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Karen B. Helle

Researcher at University of Bergen

Publications -  118
Citations -  4208

Karen B. Helle is an academic researcher from University of Bergen. The author has contributed to research in topics: Chromogranin A & Adrenal medulla. The author has an hindex of 36, co-authored 118 publications receiving 4056 citations.

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Morphological evidence for a dopaminergic terminal field in the hippocampal formation of young and adult rat.

TL;DR: The hippocampostriatal projections, that represent a link between the limbic and central motor mechanisms, could be under dopaminergic influence.
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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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The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels.

TL;DR: A vascular role for the N-terminal domain of CGA is indicated, presumably by inhibiting Ca2+ release from intracellular stores in the human vein but not the artery, and a vasoinhibitory activity in vasostatin is demonstrated.
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Vasostatins, comprising the N-terminal domain of chromogranin A, suppress tension in isolated human blood vessel segments.

TL;DR: The present study reports on the novel vasoinhibitory effect of the N‐terminal domain of the adrenomedullary CGA in isolated segments of the human internal thoracic artery and saphenous vein, suggesting that inhibition of Ca2 channel opening might indirectly contribute to the effect of vasostatins on the sustained response to ET‐1.
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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.