Disease relevance of CAPN1

• Various lines of evidence suggest that calcium dependent protease (CANP, calpain) exists in the cytosol as an inactive proenzyme which is converted to an active form by autolysis [1].

High impact information on CAPN1

• 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 [2].
• The overall amino acid sequence similarities of the mCANP large subunit with those of human muCANP and chicken CANP are 62% and 66%, respectively [3].
• The active site of calcium-activated neutral protease (CANP) was specifically labeled with iodoacetic acid [4].
• Effects of ethylene glycol tetraacetic acid, A23187 and calmodulin, calcium activated neutral proteinase antagonists on melatonin secretion in perifused chick pineal gland [5].
• OP administration caused an increase in CANP activity in brain within 4 days and in sciatic nerve and gastrocnemius muscle within 2 days of administration [6].

Biological context of CAPN1

• The amino acid sequence shows 66% and 86% identity with the mouse and zebrafish Capn1, respectively [7].
• The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined [4].
• Fifteen hybridomas secreting antibodies against calcium-activated neutral protease (CANP), especially those for rabbit muscle mCANP with low calcium sensitivity, have been produced by the cell fusion technique [8].

Anatomical context of CAPN1

• Localization of calcium-activated neutral protease (CANP) in the peripheral nerve [9].
• This study shows that the loss of perifused chick pineal gland activity is a complex process which seems to involve the release of calcium from intracellular stores, calmodulin and calcium-activated neutral protease (CANP) [5].
• Analyses of the autocatalytic activation of CANP in the presence of plasma membranes reveal that proCANP translocates to the membrane in the presence of microM Ca2+ and is activated at the membrane [1].
• CANP was demonstrated in the axon, but not in the myelin sheath or endoneurium [9].
• The amount of CANP bound to myofibrils was approximately 4 percent of that contained in the whole muscle homogenate [10].

Associations of CAPN1 with chemical compounds

• Amino acid sequence around the active site cysteine residue of calcium-activated neutral protease (CANP) [4].

Analytical, diagnostic and therapeutic context of CAPN1

• Starvation of rainbow trout fingerlings (15-20 g) for 35 days stimulated the expression of Capn1 (2.2-fold increase, P < 0.01), Capn2 (6.0-fold increase, P < 0.01), and calpastatins (1.6-fold increase, P < 0.05) as measured by quantitative real-time RT-PCR [7].
• Its specificity to CANP, as well as its cross-reactivity with rat CANP, were confirmed by the Ouchterlony immunodiffusion procedure and immunoreplica method [9].
• To clarify the mechanism of activation of calcium activated neutral protease (CANP, or mCANP: active at mM Ca2+), the structure of mCANP was examined by measuring CD spectra and by titration of SH groups in the presence of Mn2+ [11].

References