Rat brain contains multiple mRNAs for calpastatin<sup>1</sup>

Tullio, Roberta De; Sparatore, Bianca; Salamino, Franca; Melloni, Edon; Pontremoli, S.

doi:10.1016/s0014-5793(97)01588-3

Cited by 42 publications

(40 citation statements)

References 34 publications

(39 reference statements)

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“…2). This is consistent with mammalian CAST transcripts that demonstrate alternative splicing of exons 3-6, producing isoforms with divergent N-terminal L-domains (Lee et al, 1992;De Tullio et al, 1998). Also similar to the mammalian system, alternative splicing may be restricted to the 5Ј exons of cast.…”

Section: Phylogenetic Analysis Of the Zebrafish Calpain System Genessupporting

confidence: 77%

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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Section: Phylogenetic Analysis Of the Zebrafish Calpain System Genessupporting

confidence: 77%

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

Lepage

Bruce

2008

Developmental Dynamics

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“…Various calpastatin mRNA species have been described [37][38][39][40][41][42]. The 3h-untranslated regions of some calpastatin mRNA species have several polyadenylation sites and contain sequences reported to modulate mRNA stability [37][38][39][40][41].…”

Section: Discussionmentioning

confidence: 99%

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

Barnoy

Supino-Rosin

Kosower

2000

Biochemical Journal

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Tel Aviv 69978, IsraelCalpain (Ca# + -dependent intracellular protease)-induced proteolysis has been considered to play a role in myoblast fusion to myotubes. We found previously that calpastatin (the endogenous inhibitor of calpain) diminishes transiently during myoblast differentiation. To gain information about the regulation of calpain and calpastatin in differentiating myoblasts, we evaluated the stability and synthesis of calpain and calpastatin, and measured their mRNA levels in L8 myoblasts. We show here that µ-calpain and m-calpain are stable, long-lived proteins in both dividing and differentiating L8 myoblasts. Calpain is synthesized in differentiating myoblasts, and calpain mRNA levels do not change during differentiation. In contrast, calpastatin (though also a long-lived protein in myoblasts), is less stable in differentiating myoblasts than in the dividing cells, and its synthesis is inhibited upon initiation of differentiation. Inhibition of cal-

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“…Sequences of rat calpastatin obtained in early studies of this calpastatin all lacked exon 3 (94,238), and it was assumed initially that rodent calpastatins were unique in that they lacked this exon. Several forms of mouse type I, II, and III calpastatins, some of them containing exon 3 and some of them having exon 3 deleted (443) have been identified, however; hence, some rodent calpastatins also contain exon 3.…”

Section: B Properties Of Calpastatinmentioning

confidence: 99%

The Calpain System

Goll

Thompson

et al. 2003

Physiological Reviews

2,552

2,801

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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 80-kDa subunit: 1) a 19-amino acid NH2-terminal sequence; 2) and 3) two domains that constitute the active site, IIa and IIb; 4) domain III; 5) an 18-amino acid extended sequence linking domain III to domain IV; and 6) domain IV, which resembles the penta EF-hand family of polypeptides. The single calpastatin gene can produce eight or more calpastatin polypeptides ranging from 17 to 85 kDa by use of different promoters and alternative splicing events. The physiological significance of these different calpastatins is unclear, although all bind to three different places on the calpain molecule; binding to at least two of the sites is Ca2+ dependent. Since 1989, cDNA cloning has identified 12 additional mRNAs in mammals that encode polypeptides homologous to domains IIa and IIb of the 80-kDa subunit of μ- and m-calpain, and calpain-like mRNAs have been identified in other organisms. The molecules encoded by these mRNAs have not been isolated, so little is known about their properties. How calpain activity is regulated in cells is still unclear, but the calpains ostensibly participate in a variety of cellular processes including remodeling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis. Deregulated calpain activity following loss of Ca2+ homeostasis results in tissue damage in response to events such as myocardial infarcts, stroke, and brain trauma.

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Rat brain contains multiple mRNAs for calpastatin¹

Cited by 42 publications

References 34 publications

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

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

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

The Calpain System

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Rat brain contains multiple mRNAs for calpastatin1

Cited by 42 publications

References 34 publications

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

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

Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability

The Calpain System

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Rat brain contains multiple mRNAs for calpastatin¹