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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Bibliographic Details
Published inExperimental parasitology Vol. 74; no. 3; pp. 324 - 331
Main Authors McSwain, Janis L., Masaracchia, Ruthann A., Essenberg, R.C., Tucker, James S., Sauer, J.R.
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 01.05.1992
Elsevier
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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.
Bibliography:L72
9184514
ObjectType-Article-2
SourceType-Scholarly Journals-1
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content type line 23
ISSN:0014-4894
1090-2449
DOI:10.1016/0014-4894(92)90156-5