Amblyomma americanum (L.): Protein kinase C-independent fluid secretion by isolated salivary glands
Protein kinase C activity was partially purified from tick salivary glands by fast protein liquid chromatography anion-exchange chromatography. Enzyme activity was stimulated by Ca 2+, phosphatidylserine, and diacylglycerol with the highest activity observed in the presence of all three modulators....
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Published in | Experimental parasitology Vol. 74; no. 3; pp. 324 - 331 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
01.05.1992
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Protein kinase C activity was partially purified from tick salivary glands by fast protein liquid chromatography anion-exchange chromatography. Enzyme activity was stimulated by Ca
2+, phosphatidylserine, and diacylglycerol with the highest activity observed in the presence of all three modulators. Enzyme activity was inhibited by a synthetic pseudosubstrate peptide with an amino acid sequence resembling the protein kinase C substrate phosphorylation site. The protein kinase C activator, 1-oleoyl-2-acetyl-sn-glycerol (OAG), when added to whole
in vitro salivary glands previously prelabeled with
32P, stimulated the phosphorylation of salivary gland proteins. Activators of protein kinase C (phorbol ester or OAG) did not stimulate fluid secretion by isolated tick salivary glands. OAG and phorbol ester had only minimal affects on the ability of dopamine to stimulate secretion by isolated salivary glands and dopamine's ability to increase salivary gland cyclic AMP. |
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Bibliography: | L72 9184514 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0014-4894 1090-2449 |
DOI: | 10.1016/0014-4894(92)90156-5 |