http://dx.doi.org/10.1042/bj3280721.

Full text
Abstract:
For a long time now, two ubiquitously expressed mammalian calpain isoenzymes have been used to explore the structure and function of calpain. Although these two calpains, μ- and m-calpains, still attract intensive interest because of their unique characteristics, various distinct homologues to the protease domain of μ- and m-calpains have been identified in a variety of organisms. Some of these ‘novel’ calpain homologues are involved in important biological functions. For example, p94 (also called calpain 3), a mammalian calpain homologue predominantly expressed in skeletal muscle, is genetically proved to be responsible for limb-girdle muscular dystrophy type 2A. Tra-3, a calpain homologue in nematodes, is involved in the sex determination cascade during early development. PalB, a key gene product involved in the alkaline adaptation of Aspergillus nidulans, is the first example of a calpain homologue present in fungi. These findings indicate various important functional roles for intracellular proteases belonging to the calpain superfamily.
APA, Harvard, Vancouver, ISO, and other styles
5

Murphy, Robyn M., Rodney J. Snow, and Graham D. Lamb. "μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans." American Journal of Physiology-Cell Physiology 290, no. 1 (January 2006): C116—C122. http://dx.doi.org/10.1152/ajpcell.00291.2005.

Full text
Abstract:
μ-calpain and calpain-3 are Ca2+-dependent proteases found in skeletal muscle. Autolysis of calpains is observed using Western blot analysis as the cleaving of the full-length proteins to shorter products. Biochemical assays suggest that μ-calpain becomes proteolytically active in the presence of 2–200 μM Ca2+. Although calpain-3 is poorly understood, autolysis is thought to result in its activation, which is widely thought to occur at lower intracellular Ca2+ concentration levels ([Ca2+]i; ∼1 μM) than the levels at which μ-calpain activation occurs. We have demonstrated the Ca2+-dependent autolysis of the calpains in human muscle samples and rat extensor digitorum longus (EDL) muscles homogenized in solutions mimicking the intracellular environment at various [Ca2+] levels (0, 2.5, 10, and 25 μM). Autolysis of calpain-3 was found to occur across a [Ca2+] range similar to that for μ-calpain, and both calpains displayed a seemingly higher Ca2+ sensitivity in human than in rat muscle homogenates, with ∼15% autolysis observed after 1-min exposure to 2.5 μM Ca2+ in human muscle and almost none after 1- to 2-min exposure to the same [Ca2+]i level in rat muscle. During muscle activity, [Ca2+]i may transiently peak in the range found to autolyze μ-calpain and calpain-3, so we examined the effect of two types of exhaustive cycling exercise (30-s “all-out” cycling, n = 8; and 70% V̇o2 peak until fatigue, n = 3) on the amount of autolyzed μ-calpain or calpain-3 in human muscle. No significant autolysis of μ-calpain or calpain-3 occurred as a result of the exercise. These findings have shown that the time- and concentration-dependent changes in [Ca2+]i that occurred during concentric exercise fall near but below the level necessary to cause autolysis of calpains in vivo.
APA, Harvard, Vancouver, ISO, and other styles
6

Theopold, U., M. Pintér, S. Daffre, Y. Tryselius, P. Friedrich, D. R. Nässel, and 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 (February 1995): 824–34. http://dx.doi.org/10.1128/mcb.15.2.824.

Full text
Abstract:
Calpains are calcium-dependent proteases believed to participate in calcium-regulated signal pathways in cells. Ubiquitous calpains as well as tissue-specific calpains have been found in vertebrates. We isolated cDNA clones for a highly tissue-specific calpain gene from Drosophila melanogaster, CalpA, at 56C-D on the second chromosome. The expression of the CalpA gene product was monitored by using a specific antiserum directed against the product expressed by one cDNA clone. The encoded protein is found in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. In the blood cell line mbn-2, calpain is associated with a granular component in the cytoplasm. The expression of this protein is more restricted than that of the corresponding transcripts, which are widely distributed in the central nervous system, digestive tract, and other tissues. The sequence of CalpA is closely related to that of vertebrate calpains, but an additional segment is inserted in the calmodulin-like carboxy-terminal domain. This insert contains a hydrophobic region that may be involved in membrane attachment of the enzyme. Differential splicing also gives rise to a minor transcript that lacks the calmodulin-like domain.
APA, Harvard, Vancouver, ISO, and other styles
7

Covington, Marisa D., David D. Arrington, and Rick G. Schnellmann. "Calpain 10 is required for cell viability and is decreased in the aging kidney." American Journal of Physiology-Renal Physiology 296, no. 3 (March 2009): F478—F486. http://dx.doi.org/10.1152/ajprenal.90477.2008.

Full text
Abstract:
Aging is associated with abnormalities in kidney function, but the exact mechanisms are unknown. We examined calpains 1, 2, and 10 protein levels in kidneys from rats, mice, and humans of various ages and determined whether calpain 10 is required for cell viability. Calpain 10 protein expression decreased in the kidney, but not in the liver, of aging Fischer 344 rats, and this decrease was attenuated with caloric restriction. There was no change in calpains 1 or 2 levels in the kidney or liver in control and caloric-restricted aging rats. Aging mice also exhibited decreased calpain 10 protein levels. Calpain 10 protein and mRNA levels decreased linearly in human kidney samples with age in the absence of changes in calpains 1 or 2. Our laboratory previously found calpain 10 to be expressed in both the cytosol and mitochondria of rabbit renal proximal tubular cells (RPTC). Adenoviral-delivered shRNA to rabbit RPTC decreased mitochondrial calpain 10 expression below detectable levels by 3 days while cytosolic calpain 10 levels remained unchanged at 3 days and decreased to ∼20% of control by 5 days. Knockdown of mitochondrial calpain 10 resulted in nuclear condensation and cleaved procaspase 3, markers of apoptosis. In summary, mitochondrial calpain 10 is required for cell viability and calpain 10 levels specifically decrease in aging rat, mice, and human kidney tissues when renal function decreases, suggesting that calpain 10 is required for renal function and is a biomarker of the aging kidney.
APA, Harvard, Vancouver, ISO, and other styles
8

Arora, A. S., P. de Groen, Y. Emori, and G. J. Gores. "A cascade of degradative hydrolase activity contributes to hepatocyte necrosis during anoxia." American Journal of Physiology-Gastrointestinal and Liver Physiology 270, no. 2 (February 1, 1996): G238—G245. http://dx.doi.org/10.1152/ajpgi.1996.270.2.g238.

Full text
Abstract:
Calpain proteases contribute to hepatocyte necrosis during anoxia. Our aim was to ascertain the mechanism causing calpain activation during anoxia. In rat hepatocytes, a twofold increase in calpain activity occurred despite the lack of an increase in cytosolic Ca2+ concentration ([Ca2+]i). The increase in calpain activity was not associated with an increase in calpain mRNA or a decrease in calpastatin mRNA expression. Because phospholipid degradation products generated by phospholipases can activate calpains at physiological [Ca2+]i, we determined the effect of phospholipase inhibitors and activators on calpain activity. Pretreatment of hepatocytes with fluphenazine, a phospholipase inhibitor, decreased calpain activation and improved cell survival. Melittin, a phospholipase A2 activator, increased calpain activity and potentiated cell killing. Finally, phospholipid degradation preceded the increase in calpain activity. Thus the enhanced calpain activity occurring in hepatocytes during anoxia 1) is regulated at the posttranslational level and 2) appears to be dependent on phospholipase activity. These data suggest a novel cascade for degradative hydrolase activity during hepatocyte necrosis by anoxia with phospholipase-mediated activation of calpains.
APA, Harvard, Vancouver, ISO, and other styles
9

Sultan, Karim R., Bernd T. Dittrich, and Dirk Pette. "Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat." American Journal of Physiology-Cell Physiology 279, no. 3 (September 1, 2000): C639—C647. http://dx.doi.org/10.1152/ajpcell.2000.279.3.c639.

Full text
Abstract:
Fiber-type transitions in adult skeletal muscle induced by chronic low-frequency stimulation (CLFS) encompass coordinated exchanges of myofibrillar protein isoforms. CLFS-induced elevations in cytosolic Ca2+ could activate proteases, especially calpains, the major Ca2+-regulated cytosolic proteases. Calpain activity determined by a fluorogenic substrate in the presence of unaltered endogenous calpastatin activities increased twofold in low-frequency-stimulated extensor digitorum longus (EDL) muscle, reaching a level intermediate between normal fast- and slow-twitch muscles. μ- and m-calpains were delineated by a calpain-specific zymographical assay that assessed total activities independent of calpastatin and distinguished between native and processed calpains. Contrary to normal EDL, structure-bound, namely myofibrillar and microsomal calpains, were abundant in soleus muscle. However, the fast-to-slow conversion of EDL was accompanied by an early translocation of cytosolic μ-calpain, suggesting that myofibrillar and microsomal μ-calpain was responsible for the twofold increase in activity and thus involved in controlled proteolysis during fiber transformation. This is in contrast to muscle regeneration where m-calpain translocation predominated. Taken together, we suggest that translocation is an important step in the control of calpain activity in skeletal muscle in vivo.
APA, Harvard, Vancouver, ISO, and other styles
10

Miyazaki, Takuro. "Calpain and Cardiometabolic Diseases." International Journal of Molecular Sciences 24, no. 23 (November 26, 2023): 16782. http://dx.doi.org/10.3390/ijms242316782.

Full text
Abstract:
Calpain is defined as a member of the superfamily of cysteine proteases possessing the CysPC motif within the gene. Calpain-1 and -2, which are categorized as conventional isozymes, execute limited proteolysis in a calcium-dependent fashion. Accordingly, the calpain system participates in physiological and pathological phenomena, including cell migration, apoptosis, and synaptic plasticity. Recent investigations have unveiled the contributions of both conventional and unconventional calpains to the pathogenesis of cardiometabolic disorders. In the context of atherosclerosis, overactivation of conventional calpain attenuates the barrier function of vascular endothelial cells and decreases the immunosuppressive effects attributed to lymphatic endothelial cells. In addition, calpain-6 induces aberrant mRNA splicing in macrophages, conferring atheroprone properties. In terms of diabetes, polymorphisms of the calpain-10 gene can modify insulin secretion and glucose disposal. Moreover, conventional calpain reportedly participates in amino acid production from vascular endothelial cells to induce alteration of amino acid composition in the liver microenvironment, thereby facilitating steatohepatitis. Such multifaceted functionality of calpain underscores its potential as a promising candidate for pharmaceutical targets for the treatment of cardiometabolic diseases. Consequently, the present review highlights the pivotal role of calpains in the complications of cardiometabolic diseases and embarks upon a characterization of calpains as molecular targets.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Calpain"

1

Czerwinski, Eric Paul. "Two Proteins Containing Tandem DIII Domains, Calpain 10 and Dictyostelium Cpl, are Involved in Cytoskeletal Regulation." Connect to Online Resource-OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1193689816.

Full text
Abstract:
Dissertation (Ph.D.)--University of Toledo, 2007.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Title from title page of PDF document. Bibliography: p. 117-147.
APA, Harvard, Vancouver, ISO, and other styles
2

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.

Full text
Abstract:
Thesis (M.S.)--West Virginia University, 1999.
Title from document title page. Document formatted into pages; contains vii, 93 p. : ill. (some col.) Includes abstract. Includes bibliographical references (p. 72-80).
APA, Harvard, Vancouver, ISO, and other styles
3

Fernández-Montalván, Amaury Ernesto. "Structural requirements for activation and membrane binding of human m-calpain [mu-calpain]." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973390123.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Schroeder, Ewald. "Structural studies of #mu#-calpain, a novel calpain substrate, and a papain-leupeptin complex." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386677.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Huang, Xinhua. "DIII Domain of Calpain 10 and Cpl Towards an Understanding of Calpain 10 Function." University of Toledo Health Science Campus / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=mco1096641027.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Huang, Xinhua. "DIII domain of calpain 10 and Cpl towards an understanding of calpain 10 function /." Connect to full-text via OhioLINK ETD Center, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1096641027.

Full text
Abstract:
Thesis (Ph. D.)--Medical College of Ohio, 2003.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Medical Sciences." Major advisor: Ronald Mellgren. Includes abstract. Document formatted into pages: iv, 126 p. Title from title page of PDF document. Includes bibliographical references (p. 92-124).
APA, Harvard, Vancouver, ISO, and other styles
7

Rose, Robert Edward. "Calpain and lipopolysaccharide mediated hepatitis." Thesis, [College Station, Tex. : Texas A&M University, 2006. http://hdl.handle.net/1969.1/ETD-TAMU-1806.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Plammootil, Salma Martha. "Mutationen im Calpain-3-Gen." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973536306.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Douillard, Aymeric. "Implication des calpaïnes lors d'un remodelage musculaire induit par un traitement chronique au clenbutérol." Thesis, Montpellier 1, 2011. http://www.theses.fr/2011MON14001/document.

Full text
Abstract:
Afin de lutter efficacement contre les malversations du dopage, il apparaît essentiel de comprendre les mécanismes conduisant au remodelage musculaire. Dans ce but nous avons analysé les effets d’un β2-agoniste, le clenbutérol, sur le remodelage musculaire et les différentes voies de signalisation qui y sont associées. Nous nous sommes particulièrement intéressés au système des calpaïnes qui a souvent été associé à des phénomènes de remodelage musculaire, principalement dans des modèles d’atrophie. Nous avons montré une sollicitation précoce du système des calpaïnes lors d’un traitement chronique au clenbutérol chez le rat associé à une conversion phénotypique dans les muscles EDL et Soléaire et à une hypertrophie dans le muscle EDL uniquement. Puis, nous avons inhibé l’activité des calpaïnes en parallèle d’un traitement au clenbutérol. Les muscles ayant une activité des calpaïnes diminuée et soumis à un traitement au clenbutérol n’ont pas développé de remodelage musculaire. Ces premiers résultats renforcent l’idée d’une implication des calpaïnes dans le remodelage musculaire induit par un traitement chronique au clenbutérol
To fight doping in an effective manner, it is essential to understand the mechanisms leading to muscle remodeling. For this purpose we analyzed the effects of clenbuterol, on muscle remodeling and various associated signaling pathways. We were particularly interested with the calpain system which has often been associated with muscle remodeling phenomena, mainly in models of atrophy. We have shown that an early calpain system solicitation during chronic treatment with clenbuterol in rats was associated with a phenotypic conversion in the Soleus and EDL muscles and hypertrophy in the EDL muscle. We then inhibited the activity of calpains with a parallel clenbuterol treatment. The muscles with a reduced activity of calpain and treated with clenbuterol did not develop muscle remodeling. These initial results reinforce the idea of an involvement of calpain in the muscle remodeling induced by chronic treatment with clenbuterol
APA, Harvard, Vancouver, ISO, and other styles
10

Arthur, John Simon Campbell. "Regulation of m-calpain by phospholipids." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240569.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Calpain"

1

Messer, Jeannette S., ed. Calpain. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8988-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Elce, John S. Calpain Methods and Protocols. New Jersey: Humana Press, 2000. http://dx.doi.org/10.1385/1592590500.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

S, Elce John, ed. Calpain methods and protocols. Totowa, N.J: Humana Press, 2000.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

W, Wang Kevin K., and Yuen Po-Wai, eds. Calpain: Pharmacology and toxicology of calcium-dependent protease. Philadelphia, PA: Taylor & Francis, 1999.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

1946-, Mellgren Ronald L., and Murachi Takashi 1926-, eds. Intracellular calcium-dependent proteolysis. Boca Raton, Fla: CRC Press, 1990.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Las capillas posa de San Andrés Calpan, Puebla. [Puebla, México]: Universidad de las Américas Puebla, 1991.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Urbanismo indígena y español en el siglo XVI: El caso de Calpan. Tlalpan, México, D.F: Universidad Autónoma Metropolitana Xochimilco, División de Ciencias y Artes para el Diseño, 2012.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Public Service Commission of Wisconsin. and Wisconsin. Dept. of Natural Resources., eds. Calpine Fond du Lac Energy Center, LLC generation project. Madison, Wis: Public Service Commission of Wisconsin, 2002.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Carnio, Leanne katherine. Direct association of integrin-linked kinase with a novel calponin homology domain-containing protein, CLINT. Ottawa: National Library of Canada, 2000.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Ankara: Kara kalpaklı kent, 1923-1938 = Ankara : city of the black calpac, 1923-1938. İstanbul: İstanbul Araṣtirmalari Enstitüsü, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Calpain"

1

Nimmrich, Volker, Anton Bespalov, and Achim Möller. "Calpain." In Encyclopedia of Signaling Molecules, 678–82. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_23.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Carragher, Neil O. "Calpain." In Encyclopedia of Cancer, 1–4. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_782-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "Calpain." In Encyclopedia of Signaling Molecules, 225–28. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_23.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Carragher, Neil O. "Calpain." In Encyclopedia of Cancer, 729–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46875-3_782.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Carragher, Neil O. "Assaying Calpain Activity." In Adhesion Protein Protocols, 109–19. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-353-0_9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Ono, Yasuko, Hiroyuki Sorimachi, and Koichi Suzuki. "Calpains: structure and function of the calpain super family." In Proteases New Perspectives, 159–74. Basel: Birkhäuser Basel, 1999. http://dx.doi.org/10.1007/978-3-0348-8737-3_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Nguyen, Anh T. H., Matthew Campbell, Paul F. Kenna, Anna-Sophia Kiang, Lawrence Tam, Marian M. Humphries, and Peter Humphries. "Calpain and Photoreceptor Apoptosis." In Retinal Degenerative Diseases, 547–52. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4614-0631-0_69.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Ryu, Morin, and Toru Nakazawa. "Calcium and Calpain Activation." In Neuroprotection and Neuroregeneration for Retinal Diseases, 13–24. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54965-9_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Biswas, Ashim Kumar, and Samarth Tandon. "Casein Zymography for Analysis of Calpain-1 and Calpain-2 Activity." In Methods in Molecular Biology, 31–38. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8988-1_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Biswas, Ashim Kumar, and Samarth Tandon. "Single-Step Purification of Calpain-1, Calpain-2, and Calpastatin Using Anion-Exchange Chromatography." In Methods in Molecular Biology, 3–11. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8988-1_1.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Calpain"

1

Colman, Robert W., Harlan Bradford, and Anjanayaki Annamalai. "FACTOR V IS ACTIVATED AND CLEAVED BY PLATELET CALPAIN: COMPARISON WITH THROMBIN PROTEOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643884.

Full text
Abstract:
Platelets are known to process human and bovine factor V during secretion and/or membrane binding. We therefore studied the functional and structural changes produced in human factor V and Va by purified platelet calpain. A maximum increase in factor V coagulant activity of 2.5-fold over control incubations was observed for calpain (0.6 u/ml) at 25°C in comparison with a 10-fold increment for a thrombin (1 u/ml). Thrombin addition to reactions initiated by calpain resulted in further activation comparable to that of thrombin alone, while subsequent addition of calpain had no effect on the extent or pattern of the activation of factor V by thrombin. The cleavage pattern of factor V produced by these two enzymes are distinctly different. Calpain yields initial components of 210 kDa and 160 kDa within 1 min. Further digestion of the 210 kDa species give rise to polypeptides of 150, 140 and 120 kDa by 2 min with and increase in coagulant activity. The degradation of the 160 kDa polypeptide gives rise to smaller fragments of 130, 100, 90, and 87 kDa. Immunob lot ting of these fragments with the monoclonal antibody B10 directed to factor V and the thrombin generated Cl fragments yields results demonstrating an immunological relationship to the calpain generated components of 210, 160, 140 and 120 kDa. Thus platelet calpain generates a complex cleavage pattern different from thrombin which may explain the partial activation observed.
APA, Harvard, Vancouver, ISO, and other styles
2

Kajiwara, Y., M. Sakon, T. Tsujinaka, J. Kambayashi, T. Mori, and T. Murachi. "STUDIES ON ROLE OF CALPAIN IN PLATELET REACTION, UTILIZING NEWLY SYNTHETIZED PEPTIDE ANTAGONISTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642823.

Full text
Abstract:
The system of calpain (Ca2+-activated protease) and its inhibitor calpastatin in platelets have been well characterized in our laboratory but the role of the system has not been fully elucidated yet, though various endogenous substrates have been identified. Employing SH inhibitors as calpain antagonists, We have proposed a possible role of platelet calpain in myosin light chain (20K) phosphorylation (Biochem.Int. 6,767,1986) but more specific calpain antagonists were required to draw conclusion. Recentry, series of peptide calpain antagonists(PCAs) were syn-thetized such as Ac-Leu-Leu-Nle.al(PCA-I), Ac-Leu-Leu-Met.al(PCA-II) and Leu-Leu-Phe.CH2Cl(PCA-III)(J.Biochem.99,173,1986) and attempts were made to apply them to platelet reaction. ID50 of PCAs against platelet calpain I was as follows; PCA-I:0.04uM,PCA-II:0.luM and PCA-III:0.4uM. Thus, these antagonists were 1000 times more potent than N-ethylmaleimide(NEM), and they did not inhibit Mg2+-ATPase activity of platelet myosin B in contrast to NEM. When PCAs were applied to intact platelets, no effect was obtained against stimulus-linked proteolysis of ABP(aotin binding protein) and P235, indicating poor permeability of the antagonists across the plasma membrane. Thereby PCA was applied to lysed platelets or to permeabilized platelets. Lysed platelets suspension with 2mM EGTA, 2mM EDTA was incubated at 37 C with 32P -ATP,2mM MgCl2, 3mM CaCl2 in the presence or absence of PCA-II and proteolysis of. ABP,P235 and phosphorylation of 20K,47K were studied. The proteolysis and phosphorylation were inhibited by PCA-II in a dose-related manner. Then, PCA-II was applied to permeabilized platelet prepared by a high voltage electric charge to which acriflavine was loaded. PCA-II inhibited Ca2+ stimulated proteolysis and phosphsrylation of the permeabilized platelets likewise but no effect was obtained on Ca2+ stimulated acriflavine secretion from dense granules. These observations indicated that the proteolysis and protein phosphorylation are mediated by calpain but that these phenomena may not be related to secretory process.
APA, Harvard, Vancouver, ISO, and other styles
3

verhallen, P. F. J., E. M. Bevers, P. Comfurius, W. M. A. Linkskens, and R. F. A. Zwaal. "CALPAIN-MEDIATED CYTOSKELETAL DEGRADATION CORRELATES WITH STIMULATION OF PLATELET PROCOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642821.

Full text
Abstract:
We have shown earlier that the negatively charged phospholipid phosphatidylserine (PS), which becomes translocated from the inner surface to the outer surface of the plasma membrane upon platelet activation, is responsible for platelet procoagulant activity. Studies with erythrocytes have suggested a role for cytoskeletal proteins in the regulation of transmembrane asymmetry of PS. The possibility that platelet cytoskeletal proteins are involved in the loss of transmembrane asymmetry of PS, was explored by correlative investigations of both platelet prooagulant activity and activity of calpain, an endogenous Ca 2+ -dependent thiol-protease, known to hydrolyze major cytoskeletal proteins (e.g.: filamin, talin, myosin). Platelet procoagulant activity was assayed by determination of the prothrombinase activity under conditions at which the catalytic PS-surface was rate-limiting. Calpain-activity was monitored by the appearance of known degradation products of major cytoskeletal proteins. The following results were obtained: (1) The ability of thrombin, collagen, collagen & thrombin, or the Ca -ionophore A23187 to stimulate platelet procoagulant activity closely correlated with their ability to stimulate platelet calpain-activity (2). Generation of platelet procoagulant activity upon platelet stimulation by collagen & thrombin or by A23187 exhibited a time course identical to the development of calpain-activity. In addition, the local anesthetics dibucaine and tetracaine, shown to gradually stimulate calpain activity, were able to generate platelet procoagulant activity with a similar time course. (3) Using a Ca2+ buffering system and A23187 to equilibrate intracellular- and extracellular free Ca2+ , it was found that the Ca2+ -response relationship of both platelet calpain- and pro-coagulant-activity was identical. From these findings we conclude that the degradation of cytoskeletal proteins destroys their putative interactions with PS, enabling this lipid to participate in transbilayer movement, leading to the formation of a procoagulant outer surface of the platelet.
APA, Harvard, Vancouver, ISO, and other styles
4

Puri, R. N., F. Zhou, H. Bradford, E. J. Gustafson, R. F. Colman, and R. W. Colman. "HIGH MOLECULAR WEIGHT KININOGEN SPECIFICALLY BLOCKS THROMBIN-INDUCED AGGREGATION BY INHIBITING PLATELET CALPAIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643860.

Full text
Abstract:
We have previously shown that platelet-aggregation induced by alpha-thrombin (1.7 nM) involves complete cleavage of the surface membrane polypeptide, Mr = 100 kDa (MP 100) labeled by FSBA in intact platelets. The failure to cleave MP100 in membrane preparations or in platelets treated with metabolic inhibitors or leupeptin, suggested that thrombin was acting by activating platelet calpain. Since high molecular weight kininogen (HMWK) is the most potent plasma inhibitor of calpain(s), we now report that HMWK inhibited thrombin-induced aggregation in a dose-dependent manner over a range of plasma concentrations. HMWK did not inhibit aggregation induced by ADP, collagen, U46619, A23187 and/or PMA. In order to study the action of HMWK in a plasma environment we utilized Y-thrombin. The aggregation induced by γ-thrombin (25 nM) in washed human platelets was also inhibited by HMWK. A much higher concentration of γ - thrombin (200 nM) was required to induce similar aggregation of platelets suspended in normal plasma. In contrast, γ -thrombin (50nM) induced complete aggregation of platelets suspended in plasma completely deficient in total kininogen indicating that a kininogen was predominently responsible for the inhibitory effect of plasma. When platelets were suspended in plasma deficient only in HMWK, aggregation required 75 nMY-thrombin. When plasma deficient in HMWK was supplemented with a physiological concentration of HMWK (0.67 μM) the aggregation of suspended washed platelets was similar to that in normal plasma. Finally, we found that purified platelet calpain-2 not only exposed fibrinogen binding sites and induced platelet aggregation, but also completely cleaved MP 100 in both intact platelets and membrane preparations. We conclude: a) Thrombin-induced platelet aggregation involves the indirect proteolytic cleavage of MP100 by activating calpain-2, and b) Inhibition of thrombin-induced platelet aggregation by HMWK involves specific inactivation of platelet calpain.
APA, Harvard, Vancouver, ISO, and other styles
5

duVERLE, DAVID, ICHIGAKU TAKIGAWA, YASUKO ONO, HIROYUKI SORIMACHI, and HIROSHI MAMITSUKA. "CaMPDB: A RESOURCE FOR CALPAIN AND MODULATORY PROTEOLYSIS." In 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Okita, J. R., M. M. Frojmovic, S. Kristopeit, T. Wong, and T. J. Kunicki. "MONTREAL PLATELET SYNDROME: DECREASED ACTIVITY OF PLATELET CALPAINS ASSOCIATED WITH AGGREGATION ABNORMALITIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642822.

Full text
Abstract:
The Montreal platelet syndrome (MPS) is an inherited disorder of platelet function characterized by a) severe thrombocytopenia, b) formation of "giant" platelets upon physical or biochemical stimulation, c) spontaneous aggregation (stir-induced microaggregate formation) and d) a lack of aggregation in response to thrombin. The Bernard-Soulier syndrome (BSS) is similar to MPS in that both syndromes are characterized by "giant" platelets and an abnormal aggregation response to thrombin. BSS patients have a deficiency of specific platelet glycoproteins (GPs). From our investigations we conclude MPS patients have apparently normal amounts of major platelet GPs. However, a defect in calpains (calcium-activated neutral proteinases) was detected in MPS platelets. The specific activity of calpains was decreased by 70% (p<0.001) in the cytosolic fraction of platelets from MPS patients as compared to that of platelets from normal control donors. The calpain activity of platelets from BSS patients was within the normal range.During the course of the biochemical studies, platelets from the MPS patients were shown to exhibit concurrent functional defects, i.e., stir-induced spontaneous aggregation and reduced to absent aggregation response to thrombin. It is concluded that MPS can be distinguished from BSS at the molecular level as follows: 1) MPS platelets contain normal amounts of GPs Ib, V and IX which are decreased or absent in BSS platelets; 2) The specific activity of calpains is reduced in MPS platelets but normal in BSS platelets. Supported by NIH (HL-33925, HL-32279), Amer. Heart Assoc. (85—GA—67, 83-186), Canadian Med. Res. Council (248-59) and Quebec Heart Fndn.
APA, Harvard, Vancouver, ISO, and other styles
7

Supinski, Gerald S., Lin Wang, Alexander Alimov, Xiao-Hong Song, and Leigh Ann P. Callahan. "CPLA2 Modulates Cytokine Induced Superoxide Generation And Calpain Activation." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a2715.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Ryan, Dorothy M., Emer P. Reeves, Noel G. McElvaney, and Shane J. O'Neill. "Secretory Leukoprotease Inhibitor Regulates Neutrophil Chemotaxis Via Calpain Inhibition." 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.a2804.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Berkowitz, S. D., H. Nozaki, K. Titani, T. Murachi, and T. S. Zimmerman. "CALPAIN AND ELASTASE ARE NOT RESPONSIBLE FOR THE VON WILLEBRAND FACTOR FRAGMENTS IN NORMAL PLASMA AND IIA VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644103.

Full text
Abstract:
Recent evidence suggests that proteolysis plays an important role in some forms of inherited and acquired von Willebrand disease (vWD). Using monoclonal epitope mapping, we have examined the proteolysis of the von Willebrand factor (vWF) subunit with platelet calcium activated neutral protease (CANP) and human leukocyte elastase and found that they are not responsible for the proteolytic cleavage sejen in normal individuals and IIA vWD. Previously we have shown that in vivo proteolysis of vWF is a normal event with a small but consistent proportion of plasma vWF being composed of 189, 176, and 140 kD fragments cleaved from the 225 kD subunit. In IIA vWD the proportion of cleaved vWF is increased. Because calcium activated neutral protease (CANP, calpain) and one or more enzymes released from polymorphonuclear leukocytes are known to proteolyze vWF in vitro with resultant loss of large multimers similar to that seen in IIA vWD, they have been suggested as being responsible for the proteolysis in vivo. We have now digested highly purified vWF with porcine CANP I and II and performed monoclonal epitope mapping on the resulting fragments. We found no difference in the size, location, and quantity of the fragments produced by calpain I versus calpain II. New fragments were detected of approximately 200, 170, 150, and 125 kD. There was no evidence for generation of the native fragments. Mapping of the 170 and 150 kD calpain-cleaved fragments revealed them to be from different parts of the molecule than the native 176 and 140 kD fragments. Digestion of vWF with human leukocyte elastase produced new fragments at 210/205, 190, 165, 145/140, and 130/125 kD. No generation of native fragments was detected. Monoclonal epitope mapping of the 190 and 145/140 kD elastase-cleaved bands proved that they come from opposite ends of the vWF molecule than the native 189 and 140 kD fragments, respectively. Therefore, CANP and human leukocyte elastase do not produce the proteolyzed fragments present in normal and IIA vWD and probably do not cause the loss of large multimers seen in that disorder.
APA, Harvard, Vancouver, ISO, and other styles
10

Ma, J., J. A. Voynow, A. Kummarapurugu, S. Ghosh, and A. Hawkridge. "Neutrophil Elastase Mediates Macrophage Phagocytic Failure Via Increased Calpain Activity." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7447.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Calpain"

1

Mudryj, Maria. Calpain-Dependent Proteolysis of the Androgen Receptor. Fort Belvoir, VA: Defense Technical Information Center, November 2009. http://dx.doi.org/10.21236/ada517269.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Kim, Yuan, Edward M. Steadham, Steven M. Lonergan, and Elisabeth J. Huff-Lonergan. Antioxidant Capacity of Calcium Lactate on m-Calpain Activity In Vitro. Ames (Iowa): Iowa State University, January 2009. http://dx.doi.org/10.31274/ans_air-180814-1237.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Tagliarino, Collen, and David A. Boothman. Exploiting an NQ01-Directed, Calpain-Medicated Apoptotic Pathway for Breast Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, October 2001. http://dx.doi.org/10.21236/ada398218.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Maddock, K. R., Elisabeth J. Huff-Lonergan, and Steven M. Lonergan. The Effect of pH on µ-calpain Activity and Implications in Meat Tenderness. Ames (Iowa): Iowa State University, January 2005. http://dx.doi.org/10.31274/ans_air-180814-1109.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Anderson, Mark J., Kathy T. Y. Mou, Cassie Gregorich, Edward M; Steadham, Steven M. Lonergan, and Elisabeth J. Huff-Lonergan. Proteolysis, Calpastatin Activity, and µ-Calpain Autolysis in Specific Muscles from the Beef Round. Ames (Iowa): Iowa State University, January 2008. http://dx.doi.org/10.31274/ans_air-180814-1234.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Herradón, Bernardo. Calpaína y sus inhibidores. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), July 2011. http://dx.doi.org/10.18567/sebbmdiv_anc.2011.07.1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Calpain' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography