Classical second messengers are not involved in proteinase-induced degranulation of airway gland serous cells. Sommerhoff, Christian P., Kenneth C. Fang, Jay A. Nadel, and George H. Caughey. Cardiovascular Research Institute and Departments of Medicine and Physiology, University of California San Francisco, San Francisco, CA 94143-0130
APStracts 3:0115L, 1996.
Neutral serine proteinases such as mast cell chymase, cathepsin G, and neutrophil elastase are far more potent secretagogues for airway gland serous cells than all other agonists studied (e.g., histamine and bradykinin). To determine the mechanism of proteinase-induced secretion, we investigated the stimulation-secretion coupling in cultured bovine serous cells. Histamine stimulates degranulation of serous cells via cAMP-, protein kinase C-, and [Ca2+]i-dependent pathways. Similarly, bradykinin-induced secretion involves inositol phosphates, protein kinaseEC, and [Ca2+]i. Degranulation caused by both agonists also depends on the activity of an endogenous metalloprotease which is required in a late step of stimulation -secretion coupling, i.e. after the calcium entry. Based on the effect of different inhibitors, this metalloprotease is a Zn2+- and Ca2+ -dependent enzyme similar to a gelatinase A synthesised by serous cells. In marked contrast to other secretagogues, degranulation induced by chymase, cathepsin G, and neutrophil elastase neither involves the classical second messen gers nor the activity of the endogenous metalloprotease. These observations suggest that exogenous proteinases like chymase, cathepsin G and elastase may substitute for or mimic the action of an endogenous metalloprotease and directly activate degranulation, bypassing the signal transduction mechanisms necessary for secretion caused by other agonists.

Received 14 February 1995; accepted in final form 10 June 1996.
APS Manuscript Number L45-5.
Article publication pending Am. J. Physiol. (Lung Cell. Mol.
Physiology).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 25 July 1996