Abstract
In the presence of micromolar concentrations of Ca2+, both protein kinase C and a cytosolic Ca2+-requiring neutral proteinase of human neutrophils become associated with the neutrophil membrane. Binding to the membrane results in activation of the proteinase, which then catalyzes limited proteolysis of the kinase to produce a form that is fully active in the absence of Ca2+ and phospholipid. This irreversibly activated protein kinase is released from the membrane and may thus have access, in the intact cell, to intracellular protein substrates. In the absence of proteinase, Ca2+ promotes the binding of protein kinase C, but conversion to the Ca2+/phospholipid-independent form does not occur and the kinase remains associated with the membrane fraction.
| Original language | English |
|---|---|
| Pages (from-to) | 6435-6439 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 82 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 1985 |
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ASJC Scopus subject areas
- Genetics
- General
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Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase. / Melloni, E.; Pontremoli, S.; Michetti, M.; Sacco, O.; Sparatore, B.; Salamino, F.; Horecker, B. L.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 82, No. 19, 1985, p. 6435-6439.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase
AU - Melloni, E.
AU - Pontremoli, S.
AU - Michetti, M.
AU - Sacco, O.
AU - Sparatore, B.
AU - Salamino, F.
AU - Horecker, B. L.
PY - 1985
Y1 - 1985
N2 - In the presence of micromolar concentrations of Ca2+, both protein kinase C and a cytosolic Ca2+-requiring neutral proteinase of human neutrophils become associated with the neutrophil membrane. Binding to the membrane results in activation of the proteinase, which then catalyzes limited proteolysis of the kinase to produce a form that is fully active in the absence of Ca2+ and phospholipid. This irreversibly activated protein kinase is released from the membrane and may thus have access, in the intact cell, to intracellular protein substrates. In the absence of proteinase, Ca2+ promotes the binding of protein kinase C, but conversion to the Ca2+/phospholipid-independent form does not occur and the kinase remains associated with the membrane fraction.
AB - In the presence of micromolar concentrations of Ca2+, both protein kinase C and a cytosolic Ca2+-requiring neutral proteinase of human neutrophils become associated with the neutrophil membrane. Binding to the membrane results in activation of the proteinase, which then catalyzes limited proteolysis of the kinase to produce a form that is fully active in the absence of Ca2+ and phospholipid. This irreversibly activated protein kinase is released from the membrane and may thus have access, in the intact cell, to intracellular protein substrates. In the absence of proteinase, Ca2+ promotes the binding of protein kinase C, but conversion to the Ca2+/phospholipid-independent form does not occur and the kinase remains associated with the membrane fraction.
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UR - http://www.scopus.com/inward/citedby.url?scp=0344283330&partnerID=8YFLogxK
U2 - 10.1073/pnas.82.19.6435
DO - 10.1073/pnas.82.19.6435
M3 - Article
C2 - 2995965
AN - SCOPUS:0344283330
VL - 82
SP - 6435
EP - 6439
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 19
ER -