Localization and characterization of human salivary kininases.

Abstract	The human saliva of normal subjects containing large amounts of basic carboxypeptidase produces decarboxylated non inflammatory peptides, for instance, kinins and anaphilotoxins C3a, C4a and C5a. A reduction of epithelial cell-bonded enzyme (carboxypeptidase M-type or kininase I), produces inflammations by the active intact kinins and the initiation of the alternative activating pathway of complement by active anaphilotoxins, which generate complement cleavage products, containing potential destructive mechanism.
Authors	G Porcelli, R Raffaelli, A Sacchi, A R Volpe, C Miani
Journal	Agents and actions. Supplements (Agents Actions Suppl) Vol. 38 ( Pt 1) Pg. 401-6 ( 1992) ISSN: 0379-0363 [Print] Switzerland
PMID	1466288 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	GPI-Linked Proteins Complement System Proteins Dipeptidyl-Peptidases and Tripeptidyl-Peptidases carboxypeptidase M Metalloendopeptidases
Topics	Complement System Proteins (metabolism) Dialysis Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (analysis, metabolism) GPI-Linked Proteins Humans Metalloendopeptidases (analysis, metabolism) Periodontal Diseases (diagnosis, enzymology) Saliva (enzymology) Substrate Specificity

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