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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1993-9-30
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pubmed:abstractText |
To clarify the possible role of calpain (calcium activated neutral protease; EC 3.4.22.17) in Ca2+ homeostasis of human platelets, we investigated the effects of cell permeable calpain inhibitors, calpeptin and E-64d (EST), on the restoration of cytoplasmic Ca2+ ([Ca2+]i) in both Fura-2 and aspirin (ASA) loaded platelets. Although neither calpeptin (30 microM) nor EST (250 microM) altered the increase of [Ca2+]i in thrombin (1 U/ml) stimulated platelets, both calpain inhibitors delayed the decrease of [Ca2+]i back towards the basal level. These observations suggested that calpain might be involved in Ca2+ restoration. Then, the activity of Ca(2+)-ATPase was examined in thrombin (2 U/ml) stimulated platelets. Thrombin produced a rapid rise in Ca(2+)-ATPase activity by 2-fold at 8 s of incubation, which then returned to below the basal activity within 2 min. Calpeptin inhibited transient Ca(2+)-ATPase activation induced by thrombin in a dose related manner. Ca(2+)-ATPase of isolated platelet membranes was digested by purified human platelet calpain-I and Ca(2+)-ATPase activity was investigated. With a short incubation (8-15 s), Ca(2+)-ATPase activity was increased about 2-fold and then it decreased below the basal level at longer incubations or at a higher calpain/membrane ratio. The initial rate of Ca2+ uptake was also increased by about 2-fold with a short incubation (8-15 s). For molecular characterization of the Ca(2+)-ATPase, the formation of the enzyme-phosphate complex (EP) was investigated. The membrane bound intact 105 kD Ca(2+)-ATPase was converted by calpain to a fragment of approximately 50 kD.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aspirin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin,
http://linkedlifedata.com/resource/pubmed/chemical/aloxistatin,
http://linkedlifedata.com/resource/pubmed/chemical/calpeptin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0143-4160
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
455-63
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8395339-Aspirin,
pubmed-meshheading:8395339-Blood Platelets,
pubmed-meshheading:8395339-Calcimycin,
pubmed-meshheading:8395339-Calcium,
pubmed-meshheading:8395339-Calcium-Transporting ATPases,
pubmed-meshheading:8395339-Calpain,
pubmed-meshheading:8395339-Cell Compartmentation,
pubmed-meshheading:8395339-Dipeptides,
pubmed-meshheading:8395339-Enzyme Activation,
pubmed-meshheading:8395339-Homeostasis,
pubmed-meshheading:8395339-Humans,
pubmed-meshheading:8395339-Intracellular Membranes,
pubmed-meshheading:8395339-Leucine,
pubmed-meshheading:8395339-Multienzyme Complexes,
pubmed-meshheading:8395339-Platelet Activation,
pubmed-meshheading:8395339-Stimulation, Chemical,
pubmed-meshheading:8395339-Thrombin
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pubmed:year |
1993
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pubmed:articleTitle |
Stimulation of human platelet Ca(2+)-ATPase and Ca2+ restoration by calpain.
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pubmed:affiliation |
Department of Surgery II, Osaka University Medical School, Fukushima, Japan.
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pubmed:publicationType |
Journal Article
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