Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules.
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Catestatin, a neuroendocrine antimicrobial peptide, induces human mast cell migration, degranulation and production of cytokines and chemokinesProteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH(2)-terminal Edman peptide sequencing and MALDI-TOF MSPro-hormone secretogranin II regulates dense core secretory granule biogenesis in catecholaminergic cells.Catestatin: a multifunctional peptide from chromogranin AChromogranin A: a surprising link between granule biogenesis and hypertensionBoth rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology.Pyroglutamate-amyloid-β and glutaminyl cyclase are colocalized with amyloid-β in secretory vesicles and undergo activity-dependent, regulated secretion.Proteomics of dense core secretory vesicles reveal distinct protein categories for secretion of neuroeffectors for cell-cell communication.Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo.Correlation of plasma catestatin level and the prognosis of patients with acute myocardial infarctionProteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin.Novel peptide isomer strategy for stable inhibition of catecholamine release: application to hypertensionChromogranin A - unspecific neuroendocrine marker. Clinical utility and potential diagnostic pitfallsChromogranin B: intra- and extra-cellular mechanisms to regulate catecholamine storage and release, in catecholaminergic cells and organisms.Increased plasma level of catestatin might be associated with poor prognosis in hemodialysis patients.Potential applications of catestatin in cardiovascular diseases.A molecular dynamics study of catestatin docked on nicotinic acetylcholine receptors to identify amino acids potentially involved in the binding of chromogranin A fragments.Chromogranin A Regulation of Obesity and Peripheral Insulin Sensitivity.Secretory granule biogenesis in sympathoadrenal cells: identification of a granulogenic determinant in the secretory prohormone chromogranin A.Profiles of secreted neuropeptides and catecholamines illustrate similarities and differences in response to stimulation by distinct secretagogues.Catecholamine secretory vesicle stimulus-transcription coupling in vivo. Demonstration by a novel transgenic promoter/photoprotein reporter and inhibition of secretion and transcription by the chromogranin A fragment catestatin.Presence of cellular renin-angiotensin system in chromaffin cells of bovine adrenal medulla.Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.Pleiotropic effects of novel trans-acting loci influencing human sympathochromaffin secretion.D-Cateslytin: a new antifungal agent for the treatment of oral Candida albicans associated infections.
P2860
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P2860
Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Formation of the catecholamine ...... s in hormone storage granules.
@en
type
label
Formation of the catecholamine ...... s in hormone storage granules.
@en
prefLabel
Formation of the catecholamine ...... s in hormone storage granules.
@en
P2093
P2860
P356
P1476
Formation of the catecholamine ...... s in hormone storage granules.
@en
P2093
Caporale C
O'Connor DT
Taupenot L
P2860
P304
22905-22915
P356
10.1074/JBC.M001232200
P407
P577
2000-07-01T00:00:00Z