Disease relevance of calpain

• Because spectrin is a major target of calpain proteolysis, it is possible that some neurodegenerative disorders may involve the cleavage of spectrin followed by the breakage of neural processes [1].

High impact information on calpain

• The Caenorhabditis elegans tra-3 gene promotes female development in XX hermaphrodites and encodes an atypical calpain regulatory protease lacking calcium-binding EF hands [2].
• Investigations in both nematodes and mammals converge to implicate specific calpain and aspartyl proteases in the execution of necrotic cell death [3].
• This paper reviews the role of cysteine proteases such as caspase, calpain and cathepsin in order to clarify the mechanism of ischemic neuronal death being triggered by the unspecific digestion of lysosomal proteases [4].
• A reported Caenorhabditis elegans homologue contains the calpain domain and C-terminal region, but appears to lack the zinc finger region [5].

Biological context of calpain

• The calpain-like domain and C-terminal region are highly conserved (58% identity), and similar Cys2-Cys2 zinc fingers are present in the N-terminal region [5].

Anatomical context of calpain

• SOLH, a human homologue of the Drosophila melanogaster small optic lobes gene is a member of the calpain and zinc-finger gene families and maps to human chromosome 16p13.3 near CATM (cataract with microphthalmia) [5].

Other interactions of calpain

• The tra-3 sex determination gene of Caenorhabditis elegans encodes a member of the calpain regulatory protease family [6].

References