scholarly journals Identification of phosphatidylserine-binding proteins in human white blood cells

1990 ◽  
Vol 269 (3) ◽  
pp. 723-728 ◽  
Author(s):  
M Wolf ◽  
M Baggiolini
Keyword(s):  
Protein Kinase C ◽  
Blood Cells ◽  
Binding Proteins ◽  
White Blood Cells ◽  
Human Neutrophils ◽  
Kinase C ◽  
Sds Page ◽  
Molecular Masses ◽  
Human White Blood Cells ◽  
Monocytes And Lymphocytes

Cytosol and membrane fractions from human neutrophils, monocytes, lymphocytes and platelets were separated by SDS/PAGE, blotted on to nitrocellulose and assayed for selective binding of phosphatidylserine (PS). Two PS-binding proteins with apparent molecular masses of 115 kDa and 100 kDa were identified in the cytosol of neutrophils, monocytes and lymphocytes. Corresponding bands along with other PS-binding proteins were detected in platelets in both cytosol and membrane fractions. These proteins were also found to bind protein kinase C (PKC) provided that PS was present. The 115 kDa and 100 kDa proteins (PS-p115/110) were partially purified from neutrophils and were used for the study of PS and PKC binding. The binding of PS did not require Ca2+ or Mg2+ and was inhibited by phosphatidic acid, by 1-alkyl-2-acetylphosphocholine and, to a lesser extent, by other lipids. The binding of PKC, however, was strictly PS- and Ca2(+)-dependent and seems to occur secondarily to PS binding.

scholarly journals Defective phosphorylation of a calmodulin-binding protein in cystic-fibrosis submandibular glands

1989 ◽  
Vol 263 (2) ◽  
pp. 613-616 ◽  
Author(s):  
D K Shori ◽  
R L Dormer ◽  
M C Goodchild ◽  
M A McPherson
Keyword(s):  
Cystic Fibrosis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Proteins ◽  
Binding Protein ◽  
Submandibular Glands ◽  
Calmodulin Binding ◽  
Kinase C ◽  
Exogenous Protein ◽  
Molecular Masses

Calmodulin-binding proteins in fractions purified from human submandibular glands by calmodulin-Sepharose were phosphorylated with [gamma-32P]ATP, in the absence of exogenous protein kinase. The major proteins phosphorylated had molecular masses of 45, 51 and 61 kDa. Phosphorylation was increased by activators of protein kinase C and inhibited by H-7. Phosphorylation of the 61 kDa band was markedly decreased in cystic-fibrosis submandibular glands.

scholarly journals Changes in protein kinase C ∊ phosphorylation status and intracellular localization as 3T3 and 3T6 fibroblasts grow to confluency and quiescence: a role for phosphorylation at Ser-729?

2000 ◽  
Vol 352 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Karen ENGLAND ◽  
Martin G. RUMSBY
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Intracellular Localization ◽  
C6 Glioma Cells ◽  
Nuclear Fraction ◽  
Cell Fractionation ◽  
Cytosol Fraction ◽  
Kinase C ◽  
Sds Page ◽  
Molecular Masses

Protein kinase C (PKC) ε in 3T3 and 3T6 fibroblasts and in C6 glioma cells migrated on SDS/PAGE predominantly as a doublet with molecular masses of 87 and 95kDa (PKC ε87 and PKC ε95 respectively). PKC ε95 predominates when cells reach confluency but PKC ε87 was the main form detected within 15min when confluent cells were passaged at low cell density into fresh medium containing serum and allowed to adhere. Matrix-assisted laser-desorption ionization–time-of-flight MS analysis and experiments with phosphospecific antibodies revealed that PKC ε87 is phosphorylated at Thr-566 and Ser-703, and PKC ε95 is additionally phosphorylated at Ser-729. Cell fractionation studies revealed that PKC ε95 is associated with the nuclear fraction, whereas PKC ε87 was found in the 100000g cytosol fraction. Immunofluorescence studies confirmed these findings and showed that PKC ε95 had a perinuclear, probably Golgi, localization and PKC ε87 was distributed in the cytosol. It is proposed that phosphorylation at Ser-729 may be important for determining the intracellular localization of PKC ε, and that a specific Ser-729 phosphatase may be activated on cell passage to convert PKC ε95 to PKC ε87.

The protein kinase C inhibitor H-7 activates human neutrophils: effect on shape, actin polymerization, fluid pinocytosis and locomotion

1990 ◽  
Vol 96 (1) ◽  
pp. 99-106
Author(s):  
H.U. Keller ◽  
V. Niggli ◽  
A. Zimmermann ◽  
R. Portmann
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Actin Polymerization ◽  
Kinase Inhibitor ◽  
Human Neutrophils ◽  
Kinase C ◽  
Chemotactic Peptides ◽  
Protein Kinase C Inhibitor ◽  
Shape Changes ◽  
Stimulation Of

The present study demonstrates new properties of H-7. The protein kinase inhibitor H-7 is a potent activator of several neutrophil functions. Stimulation of initially spherical nonmotile neutrophils elicits vigorous shape changes within a few seconds, increases in cytoskeletal actin, altered F-actin distribution, increased adhesiveness and a relatively small increase in pinocytic activity. H-7 has also chemokinetic activities. Depending on the experimental condition, H-7 may elicit or inhibit neutrophil locomotion. It failed to induce chemotaxis. Thus, the response pattern elicited by H-7 is different from that of other leukocyte activators such as chemotactic peptides, PMA or diacylglycerols. The finding that H-7 can elicit shape changes, actin polymerization and pinocytosis suggests that these events can occur without activation of protein kinase C (PKC). PMA-induced shape changes and stimulation of pinocytosis were not inhibited by H-7.

scholarly journals Supernatants and lipids from stored red blood cells activate pulmonary microvascular endothelium through the BLT2 receptor and protein kinase C activation

Transfusion ◽  
2017 ◽  
Vol 57 (11) ◽  
pp. 2690-2700 ◽  
Author(s):  
Christopher C. Silliman ◽  
Marguerite R. Kelher ◽  
Samina Y. Khan ◽  
F. Bernadette West ◽  
Nathan J.D. McLaughlin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Microvascular Endothelium ◽  
Kinase C ◽  
Protein Kinase C Activation

A new group of glucocerebrosidase isozymes found in human white blood cells

1980 ◽  
Vol 97 (3) ◽  
pp. 1103-1107 ◽  
Author(s):  
Edward I. Ginns ◽  
Roscoe O. Brady ◽  
Daniel W. Stowens ◽  
F.Scott Furbish ◽  
John A. Barranger
Keyword(s):  
Blood Cells ◽  
White Blood Cells ◽  
Human White Blood Cells
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