From nudeadultcams

Rated 4.5/5 based on 565 customer reviews

Recent studies have demonstrated that catecholamine release-inhibitory activity is generated when Cg A is co-incubated with chromaffin cells, suggesting that at least some component of the cleavage occurs extracellularly (as would occur after secretion) ().

Thus, the secretion of Cg A, followed by its appropriate proteolytic processing, may exert an autocrine/paracrine negative-feedback control on local catecholamine release.

Chromogranin A (Cg A) is the major soluble protein in the core of catecholamine-storage vesicles and is released with catecholamines by exocytosis from the chromaffin cells of the adrenal medulla and from sympathetic axons.

Cg A is found in secretory vesicles throughout the neuroendocrine system and may exemplify a prototypical prohormone precursor (), which inhibits parathyroid hormone release.

In addition, recent studies have revealed that Cg A may function as a prohormone from which peptides are released that modulate the function of catecholaminergic cells.

in: JCI | Pub Med | Google Scholar Chromogranin A (Cg A) is the major soluble protein in the core of catecholamine-storage vesicles and is also distributed widely in secretory vesicles throughout the neuroendocrine system. in: JCI | Pub Med | Google Scholar Department of Vascular Biology, The Scripps Research Institute, La Jolla, California, USA Address correspondence to: Robert J. Parmer, Nephrology/Hypertension (9111-H), University of California, San Diego, 3350 La Jolla Village Drive, San Diego, California 92161, USA. These results suggest that catecholaminergic cells express binding sites that localize fibrinolytic molecules on their surfaces to promote plasminogen activation and proteolytic processing of Cg A in the environment into which Cg A is secreted to generate peptides which may regulate neuroendocrine secretion. in: JCI | Pub Med | Google Scholar Department of Vascular Biology, The Scripps Research Institute, La Jolla, California, USA Address correspondence to: Robert J. Parmer, Nephrology/Hypertension (9111-H), University of California, San Diego, 3350 La Jolla Village Drive, San Diego, California 92161, USA. Positive and negative modulation of the local cellular fibrinolytic system resulted in substantial alterations in catecholamine release.Thus, plasminogen receptors function to localize the proteolytic activity of plasmin in the local milieu of cells, an environment into which prohormones are secreted directly.However, the fundamental importance of cell-surface receptors for plasminogen in regulating prohormone processing has not been investigated previously.

Leave a Reply