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Thrombin and melittin activate phospholipase C in human HaCaT keratinocytes
Author(s) -
Haase I.,
Czarnetzki B. M.,
Rosenbach T.
Publication year - 1996
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/j.1600-0625.1996.tb00099.x
Subject(s) - phospholipase c , second messenger system , phosphoinositide phospholipase c , gq alpha subunit , hacat , thrombin , chemistry , inositol trisphosphate , microbiology and biotechnology , phosphatidylinositol , inositol , biochemistry , phospholipase , receptor , biology , signal transduction , g protein , enzyme , immunology , platelet , in vitro
Following the activation of specific receptors, phospholipase C has been shown to cleave the membrane phospholipid phosphatidylinositol bisphosphate into the 2nd messengers inositol 1,4,5‐trisphosphate and di‐acylgiycerol. Both 2nd messengers contribute to the regulation of cellular proliferation. The receptor for bradykinin is coupled to this pathway in keratinocytes, but knowledge about other activators of phospholipase C is limited. Additional mediators and agents were therefore examined regarding their ability to activate phospholipase C in HaCaT keratinocytes. Analysis for 3 H‐inositol phosphates was performed by anion‐exchange HPLC. Thrombin and melittin induced a time‐ and dose‐dependent release of inositol 1,4,5‐trisphosphate. Several other mediators examined such as angiotension II, neurotensin, C3a, pituitary adenylate cyclase activating peptide, phenylephrin, and prostaglandin E 2 , did not induce the formation of inositol phosphates. In view of the mitogenic activity and the increased formation of thrombin after tissue injury, the coupling of the thrombin receptor to phospholipase C in HaCaT keratinocytes suggests a rôle of this protease in epidermal wound healing.