title: 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: Center of Receptors Chemistry of the National Research Council (C.N.R.), Medical Faculty, Catholic University, Rome, Italy.
authors: G
authors: G
authors: Porcelli
authors: R
authors: R
authors: Raffaelli
authors: A
authors: A
authors: Sacchi
authors: A R
authors: AR
authors: Volpe
authors: C
authors: C
authors: Miani
mesh_terms: D003165:Complement System Proteins / Q000378:metabolism; D003956:Dialysis; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000032:analysis / Q000378:metabolism*; D058851:GPI-Linked Proteins; D006801:Humans; D008666:Metalloendopeptidases / Q000032:analysis / Q000378:metabolism*; D010510:Periodontal Diseases / Q000175:diagnosis / Q000201:enzymology; D012463:Saliva / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D058851:GPI-Linked Proteins; D003165:Complement System Proteins; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C058479:carboxypeptidase M; D008666:Metalloendopeptidases