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Journal ArticleDOI

Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo.

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TLDR
It is concluded that catestatin is a potent vasodilator in vivo whose actions appear to be mediated, at least in part, by histamine release and action at H1 receptors.
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This article is published in Peptides.The article was published on 1998-07-01. It has received 124 citations till now. The article focuses on the topics: Catecholamine & Histamine.

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Citations
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Journal ArticleDOI

Catecholaminergic Systems in Stress: Structural and Molecular Genetic Approaches

TL;DR: Data summarized here indicate that catecholaminergic systems are activated in different ways following exposure to distinct stressful stimuli.
Journal ArticleDOI

The Extended Granin Family: Structure, Function, and Biomedical Implications

TL;DR: The structure and function of granins and granin-derived peptides and expansive new genetic evidence are reviewed, including recent single-nucleotide polymorphism mapping, genomic sequence comparisons, and analysis of transgenic and knockout mice, which together support an important and evolutionarily conserved role for these proteins in large dense-core vesicle biogenesis and regulated secretion.
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The endocrine role for chromogranin A: a prohormone for peptides with regulatory properties.

TL;DR: Endocrine regulations are indicated from in vivo studies, consistent with the postulated prohormone function of CgA for peptides with regulatory properties, implicating C gA peptides in regulation of calcium and glucose metabolism, cardiovascular functions, gastrointestinal motility and nociception, tissue repair, inflammatory responses and in the first phase of microbial invasions.
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Early decline in the catecholamine release-inhibitory peptide catestatin in humans at genetic risk of hypertension.

TL;DR: It is concluded that catestatin is diminished early in the course of development of hypertension, even in the normotensive offspring of patients with the disease.
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The granin family of uniquely acidic proteins of the diffuse neuroendocrine system: comparative and functional aspects.

TL;DR: The chromogranins A and B and SgII constitute the main members of a family of uniquely acidic secretory proteins in elements of the diffuse neuroendocrine system, characterised by numerous pairs of basic amino acids as potential cleavage sites for processing by the co‐stored prohormone converting enzymes PC 1/3 and PC2.
References
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Journal ArticleDOI

The Pharmacological Basis of Therapeutics

Louis S. Goodman, +1 more
- 01 May 1941 - 
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Differentiation of receptor systems activated by sympathomimetic amines.

TL;DR: The classification of receptor systems which are activated by sympathomimetic amines has engaged the attention of many investigators as mentioned in this paper, who have suggested the convenient designations of alpha (α) and beta (β) to distinguish major differences in the responses elicited in various organ systems.
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The hydrophobic moment detects periodicity in protein hydrophobicity

TL;DR: The observation that many protein sequences tend to form segments of maximum amphiphilicity suggests that segments of secondary structure fold at a hydrophobic surface, probably formed from other parts of the folding protein.
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Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist.

TL;DR: This small domain within chromogranin A may contribute to a novel, autocrine, homeostatic (negative-feedback) mechanism controlling catecholamine release from chromaffin cells and neurons.
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Chromogranin A, the major catecholamine storage vesicle soluble protein. Multiple size forms, subcellular storage, and regional distribution in chromaffin and nervous tissue elucidated by radioimmunoassay.

TL;DR: A "family" of adrenal medulla chromogranins, similar structurally and immunoligically to CgA, is suggested, which may provide a useful tool for sympathoadrenal studies in intact organisms.
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