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Artykuły w czasopismach na temat „Calpain 2”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 13 lutego 2022

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1

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.

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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 E

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2

Wang, Yubin, Yan Liu, Xiaoning Bi, and Michel Baudry. "Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death." Cells 9, no. 12 (December 16, 2020): 2698. http://dx.doi.org/10.3390/cells9122698.

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Calpains are a family of soluble calcium-dependent proteases that are involved in multiple regulatory pathways. Our laboratory has focused on the understanding of the functions of two ubiquitous calpain isoforms, calpain-1 and calpain-2, in the brain. Results obtained over the last 30 years led to the remarkable conclusion that these two calpain isoforms exhibit opposite functions in the brain. Calpain-1 activation is required for certain forms of synaptic plasticity and corresponding types of learning and memory, while calpain-2 activation limits the extent of plasticity and learning. Calpain

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3

Ben-Aharon, Irit, Paula R. Brown, Nir Etkovitz, Edward M. Eddy, and Ruth Shalgi. "The expression of calpain 1 and calpain 2 in spermatogenic cells and spermatozoa of the mouse." Reproduction 129, no. 4 (April 2005): 435–42. http://dx.doi.org/10.1530/rep.1.00255.

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There is some evidence suggesting that Ca2+is involved in processes that occur during the development and function of spermatozoa. Calcium-dependent proteins, such as calmodulin, are expressed during mammalian spermatogenesis further suggesting that Ca2+takes part in its regulation. However, the precise roles of Ca2+in spermatogenesis remain to be elucidated. Calpains are a family of Ca2+-dependent cysteine proteases whose members are expressed ubiquitously or in a tissue-specific manner. Calpain has been demonstrated to mediate specific Ca2+-dependent processes including cell fusion, mitosis

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4

Baudry, Michel. "Calpain-1 and Calpain-2 in the Brain: Dr. Jekill and Mr Hyde?" Current Neuropharmacology 17, no. 9 (August 22, 2019): 823–29. http://dx.doi.org/10.2174/1570159x17666190228112451.

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While the calpain system has now been discovered for over 50 years, there is still a paucity of information regarding the organization and functions of the signaling pathways regulated by these proteases, although calpains play critical roles in many cell functions. Moreover, calpain overactivation has been shown to be involved in numerous diseases. Among the 15 calpain isoforms identified, calpain-1 (aka &#181;-calpain) and calpain-2 (aka m-calpain) are ubiquitously distributed in most tissues and organs, including the brain. We have recently proposed that calpain-1 and calpain- 2 play op

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5

McCartney, Christian-Scott E., Qilu Ye, Robert L. Campbell, and Peter L. Davies. "Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide." Journal of Biological Chemistry 293, no. 46 (September 25, 2018): 17716–30. http://dx.doi.org/10.1074/jbc.ra118.004803.

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Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit–containing calpain-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain. It also has two unique insertion sequences (ISs) not found in the other calpains: IS1 within calpain-3's protease core and IS2 just prior to the penta-EF-hand domain. Production of either native or recombinant full-length calpain-3 to characterize the fun

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6

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.

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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

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7

Muniappan, Latha, Michihiro Okuyama, Aida Javidan, Devi Thiagarajan, Weihua Jiang, Jessica J. Moorleghen, Lihua Yang, et al. "Inducible Depletion of Calpain-2 Mitigates Abdominal Aortic Aneurysm in Mice." Arteriosclerosis, Thrombosis, and Vascular Biology 41, no. 5 (May 5, 2021): 1694–709. http://dx.doi.org/10.1161/atvbaha.120.315546.

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Objective: Cytoskeletal structural proteins maintain cell structural integrity by bridging extracellular matrix with contractile filaments. During abdominal aortic aneurysm (AAA) development, (1) aortic medial degeneration is associated with loss of smooth muscle cell integrity and (2) fibrogenic mesenchymal cells mediate extracellular matrix remodeling. Calpains cleave cytoskeletal proteins that maintain cell structural integrity. Pharmacological inhibition of calpains exert beneficial effects on Ang II (angiotensin II)–induced AAAs in LDLR −/− (low-density receptor deficient) mice. Here, we

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8

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

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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 aut

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9

Piper, Ann-Katrin, Reece A. Sophocleous, Samuel E. Ross, Frances J. Evesson, Omar Saleh, Adam Bournazos, Joe Yasa, et al. "Loss of calpains-1 and -2 prevents repair of plasma membrane scrape injuries, but not small pores, and induces a severe muscular dystrophy." American Journal of Physiology-Cell Physiology 318, no. 6 (June 1, 2020): C1226—C1237. http://dx.doi.org/10.1152/ajpcell.00408.2019.

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The ubiquitous calpains, calpain-1 and -2, play important roles in Ca2+-dependent membrane repair. Mechanically active tissues like skeletal muscle are particularly reliant on mechanisms to repair and remodel membrane injury, such as those caused by eccentric damage. We demonstrate that calpain-1 and -2 are master effectors of Ca2+-dependent repair of mechanical plasma membrane scrape injuries, although they are dispensable for repair/removal of small wounds caused by pore-forming agents. Using CRISPR gene-edited human embryonic kidney 293 (HEK293) cell lines, we established that loss of both

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10

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.

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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

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11

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.

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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 act

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12

Ilian, M. A., and 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 (October 1, 1992): 163–71. http://dx.doi.org/10.1042/bj2870163.

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To investigate the role of calpains in myofibrillar protein degradation in skeletal muscle and the regulation of their activity in vivo, we studied the effects of fasting on gene expression of calpains and calpastatin in the skeletal muscle of rabbits. In response to fasting, myofibrillar protein degradation increased 2-fold and mRNA levels of calpain I, calpain II and calpastatin were also increased. However, calpain and calpastatin activities remained unchanged. To investigate this discrepancy, we analysed polysomal calpain mRNA. Results indicated that fasting caused a 2-fold increase in the

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13

Montgomery, Darrice S., Ling Yu, Zinah M. Ghazi, Tiffany L. Thai, Otor Al-Khalili, He-Ping Ma, Douglas C. Eaton, and Abdel A. Alli. "ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins." American Journal of Physiology-Cell Physiology 313, no. 1 (July 1, 2017): C42—C53. http://dx.doi.org/10.1152/ajpcell.00244.2016.

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We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca2+-dependent cysteine proteases involved in signal transduction. Here we examine the role of calpain-2 in regulating MARCKS and ENaC in cultured renal epithelial cells and in the mouse kidney. Using recombinant fusion proteins, we show that MARCKS, but not

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Pánico, Pablo, Marcia Hiriart, Patricia Ostrosky-Wegman, and Ana María Salazar. "TUG is a calpain-10 substrate involved in the translocation of GLUT4 in adipocytes." Journal of Molecular Endocrinology 65, no. 3 (October 2020): 45–57. http://dx.doi.org/10.1530/jme-19-0253.

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The calpain-10 (CAPN10) protease is implicated in the translocation of the glucose transporter 4 (GLUT4), which is retained in the Golgi matrix via the Tether containing a UBX domain for GLUT4 (TUG) protein. Insulin stimulation induces the proteolytic processing of TUG, which leads to the translocation of GLUT4 to the cell membrane. We tested whether TUG is a CAPN10 substrate. Proteolysis of TUG by calpains was assessed using a cell-free system containing calpain-1 and TUG. In situ proteolysis of TUG by calpains was demonstrated in 3T3-L1 adipocytes in the presence of insulin or calpain inhibi

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15

Vermaelen, Marianne, Pascal Sirvent, Fabrice Raynaud, Catherine Astier, Jacques Mercier, Alain Lacampagne, and Olivier Cazorla. "Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy." American Journal of Physiology-Cell Physiology 292, no. 5 (May 2007): C1723—C1731. http://dx.doi.org/10.1152/ajpcell.00398.2006.

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Calpains have been proposed to be involved in the cytoskeletal remodeling and wasting of skeletal muscle. However, limited data are available about the specific involvement of each calpain in the early stages of muscle atrophy. The aims of this study were to determine whether calpains 1 and 2 are autolyzed after a short period of muscle disuse, and, if so, where in the myofibers the autolyzed products are localized. In the rat soleus muscle, 5 days of immobilization increased autolyzed calpain 1 in the particulate and not the soluble fraction. Conversely, autolyzed calpain 2 was not found in t

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16

Moshal, Karni S., Mahavir Singh, Utpal Sen, Dorothea Susanne E. Rosenberger, Brooke Henderson, Neetu Tyagi, Hong Zhang, and Suresh C. Tyagi. "Homocysteine-mediated activation and mitochondrial translocation of calpain regulates MMP-9 in MVEC." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 6 (December 2006): H2825—H2835. http://dx.doi.org/10.1152/ajpheart.00377.2006.

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Hyperhomocysteinemia (HHcy) is associated with atherosclerosis, stroke, and dementia. Hcy causes extracellular matrix remodeling by the activation of matrix metalloproteinase-9 (MMP-9), in part, by inducing redox signaling and modulating the intracellular calcium dynamics. Calpains are the calcium-dependent cysteine proteases that are implicated in mitochondrial damage via oxidative burst. Mitochondrial abnormalities have been identified in HHcy. The mechanism of Hcy-induced extracellular matrix remodeling by MMP-9 activation via mitochondrial pathway is largely unknown. We report a novel role

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17

Liu, Xiuli, Juanita J. Rainey, Jay F. Harriman, and Rick G. Schnellmann. "Calpains mediate acute renal cell death: role of autolysis and translocation." American Journal of Physiology-Renal Physiology 281, no. 4 (October 1, 2001): F728—F738. http://dx.doi.org/10.1152/ajprenal.2001.281.4.f728.

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The goals of this study were to determine 1) the expression of calpain isoforms in rabbit renal proximal tubules (RPT); 2) calpain autolysis and translocation, and calpastatin levels during RPT injury; and 3) the effect of a calpain inhibitor (PD-150606) on calpain levels, mitochondrial function, and ion transport during RPT injury. RT-PCR, immunoblot analysis, and FITC-casein zymography demonstrated the presence of only μ- and m-calpains in rabbit RPT. The mitochondrial inhibitor antimycin A decreased RPT μ- and m-calpain and calpastatin levels in conjunction with cell death and increased pla

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Seremwe, Mutsa, Rick G. Schnellmann, and Wendy B. Bollag. "Calpain-10 Activity Underlies Angiotensin II-Induced Aldosterone Production in an Adrenal Glomerulosa Cell Model." Endocrinology 156, no. 6 (June 1, 2015): 2138–49. http://dx.doi.org/10.1210/en.2014-1866.

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Abstract Aldosterone is a steroid hormone important in the regulation of blood pressure. Aberrant production of aldosterone results in the development and progression of diseases including hypertension and congestive heart failure; therefore, a complete understanding of aldosterone production is important for developing more effective treatments. Angiotensin II (AngII) regulates steroidogenesis, in part through its ability to increase intracellular calcium levels. Calcium can activate calpains, proteases classified as typical or atypical based on the presence or absence of penta-EF-hands, whic

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Hata, Shoji, Naoko Doi, Fujiko Kitamura, and Hiroyuki Sorimachi. "Stomach-specific Calpain, nCL-2/Calpain 8, Is Active without Calpain Regulatory Subunit and Oligomerizes through C2-like Domains." Journal of Biological Chemistry 282, no. 38 (July 23, 2007): 27847–56. http://dx.doi.org/10.1074/jbc.m703168200.

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Calpains constitute a family of intracellular Ca2+-regulated cysteine proteases that are indispensable in the regulation of a wide variety of cellular functions. The improper activation of calpain causes lethality or various disorders, such as muscular dystrophies and tumor formation. nCL-2/calpain 8 is predominantly expressed in the stomach, where it appears to be involved in membrane trafficking in the gastric surface mucus cells (pit cells). Although the primary structure of nCL-2 is quite similar to that of the ubiquitous m-calpain large subunit, the enzymatic properties of nCL-2 have neve

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Ou, B. R., and N. E. Forsberg. "Determination of skeletal muscle calpain and calpastatin activities during maturation." American Journal of Physiology-Endocrinology and Metabolism 261, no. 6 (December 1, 1991): E677—E683. http://dx.doi.org/10.1152/ajpendo.1991.261.6.e677.

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Our objectives were to characterize events underlying changes in skeletal muscle calpain and calpastatin activities, using maturation as a model. Muscle samples were taken from rabbits of four ages (newborn and 1, 2, and 5 mo old). Concentrations of RNA and protein and activities of calpains I and II and calpastatin were determined. Steady-state concentrations of mRNAs encoding calpain I, calpain II, calpastatin, alpha- and beta-tubulin, and beta-actin were determined using Northern blot analysis. Calpain and calpastatin activities declined markedly between birth and 1 mo of age and remained u

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Lee, Wing-Kee, Blazej Torchalski, and Frank Thévenod. "Cadmium-induced ceramide formation triggers calpain-dependent apoptosis in cultured kidney proximal tubule cells." American Journal of Physiology-Cell Physiology 293, no. 3 (September 2007): C839—C847. http://dx.doi.org/10.1152/ajpcell.00197.2007.

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A major target of cadmium (Cd2+) toxicity is the kidney proximal tubule (PT) cell. Cd2+-induced apoptosis of PT cells is mediated by sequential activation of calpains at 3–6 h and caspases-9 and -3 after 24-h exposure. Calpains also partly contribute to caspase activation, which emphasizes the importance of calpains for PT apoptosis by Cd2+. Upstream processes underlying Cd2+-induced calpain activation remain unclear. We describe for the first time that 10–50 μM Cd2+ causes a significant increase in ceramide formation by ∼22% (3 h) and ∼72% (24 h), as measured by diacylglycerol kinase assay. I

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Laajala, Mira, Minna M. Hankaniemi, Juha A. E. Määttä, Vesa P. Hytönen, Olli H. Laitinen, and Varpu Marjomäki. "Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein." Viruses 11, no. 12 (November 28, 2019): 1106. http://dx.doi.org/10.3390/v11121106.

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Enteroviruses are small RNA viruses that cause diseases with various symptoms ranging from mild to severe. Enterovirus proteins are translated as a single polyprotein, which is cleaved by viral proteases to release capsid and nonstructural proteins. Here, we show that also cellular calpains have a potential role in the processing of the enteroviral polyprotein. Using purified calpains 1 and 2 in an in vitro assay, we show that addition of calpains leads to an increase in the release of VP1 and VP3 capsid proteins from P1 of enterovirus B species, detected by western blotting. This was prevente

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Douillard, Aymeric, Olivier Galbes, Bernadette Rossano, Barbara Vernus, Anne Bonnieu, Robin Candau, and Guillaume Py. "Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment." Canadian Journal of Physiology and Pharmacology 89, no. 2 (February 2011): 117–25. http://dx.doi.org/10.1139/y10-114.

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Calpains are Ca2+ cysteine proteases that have been proposed to be involved in the cytoskeletal remodeling and wasting of skeletal muscle. Cumulative evidence also suggests that β2-agonists can lead to skeletal muscle hypertrophy through a mechanism probably related to calcium-dependent proteolytic enzyme. The aim of our study was to monitor calpain activity as a function of clenbuterol treatment in both slow and fast phenotype rat muscles. For this purpose, for 21 days we followed the time course of the calpain activity and of the ubiquitous calpain 1 and 2 autolysis, as well as muscle remode

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GOLL, DARREL E., VALERY F. THOMPSON, HONGQI LI, WEI WEI, and JINYANG CONG. "The Calpain System." Physiological Reviews 83, no. 3 (July 2003): 731–801. http://dx.doi.org/10.1152/physrev.00029.2002.

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Goll, Darrel E., Valery F. Thompson, Hongqi Li, Wei Wei, and Jinyang Cong. The Calpain System. Physiol Rev 83: 731–801, 2003; 10.1152/physrev.00029.2002.—The calpain system originally comprised three molecules: two Ca2+-dependent proteases, μ-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains. Both μ- and m-calpain are heterodimers containing an identical 28-kDa subunit and an 80-kDa subunit that shares 55–65% sequence homology between the two proteases. The crystallographic structure of m-calpain reveals six “domains” in the 8

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Wang, Lijing, Ligong Duan, Xukun Li, and Guoping Li. "Acute-Exercise-Induced Alterations in Calpain and Calpastatin Expression in Rat Muscle." Journal of Sport Rehabilitation 18, no. 2 (May 2009): 213–28. http://dx.doi.org/10.1123/jsr.18.2.213.

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Context:Calpains and calpastatin can degrade muscle proteins, but no research has investigated the expression pattern of calpains and calpastatin after exhaustive exercise.Objective:To investigate the alterations in expression of μ-, m-, and n-calpain and calpastatin after exhaustive exercise and its association with muscle injury.Method:64 rats divided into 2 groups, a nonexercise control group and an acute-exhaustive-exercise (AEE) group. Biopsies in the AEE group were taken at different times after exercise.Results:Calpastatin protein expression and m-calpain activity increased early after

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PAUL, David S., Anne W. HARMON, Courtney P. WINSTON, and Yashomati M. PATEL. "Calpain facilitates GLUT4 vesicle translocation during insulin-stimulated glucose uptake in adipocytes." Biochemical Journal 376, no. 3 (December 15, 2003): 625–32. http://dx.doi.org/10.1042/bj20030681.

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Calpains are a family of non-lysosomal cysteine proteases. Recent studies have identified a member of the calpain family of proteases, calpain 10, as a putative diabetes-susceptibility gene that may be involved in the development of type 2 diabetes. Inhibition of calpain activity has been shown to reduce insulinstimulated glucose uptake in isolated rat-muscle strips and adipocytes. In this report, we examine the mechanism by which calpain affects insulin-stimulated glucose uptake in 3T3-L1 adipocytes. Inhibition of calpain activity resulted in approx. a 60% decrease in insulin-stimulated gluco

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Suzuki, K., K. Shimizu, T. Hamamoto, Y. Nakagawa, T. Murachi, and T. Yamamuro. "Characterization of proteoglycan degradation by calpain." Biochemical Journal 285, no. 3 (August 1, 1992): 857–62. http://dx.doi.org/10.1042/bj2850857.

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Degradation of cartilage proteoglycans was investigated under neutral conditions (pH 7.5) by using pig kidney calpain II (EC 3.4.22.17; Ca(2+)-dependent cysteine proteinase). Aggregate and monomer degradation reached a maximum in 5 min at 30 degrees C when the substrate/enzyme ratio was less than 1000:1. The mode of degradation was limited proteolysis of the core protein; the size of the products was larger than that of papain-digested products and comparable with that of trypsin-digested products. The hyaluronic acid-binding region was lost from the major glycosaminoglycan-bearing region afte

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Elagib, Kamaleldin E., Lorrie L. Delehanty, Ivailo Mihaylov, and Adam Goldfarb. "Calpain Regulation of Megakaryopoiesis through a Positive Regulatory Loop Involving P-TEFb, GATA-1, and RUNX1." Blood 114, no. 22 (November 20, 2009): 566. http://dx.doi.org/10.1182/blood.v114.22.566.566.

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Abstract Abstract 566 GATA-1 and RUNX1 cooperate in programming megakaryocytic development through the critical intermediation of the active P-TEFb kinase complex (Cdk9/cyclin T1). RUNX1 on its own traps P-TEFb in inactive chromatin loops and causes RNA pol II (RNAP II) stalling. GATA-1 by contrast remodels chromatin loops and promotes RNAP II elongation. Thus, P-TEFb most likely integrates and resolves conflicting signals from RUNX1 and GATA-1 to coordinate orderly activation of megakaryocytic target genes during development. P-TEFb activity is tightly regulated by a large network of interact

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Macqueen, Daniel J., and Alexander H. Wilcox. "Characterization of the definitive classical calpain family of vertebrates using phylogenetic, evolutionary and expression analyses." Open Biology 4, no. 4 (April 2014): 130219. http://dx.doi.org/10.1098/rsob.130219.

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The calpains are a superfamily of proteases with extensive relevance to human health and welfare. Vast research attention is given to the vertebrate ‘classical’ subfamily, making it surprising that the evolutionary origins, distribution and relationships of these genes is poorly characterized. Consequently, there exists uncertainty about the conservation of gene family structure, function and expression that has been principally defined from work with mammals. Here, more than 200 vertebrate classical calpains were incorporated in phylogenetic analyses spanning an unprecedented range of taxa, i

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Lehti, Maarit, Riikka Kivelä, Paavo Komi, Jyrki Komulainen, Heikki Kainulainen, and Heikki Kyröläinen. "Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains." Journal of Applied Physiology 106, no. 4 (April 2009): 1419–24. http://dx.doi.org/10.1152/japplphysiol.90660.2008.

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Eccentric exercise induced by electrostimulation increases mRNA expression of titin-complex proteins in rodent skeletal muscle. In this study, mRNA expression of titin, muscle LIM protein (MLP), cardiac ankyrin repeat protein (CARP), ankyrin repeat domain protein 2 (Ankrd2), diabetes-related ankyrin repeat protein (DARP), and calcium-activated proteinases, calpains, were investigated in human skeletal muscle after fatiguing jumping exercise. Fatiguing jumping exercise did not change mRNA expression of titin, DARP, calpain 1, or calpain 3. MLP, Ankrd2 and calpain 2 mRNA levels were increased 2

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Bartus, Raymond T. "The Calpain Hypothesis of Neurodegeneration: Evidence for a Common Cytotoxic Pathway." Neuroscientist 3, no. 5 (September 1997): 314–27. http://dx.doi.org/10.1177/107385849700300513.

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Calpain's general function and pathogenic role in the CNS are reviewed. Collectively, the literature indicates that calpain proteolysis plays a common and important role in a variety of acute neurodegenerative conditions, including focal ischemia (stroke), global ischemia, traumatic brain injury, and spinal cord injury. This evidence indicates that 1) calpain is activated in an abnormally sustained fashion during cellular events commonly associated with neurodegeneration (e.g., excessive interstitial glutamate and cytosolic calcium); 2) many of calpain's preferred substrates are degraded as im

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Nuzzi, Paul A., Melissa A. Senetar, and Anna Huttenlocher. "Asymmetric Localization of Calpain 2 during Neutrophil Chemotaxis." Molecular Biology of the Cell 18, no. 3 (March 2007): 795–805. http://dx.doi.org/10.1091/mbc.e06-09-0876.

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Chemoattractants induce neutrophil polarization through localized polymerization of F-actin at the leading edge. The suppression of rear and lateral protrusions is required for efficient chemotaxis and involves the temporal and spatial segregation of signaling molecules. We have previously shown that the intracellular calcium-dependent protease calpain is required for cell migration and is involved in regulating neutrophil chemotaxis. Here, we show that primary neutrophils and neutrophil-like HL-60 cells express both calpain 1 and calpain 2 and that chemoattractants induce the asymmetric recru

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Goll, Darrel E., Valery F. Thompson, Richard G. Taylor, and Ahmed Ouali. "The calpain system and skeletal muscle growth." Canadian Journal of Animal Science 78, no. 4 (December 1, 1998): 503–12. http://dx.doi.org/10.4141/a98-081.

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The first protein of a group of proteins now identified as belonging to the calpain system was purified in 1976. The calpain system presently is known to be constituted of three well-characterized proteins; several lesser studied proteins that have been isolated from invertebrates; and 10 mRNAs, two each in Drosophila and C. elegans and six in vertebrates, that encode proteins, which, based on sequence homology, belong to the calpain family. The three well-characterized proteins in the calpain family include two Ca2+-dependent proteolytic enzymes, µ-calpain and m-calpain, and a protein, calpas

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Larsen, Anna K., René Lametsch, John S. Elce, Jørgen K. Larsen, Bo Thomsen, Martin R. Larsen, Moira A. Lawson, Peter A. Greer, and Per Ertbjerg. "Genetic disruption of calpain correlates with loss of membrane blebbing and differential expression of RhoGDI-1, cofilin and tropomyosin." Biochemical Journal 411, no. 3 (April 14, 2008): 657–66. http://dx.doi.org/10.1042/bj20070522.

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Dynamic regulation of the actin cytoskeleton is important for cell motility, spreading and the formation of membrane surface extensions such as lamellipodia, ruffles and blebs. The ubiquitous calpains contribute to integrin-mediated cytoskeletal remodelling during cell migration and spreading, by cleavage of focal adhesion components and signalling molecules. In the present study, the live-cell morphology of calpain-knockout and wild-type cells was examined by time-lapse fluorescence microscopy, and a role of calpain in mediating the formation of sporadic membrane blebs was established. Membra

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Randriamboavonjy, Voahanginirina, Johann Isaak, Amro Elgheznawy, Frank Pistrosch, Timo Frömel, Xiaoke Yin, Klaus Badenhoop, Heinrich Heide, Manuel Mayr, and Ingrid Fleming. "Calpain inhibition stabilizes the platelet proteome and reactivity in diabetes." Blood 120, no. 2 (July 12, 2012): 415–23. http://dx.doi.org/10.1182/blood-2011-12-399980.

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Abstract Platelets from patients with diabetes are hyperreactive and demonstrate increased adhesiveness, aggregation, degranulation, and thrombus formation, processes that contribute to the accelerated development of vascular disease. Part of the problem seems to be dysregulated platelet Ca2+ signaling and the activation of calpains, which are Ca2+-activated proteases that result in the limited proteolysis of substrate proteins and subsequent alterations in signaling. In the present study, we report that the activation of μ- and m-calpain in patients with type 2 diabetes has profound effects o

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Meier, Markus, Harald H. Klein, Jan Kramer, Maren Drenckhan, and Morten Schütt. "Calpain inhibition impairs glycogen syntheses in HepG2 hepatoma cells without altering insulin signaling." Journal of Endocrinology 193, no. 1 (April 2007): 45–51. http://dx.doi.org/10.1677/joe.1.07087.

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Calpains are a family of non-lysosomal cytoplasmatic cysteine proteases. Since calpain 10 (CAPN10), a member of the calpain family of proteases, has been found to represent a putative diabetes susceptibility gene, it was argued that calpains may be involved in the development of type 2 diabetes. The functional role of calpains in insulin signaling and/or insulin action is, however, not clear. We investigated the effects of the calpains 1 and 2 inhibitor PD151746 on insulin signaling and insulin action in human hepatoma G2 cells (HepG2). HepG2 cells were incubated without (−PD) or with (+PD) 5.

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NATH, Rathna, Kadee J. RASER, Daniel STAFFORD, Iradj HAJIMOHAMMADREZA, Avigail POSNER, Hamish ALLEN, Robert V. TALANIAN, Po-wai YUEN, Richard B. GILBERTSEN та Kevin K. W. WANG. "Non-erythroid α-spectrin breakdown by calpain and interleukin 1 β-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis". Biochemical Journal 319, № 3 (1 листопада 1996): 683–90. http://dx.doi.org/10.1042/bj3190683.

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The cytoskeletal protein non-erythroid α-spectrin is well documented as an endogenous calpain substrate, especially under pathophysiological conditions. In cell necrosis (e.g. maitotoxin-treated neuroblastoma SH-SY5Y cells), α-spectrin breakdown products (SBDPs) of 150 kDa and 145 kDa were produced by cellular calpains. In contrast, in neuronal cells undergoing apoptosis (cerebellar granule neurons subjected to low potassium and SH-SY5Y cells treated with staurosporine), an additional SBDP of 120 kDa was also observed. The formation of the 120 kDa SBDP was insensitive to calpain inhibitors but

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Perrin, B. J., and A. Huttenlocher. "Calpain." International Journal of Biochemistry & Cell Biology 34, no. 7 (July 2002): 722–25. http://dx.doi.org/10.1016/s1357-2725(02)00009-2.

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Goette, Andreas, Marco Arndt, Christoph Röcken, Thorsten Staack, Roland Bechtloff, Dirk Reinhold, Christof Huth, Siegfried Ansorge, Helmut U. Klein, and Uwe Lendeckel. "Calpains and cytokines in fibrillating human atria." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 1 (July 1, 2002): H264—H272. http://dx.doi.org/10.1152/ajpheart.00505.2001.

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Atrial fibrillation (AF) is accompanied by intracellular calcium overload. The purpose of this study was to assess the role of calcium-dependent calpains and cytokines during AF. Atrial tissue samples from 32 patients [16 with chronic AF and 16 in sinus rhythm (SR)] undergoing open heart surgery were studied. Atrial expression of calpain I and II, calpastatin, troponin T (TnT), troponin C (TnC), and cytokines [interleukin (IL)-1β, IL-2, IL-6, IL-8, IL-10, transforming growth factor (TGF)-β1, and tumor necrosis factor-α] were determined. Expression of calpain I was increased during AF (461 ± 20

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Pestereva, N. S., A. Z. Marshak, and M. N. Karpenko. "CALPAIN ACTIVITY UNDER EXPERIMENTAL INCREASING OF DOPAMINE LEVEL." Medical academic journal 19, no. 1S (December 15, 2019): 221–22. http://dx.doi.org/10.17816/maj191s1221-222.

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The aim of our study was to identify the activity of calpains under conditions of an experimental increase in the level of dopamine. The work was performed at three levels: in vivo, in situ, in vitro. An in situ study was carried on a model of isolated nerve endings - synaptosomes. Using casein zymography in solution with FITC-casein, it was shown that incubation of synaptosomes dopamine leads to calpains secretion into the synaptosomal medium. The dopamine ability to directly activate calpain was demonstrated by casein zymography in a gel. Incubation in an activation buffer containing dopamin

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Liu, Ming Cheng, Veronica Akle, Wenrong Zheng, Jitendra R. Dave, Frank C. Tortella, Ronald L. Hayes, and Kevin K. W. Wang. "Comparing calpain- and caspase-3-mediated degradation patterns in traumatic brain injury by differential proteome analysis." Biochemical Journal 394, no. 3 (February 24, 2006): 715–25. http://dx.doi.org/10.1042/bj20050905.

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A major theme of TBI (traumatic brain injury) pathology is the over-activation of multiple proteases. We have previously shown that calpain-1 and -2, and caspase-3 simultaneously produced αII-spectrin BDPs (breakdown products) following TBI. In the present study, we attempted to identify a comprehensive set of protease substrates (degradome) for calpains and caspase-3. We further hypothesized that the TBI differential proteome is likely to overlap significantly with the calpain- and caspase-3-degradomes. Using a novel HTPI (high throughput immunoblotting) approach and 1000 monoclonal antibodie

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Wang, Yubin, Yan Liu, Amy Nham, Arash Sherbaf, Diana Quach, Emad Yahya, Davis Ranburger, Xiaoning Bi, and Michel Baudry. "Calpain-2 as a therapeutic target in repeated concussion–induced neuropathy and behavioral impairment." Science Advances 6, no. 27 (July 2020): eaba5547. http://dx.doi.org/10.1126/sciadv.aba5547.

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Repeated concussion represents a serious health problem as it can result in various brain pathologies, ranging from minor focal tissue injury to severe chronic traumatic encephalopathy. The calcium-dependent protease, calpain, participates in the development of neurodegeneration following concussion, but there is no information regarding the relative contribution of calpain-1 and calpain-2, the major calpain isoforms in the brain. We used a mouse model of repeated concussions, which reproduces most of the behavioral and neuropathological features of the human condition, to address this issue.

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Saatman, Kathryn E., Babak Abai, Ashley Grosvenor, Christian K. Vorwerk, Douglas H. Smith, and David F. Meaney. "Traumatic Axonal Injury Results in Biphasic Calpain Activation and Retrograde Transport Impairment in Mice." Journal of Cerebral Blood Flow & Metabolism 23, no. 1 (January 2003): 34–42. http://dx.doi.org/10.1097/01.wcb.0000035040.10031.b0.

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Traumatic axonal injury (TAI) is one of the most important pathologies associated with closed head injury, and contributes to ensuing morbidity. The authors evaluated the potential role of calpains in TAI using a new model of optic nerve stretch injury in mice. Male C57BL/6 mice were anesthetized, surgically prepared, and subjected to a 2.0-mm optic nerve stretch injury (n = 34) or sham injury (n = 18). At various intervals up to 2 weeks after injury, optic nerves were examined for neurofilament proteins and calpain-mediated spectrin breakdown products using immunohistochemistry. In addition,

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Supinski, Gerald S., Alexander P. Alimov, Lin Wang, Xiao-Hong Song, and Leigh A. Callahan. "Neutral sphingomyelinase 2 is required for cytokine-induced skeletal muscle calpain activation." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 6 (September 15, 2015): L614—L624. http://dx.doi.org/10.1152/ajplung.00141.2015.

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Calpain contributes to infection-induced diaphragm dysfunction but the upstream mechanism(s) responsible for calpain activation are poorly understood. It is known, however, that cytokines activate neutral sphingomyelinase (nSMase) and nSMase has downstream effects with the potential to increase calpain activity. We tested the hypothesis that infection-induced skeletal muscle calpain activation is a consequence of nSMase activation. We administered cytomix (20 ng/ml TNF-α, 50 U/ml IL-1β, 100 U/ml IFN-γ, 10 μg/ml LPS) to C2C12 muscle cells to simulate the effects of infection in vitro and studie

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Struglics, André, and Maria Hansson. "Calpain is involved in C-terminal truncation of human aggrecan." Biochemical Journal 430, no. 3 (August 27, 2010): 531–38. http://dx.doi.org/10.1042/bj20100591.

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Mature aggrecan is generally C-terminally truncated at several sites in the CS (chondroitin sulfate) region. Aggrecanases and MMPs (matrix metalloproteinases) have been suggested to be responsible for this digestion. To identify whether calpain, a common intracellular protease, has a specific role in the proteolysis of aggrecan we developed neoepitope antibodies (anti-PGVA, anti-GDLS and anti-EDLS) against calpain cleavage sites and used Western blot analysis to identify calpain-generated fragments in normal and OA (osteoarthritis) knee cartilage and SF (synovial fluid) samples. Our results sh

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RAVULAPALLI, Ravikiran, Beatriz GARCIA DIAZ, Robert L. CAMPBELL, and Peter L. DAVIES. "Homodimerization of calpain 3 penta-EF-hand domain." Biochemical Journal 388, no. 2 (May 24, 2005): 585–91. http://dx.doi.org/10.1042/bj20041821.

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Calpains 1 and 2 are heterodimeric proteases in which large (relative molecular mass Mr 80000) and small (Mr 28000) subunits are linked through their respective PEF (penta-EF-hand) domains. The skeletal muscle-specific calpain 3 is believed not to form a heterodimer with the small subunit but might homodimerize through its PEF domain. Size-exclusion chromatography and analytical ultracentrifugation of the recombinant PEF domain of calpain 3 show that it forms a stable homodimer that does not dissociate on dilution. Molecular modelling suggests that there would be no barriers to the dimerizatio

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Parnaud, Géraldine, Eva Hammar, Dominique G. Rouiller та Domenico Bosco. "Inhibition of calpain blocks pancreatic β-cell spreading and insulin secretion". American Journal of Physiology-Endocrinology and Metabolism 289, № 2 (серпень 2005): E313—E321. http://dx.doi.org/10.1152/ajpendo.00006.2005.

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In addition to promoting insulin secretion, an increase in cytosolic Ca2+ triggered by glucose has been shown to be crucial for spreading of β-cells attached on extracellular matrix (804G matrix). Calpains are Ca2+-dependent cysteine proteases involved in an extended spectrum of cellular responses, including cytoskeletal rearrangements and vesicular trafficking. The present work aimed to assess whether calpain is also implicated in the process of Ca2+-induced insulin secretion and spreading of rat pancreatic β-cells. The results indicate calpain dependency of β-cell spreading on 804G matrix. I

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Alvarez-Arce, Alejandro, Irene Lee-Rivera, Edith López, Arturo Hernández-Cruz, and Ana María López-Colomé. "Thrombin-Induced Calpain Activation Promotes Protease-Activated Receptor 1 Internalization." International Journal of Cell Biology 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/1908310.

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The serine protease thrombin activates Protease-Activated Receptors (PARs), a family of G-protein-coupled receptors (GPCRs) activated by the proteolytic cleavage of their extracellular N-terminal domain. Four members of this family have been identified: PAR1–4. The activation of Protease-Activated Receptor 1(PAR1), the prototype of this receptor family, leads to an increase in intracellular Ca+2concentration ([Ca+2]i) mediated byGq11αcoupling and phospholipase C (PLC) activation. We have previously shown that the stimulation of PAR1 by thrombin promotes intracellular signaling leading to RPE c

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Abeyrathna, Prasanna, Laszlo Kovacs, Weihong Han та Yunchao Su. "Calpain-2 activates Akt via TGF-β1-mTORC2 pathway in pulmonary artery smooth muscle cells". American Journal of Physiology-Cell Physiology 311, № 1 (1 липня 2016): C24—C34. http://dx.doi.org/10.1152/ajpcell.00295.2015.

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Calpain is a family of calcium-dependent nonlysosomal neutral cysteine endopeptidases. Akt is a serine/threonine kinase that belongs to AGC kinases and plays important roles in cell survival, growth, proliferation, angiogenesis, and cell metabolism. Both calpain and Akt are the downstream signaling molecules of platelet-derived growth factor (PDGF) and mediate PDGF-induced collagen synthesis and proliferation of pulmonary artery smooth muscle cells (PASMCs) in pulmonary vascular remodeling. We found that inhibitions of calpain-2 by using calpain inhibitor MDL28170 and calpain-2 small interferi

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Yeh, J.-Y., B.-R. Ou, and N. E. Forsberg. "Effects of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits." Journal of Endocrinology 141, no. 2 (May 1994): 209–17. http://dx.doi.org/10.1677/joe.0.1410209.

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Abstract The objectives were to investigate the mechanisms by which glucocorticoids control proteolysis in muscle cells and the relationship between the calpain:calpastatin system and proteolysis in muscle. Female rabbits were treated with 1 mg dexamethasone (Dex)/kg body weight per day for 0, 1, 2 or 4 days after which animals were killed and muscle samples taken for analyses. Dex reduced urinary Nτ-methylhistidine (NMH) 48% (day 4 versus day 1 of Dex treatment) and muscle NMH concentrations by 49% (day 1) to 40% (day 2) respectively, suggesting that protein degradation was reduced. To invest

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