Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.22.54 (calpain 3)
 430 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two types of calcium-dependent protease with distinct calcium requirements (termed muCANP and mCANP) are known in mammalian tissues. These two isozymes consist of different large (80-kDa) subunits (mu- or m-types) and identical small (30-kDa) subunits. By screening human and rat muscle cDNA libraries with a cDNA probe for the chicken CANP large subunit, which has a structure similar to both the mammalian mu- and m-types, a cDNA clone encoding a novel member of the CANP large subunit family was obtained. The encoded protein (designated "p94") consists of 821 amino acid residues (Mr 94,084) and shows significant sequence homology with both human mu-type (54%) and m-type (51%) large subunits. p94 can be divided into four domains (I-IV) as reported for the CANP large subunit family. Domains II and IV are potential cysteine protease and calcium-binding domains, respectively, and have sequences homologous to the corresponding domains of other CANP large subunits. However, domain I of p94 is significantly different from others. Moreover, p94 contains two unique sequences of 62 and 77 residues in domains II and III, respectively. In contrast to the ubiquitous expression of mu- and m-types, Northern blot analysis revealed that the mRNA for p94 exists only in skeletal muscle with none detected in other tissues including heart muscle and smooth muscles such as intestine.
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PMID:Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. 255 41

In the mammalian calpain system, two isozymes, mu- and m-types, have been well-characterized, and are considered to be conserved in the avian system as well. Thus, chicken calpain, whose large subunit was cloned in 1984, has long been regarded as 'm-type', since chicken also possesses 'mu-type' activity, although its structure has not yet been elucidated. In this study, we identified three kinds of cDNAs encoding distinct chicken calpain large subunits. Two of the three were highly similar to the mammalian mu-type and p94, respectively. The third shows a much higher similarity to mammalian m-type than the first identified chicken calpain, indicating that this molecule, which has been considered as 'm-type', should be renamed. We, therefore, designated it 'mu/m-calpain', because its sequence and Ca(2+)-sensitivity lie between mu- and m-types. Northern blot analyses revealed that chicken mCL and muCL, as well as mu/mCL, show ubiquitous expression, while p94 was detected predominantly in skeletal muscle, as previously reported. Chicken skeletal muscle, therefore, expresses at least four types of calpain, three ubiquitous and one tissue-specific.
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PMID:Identification of a third ubiquitous calpain species--chicken muscle expresses four distinct calpains. 774 67