Today, Calpain-3 is a highly relevant and topical issue that affects people of all ages and cultures. More and more people are interested in learning about Calpain-3 and understanding its impact on modern society. Due to its importance, it is crucial to further study Calpain-3 in order to understand its implications and possible solutions. In this article, we will explore various perspectives on Calpain-3 and how it is influencing our daily lives. Additionally, we will discuss the global implications and possible measures that can be taken to address this challenge.
Calpain-3 is a protein that in humans is encoded by the CAPN3gene.[1][2]
Function
Calpain, a heterodimer consisting of a large and a small subunit, is a major intracellular protease, although its function has not been well established. This gene encodes a muscle-specific member of the calpain large subunit family that specifically binds to titin. Mutations in this gene are associated with limb-girdle muscular dystrophies type 2A. Alternate promoters and alternative splicing result in multiple transcript variants encoding different isoforms and some variants are ubiquitously expressed.[3]
In melanocytic cells CAPN3 gene expression may be regulated by MITF.[4]
Sorimachi H, Ono Y, Suzuki K (2000). "Skeletal Muscle-Specific Calpain, p94, and Connectin/Titin: Their Physiological Functions and Relationship to Limb-Girdle Muscular Dystrophy Type 2A". Elastic Filaments of the Cell. Advances in Experimental Medicine and Biology. Vol. 481. pp. 383–95, discussion 395-7. doi:10.1007/978-1-4615-4267-4_23. ISBN978-1-4613-6916-5. PMID10987085.
Baghdiguian S, Richard I, Martin M, Coopman P, Beckmann JS, Mangeat P, Lefranc G (2001). "Pathophysiology of limb girdle muscular dystrophy type 2A: hypothesis and new insights into the IkappaBalpha/NF-kappaB survival pathway in skeletal muscle". J. Mol. Med. 79 (5–6): 254–61. doi:10.1007/s001090100225. PMID11485017. S2CID286784.
Canki-Klain N, Milic A, Kovac B, Trlaja A, Grgicevic D, Zurak N, Fardeau M, Leturcq F, Kaplan JC, Urtizberea JA, Politano L, Piluso G, Feingold J (2004). "Prevalence of the 550delA mutation in calpainopathy (LGMD 2A) in Croatia". Am. J. Med. Genet. A. 125A (2): 152–6. doi:10.1002/ajmg.a.20408. PMID14981715. S2CID21946737.
Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet. Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID2209092.
Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A (1996). "NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain". Biochem. Biophys. Res. Commun. 229 (1): 299–304. doi:10.1006/bbrc.1996.1796. PMID8954122.
Kinbara K, Sorimachi H, Ishiura S, Suzuki K (1997). "Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs". Arch. Biochem. Biophys. 342 (1): 99–107. doi:10.1006/abbi.1997.0108. PMID9185618.
Dinçer P, Leturcq F, Richard I, Piccolo F, Yalnizoglu D, de Toma C, Akçören Z, Broux O, Deburgrave N, Brenguier L, Roudaut C, Urtizberea JA, Jung D, Tan E, Jeanpierre M, Campbell KP, Kaplan JC, Beckmann JS, Topaloglu H (1997). "A biochemical, genetic, and clinical survey of autosomal recessive limb girdle muscular dystrophies in Turkey". Ann. Neurol. 42 (2): 222–9. doi:10.1002/ana.410420214. PMID9266733. S2CID28524591.