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Biochem Biophys Res Commun. 1999 Jul 14;260(3):671-5.

CAPN 8: isolation of a new mouse calpain-isoenzyme.

Author information

1
Institute of Human Genetics, University of Saar, Homburg/Saar, D-66421, Germany.

Abstract

Recent molecular biological approaches indicate that calpain, also named CANP for calcium-activated neutral protease and originally characterized as an intracellular cytoplasmatic nonlysosomal cysteine protease that requires calcium ions for activity, constitutes a large superfamily consisting of ubiquitous and tissue specific homologues, which are widely distributed in cells of various organisms from human to fungus. Due to the increasing number of substrates along with the involvement of calpain isoenzymes in mammalian diseases, especially in malignancies, members of the calpain superfamily seem to be important biomodulators in physiological as well as pathological cell function. Here we report the characterisation of a new calpain, named CAPN 8 with a different C-terminal domain, implicating a putative new regulatory mechanism. Northern blot analysis revealed an ubiquitous expression with different RNA levels in all tissues examined. Highest levels were found in brain, kidney, and digestive tract, suggesting a specific regulatory function of CAPN 8 in these tissues.

PMID:
10403824
DOI:
10.1006/bbrc.1999.0948
[Indexed for MEDLINE]

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