Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.
about
Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptidesCathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expressionCatestatin: a multifunctional peptide from chromogranin APyroglutamate-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.Mass spectrometry-based neuropeptidomics of secretory vesicles from human adrenal medullary pheochromocytoma reveals novel peptide products of prohormone processingUnique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides.Evaluation of silicon nitride as a substrate for culture of PC12 cells: an interfacial model for functional studies in neurons.Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's diseaseHuman cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters.Cathepsin L targeting in cancer treatment.Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expressionProteases for processing proneuropeptides into peptide neurotransmitters and hormones.Peptidomics of Cpe(fat/fat) mouse brain regions: implications for neuropeptide processingHuman pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin.Endopin serpin protease inhibitors localize with neuropeptides in secretory vesicles and neuroendocrine tissues.Differential accessibilities of dibasic prohormone processing sites of proenkephalin to the aqueous environment revealed by H-D exchange mass spectrometry.Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies.Zinc regulation of aminopeptidase B involved in neuropeptide production.Autophagy and cathepsin L are involved in the antinociceptive effect of DMBC in a mouse acetic acid-writhing modelSpecialized roles for cysteine cathepsins in health and disease.Profiles of secreted neuropeptides and catecholamines illustrate similarities and differences in response to stimulation by distinct secretagogues.Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis.The prohormone proenkephalin possesses differential conformational features of subdomains revealed by rapid H-D exchange mass spectrometry.Intrathecal implantation of microencapsulated PC12 cells reduces cold allodynia in a rat model of neuropathic pain.
P2860
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P2860
Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@en
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@nl
type
label
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@en
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@nl
prefLabel
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@en
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@nl
P2093
P2860
P356
P1476
Cathepsin L expression is dire ...... de biosynthesis and secretion.
@en
P2093
Charles Mosier
Christina Garza
Eric Wunderlich
Paul Goldsmith
Shin-Rong Hwang
Thomas Toneff
Vivian Hook
P2860
P304
P356
10.1074/JBC.M605510200
P407
P577
2007-01-23T00:00:00Z