2000
DOI: 10.1007/bf02890657
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Calcium-activated neutral proteinase in gametes of the sea urchinStrongylocentrotus droebachiensis

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Cited by 3 publications
(4 citation statements)
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“…It can be supposed that a higher level of calpain activity in organisms of the phylum Annelida reflects the ancient and primitive organization of this group of organisms. The high efficacy of Ca 2+ depen dent proteolysis in the cytosol of lower animals (according to Mykles [10], up to 60% of proteins are hydrolyzed in the cytosol in crustaceans) is associated with another characteristic of their calpains,namely, low selectivity in comparison with homologues from warm blooded animals, which reflects wider substrate specificity [10,15] and more complete hydrolysis of substrate proteins (to short peptides). Thus, for exam ple, calcium dependent proteinases from skeletal muscles of lobster Homarus americanus cleave myo fibrillar proteins, including actin and myosin [10], calpain like proteinase from octopus Octopus vulgaris degrades the majority of proteins in intact myofibrils, particularly myosin, paramyosin, and actin [14].…”
Section: Calpain Activity In Organisms Of Different Taxamentioning
confidence: 99%
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“…It can be supposed that a higher level of calpain activity in organisms of the phylum Annelida reflects the ancient and primitive organization of this group of organisms. The high efficacy of Ca 2+ depen dent proteolysis in the cytosol of lower animals (according to Mykles [10], up to 60% of proteins are hydrolyzed in the cytosol in crustaceans) is associated with another characteristic of their calpains,namely, low selectivity in comparison with homologues from warm blooded animals, which reflects wider substrate specificity [10,15] and more complete hydrolysis of substrate proteins (to short peptides). Thus, for exam ple, calcium dependent proteinases from skeletal muscles of lobster Homarus americanus cleave myo fibrillar proteins, including actin and myosin [10], calpain like proteinase from octopus Octopus vulgaris degrades the majority of proteins in intact myofibrils, particularly myosin, paramyosin, and actin [14].…”
Section: Calpain Activity In Organisms Of Different Taxamentioning
confidence: 99%
“…Three calcium dependent proteinases were isolated from muscles of European bass Dicentrarchus labrax, and one of them consists of subunits 25 and 80 kDa similar to the µ and m calpains of higher vertebrates [13]. Calpain like proteins were isolated from trema todes Schistosoma mansoni and S. japonicum, the fruit fly Drosophila melanogaster, several crustaceans and cephalopods, and their structure and properties have partially been studied [3,10,[14][15][16].…”
Section: Introductionmentioning
confidence: 99%
“…Ca 2+ -activated proteinases were detected in all vertebrate tissues [8] and in some invertebrates [7,14], but the mechanisms regulating activities of these proteinases are not yet studied sufficiently well [12]. One of these regulators, along with Ca 2+ , thiol groups, and calpastatin can be modification of the membrane microviscosity, which is largely determined by cholesterol.…”
mentioning
confidence: 99%
“…In addition to these enzymes, hepatopancreas contains chitinase, chitosanase [3], cathepsin [4], and elastase [5] activities. At present, king crab hepatopancreas is a commercial source of proteolytic enzymes, including collagenase KK.…”
mentioning
confidence: 99%