title: Novel rat calpastatin mRNA variants.
abstract: Rat calpastatin cDNAs obtained by RT-PCR method were isolated and directly sequenced; this allowed the identification of two new variants both characterized by a 23 amino acids deletion at the end of the unique N-terminal domain L, increasing the number of functional isoforms. The deletion shows high homology to the amino acid sequence coded by exon 8 of human calpastatin gene and properly conserved splicing consensus sequences, suggesting exon skipping in domain L. Furthermore, three point mutations scattered along the coding region were found.
authors.affiliation: Istituto Scientifico H. San Raffaele, Milan, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Servadio
authors.forename: G
authors.initials: G
authors.lastname: Casari
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry* / Q000235:genetics; D018076:DNA, Complementary / Q000737:chemistry; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D012333:RNA, Messenger / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051381:Rats; D011921:Rats, Inbred WKY; D017207:Rats, Sprague-Dawley; D017386:Sequence Homology, Amino Acid
chemical_list: D002135:Calcium-Binding Proteins; D015853:Cysteine Proteinase Inhibitors; D018076:DNA, Complementary; D012333:RNA, Messenger; C033668:calpastatin