SOLH, a Human Homologue of theDrosophila melanogaster small optic lobesGene Is a Member of the Calpain and Zinc-Finger Gene Families and Maps to Human Chromosome 16p13.3 nearCATM(Cataract with Microphthalmia)

Kamei, Makoto; Webb, Graham C.; Young, Ian G.; Campbell, Hugh D.

doi:10.1006/geno.1998.5395

Cited by 38 publications

(28 citation statements)

References 48 publications

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“…SOL has several Zn-finger motifs located at the N-terminus followed by the protease domain. Mammals have one orthologue, calpain-15/SOLH, and all other animals including Leishmania and Trypanosoma and green algae also have orthologues, constituting the SOL subfamily [72,73]. They share a conserved C-terminal structure called the SOH domain, but the physiological role of SOLH is still unclear.…”

Section: Expanding Calpain Speciesmentioning

confidence: 99%

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

2010

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Abstract:Calpains are intracellular Ca 2+ -dependent cysteine proteases (Clan CA, family C02, EC 3.4.22.17) found in almost all eukaryotes and some bacteria. Calpains display limited proteolytic activity at neutral pH, proteolysing substrates to transform and modulate their structures and activities, and are therefore called "modulator proteases". The human genome has 15 genes that encode a calpain-like protease domain, generating diverse calpain homologues that possess combinations of several functional domains such as Ca 2+ -binding domains and Zn-finger domains. The importance of the physiological roles of calpains is reflected in the fact that particular defects in calpain functionality cause a variety of deficiencies in many different organisms, including lethality, muscular dystrophies, lissencephaly, and tumorigenesis. In this review, the unique characteristics of this distinctive protease superfamily are introduced in terms of genetically modified animals, some of which are animal models of calpain deficiency diseases.

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Section: Expanding Calpain Speciesmentioning

confidence: 99%

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

2010

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“…Calpain-5 is expressed ubiquitously and may have a role in sex determination (25). Calpain-10 has been identified as a type 2 diabetes susceptibility gene (39) and calpain-13 is a homologue of a Drosophila small optic lobe gene (40). Calpain-10 was found to be partially localized to the nucleus, and nuclear localization was enhanced upon ionomycin treatment (41).…”

Section: Huntington's Disease (Hd)mentioning

confidence: 99%

Inhibition of Calpain Cleavage of Huntingtin Reduces Toxicity

Gafni

Hermel

Young

et al. 2004

Journal of Biological Chemistry

244

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Huntington's disease (HD) is a neurodegenerative disorder caused by a polyglutamine (polyQ) tract expansion near the N terminus of huntingtin (Htt). Proteolytic processing of mutant Htt and abnormal calcium signaling may play a critical role in disease progression and pathogenesis. Recent work indicates that calpains may participate in the increased and/or altered patterns of Htt proteolysis leading to the selective toxicity observed in HD striatum. Here, we identify two calpain cleavage sites in Htt and show that mutation of these sites renders the polyQ expanded Htt less susceptible to proteolysis and aggregation, resulting in decreased toxicity in an in vitro cell culture model. In addition, we found that calpain-and caspase-derived Htt fragments preferentially accumulate in the nucleus without the requirement of further cleavage into smaller fragments. Calpain family members, calpain-1, -5, -7, and -10, have increased levels or are activated in HD tissue culture and transgenic mouse models, suggesting they may play a key role in Htt proteolysis and disease pathology. Interestingly, calpain-1, -5, -7, and -10 localize to the cytoplasm and the nucleus, whereas the activated forms of calpain-7 and -10 are found only in the nucleus. These results support the role of calpain-derived Htt fragmentation in HD and suggest that aberrant activation of calpains may play a role in HD pathogenesis.

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“…Five other catalytic-type calpain genes (CAPN3,8,9,11,12 and 13) encode products with domain structures similar to that of CAPN1 and CAPN2, and together, these are classified as typical calpains (Aoki et al, 1986;Sorimachi et al, 1993;Dear et al, 1999Dear et al, , 2000Dear and Boehm, 2001;Hata et al, 2001;Suzuki et al, 2004). The remaining six catalytic-type calpain genes (CAPN5,6,7,10,14,and 15) constitute the group of atypical calpains as they lack domains characteristic of typical calpains and/or possess unique domains (Dear et al, 1997;Kamei et al, 1998;Franz et al, 1999;Dear and Boehm, 2001;Suzuki et al, 2004). Traditionally, typical and atypical calpains have been further subdivided based on the diversity of tissues in which their respective proteins have been found (Suzuki et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Characterization and comparative expression of zebrafish calpain system genes during early development

Lepage

Bruce

2008

Developmental Dynamics

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The classic calpain system has been implicated in regulating a variety of cellular processes including cell adhesion, migration, and intracellular signaling; however, little is known regarding the function of this system in vivo. Two heterodimeric Ca 2؉ -dependent cysteine proteases, -calpain (CAPN1) and m-calpain (CAPN2), and the endogenous inhibitor calpastatin (CAST) comprise the classic/ubiquitous calpain system in mammals. Recently, knockout of two murine classic calpain genes, Capn2 and Capn4/Capns1, revealed that components of the classic system are indispensable for preimplantation development. We identified four classic calpain catalytic subunit genes (capn1a, 1b, 2a, 2b), two regulatory subunit genes (capns1a, 1b), and calpastatin (cast) from the zebrafish. Our data suggest that the components of the classic mammalian system are both conserved and expanded in the teleost lineage. In contrast to the classic/ubiquitous mammalian system, zebrafish calpain system genes acquire unique, tissue-specific patterns of expression within the first 2 days of development. Developmental Dynamics 237:819 -829, 2008.

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SOLH, a Human Homologue of theDrosophila melanogaster small optic lobesGene Is a Member of the Calpain and Zinc-Finger Gene Families and Maps to Human Chromosome 16p13.3 nearCATM(Cataract with Microphthalmia)

Cited by 38 publications

References 48 publications

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

Expanding Members and Roles of the Calpain Superfamily and Their Genetically Modified Animals

Inhibition of Calpain Cleavage of Huntingtin Reduces Toxicity

Characterization and comparative expression of zebrafish calpain system genes during early development

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