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Secretory character of a group of isoproterenol‐induced polypeptides in mouse parotid glands
Author(s) -
Solís Remigio O. López,
Miranda Dante,
Alliende Cecilia,
González Julieta,
Díaz Nelson,
Díaz Héctor,
Ruiz Fernando
Publication year - 1989
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041410326
Subject(s) - secretion , parotid gland , stimulation , endocrinology , cytoplasm , medicine , secretory protein , amylase , chemistry , polyacrylamide gel electrophoresis , enzyme , biology , microbiology and biotechnology , biochemistry , pathology
Abstract The secretory nature of the isoproterenol‐induced mouse parotid polypeptides C, D, E, F, and G (molecular weights 64,000, 61,000, 51,500, 38,000, and 37,000, respectively) is documented. Polypeptides C, D, E, F, and G, accumulated in response to successive daily stimulations with isoproterenol, were detected in a fraction enriched in hypertrophic parotid acinar cells. These cells, characterized by an increased content of cytoplasmic granules, maintain a secretory responsiveness to isoproterenol, which has been evidenced by light microscopy, enzymatic analysis, and unidimensional SDS‐polyacrylamide gel electrophoresis. Thus, a parallelism in the loss and recovery of both secretory granules, α‐amylase and polypeptides C, D, E, F, and G, was observed. Moreover, after secretion stimulation, polypeptides C, D, E, F, and G were detected in the fluid collected directly from parotid gland cannulation. Given the secretory character of polypeptides C, D, E, F, and G, mechanisms explaining both their progressive accumulation along the chronic administration of isoproterenol, as well as their progressive disappearance observed after suspending that treatment, are discussed.