Linked Life Data

8987779

Source:http://linkedlifedata.com/resource/pubmed/id/8987779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-11-28
pubmed:abstractText
The prohormone convertases (PCs) are processing enzymes that activate proproteins via cleavage at specific single or pairs of basic residues. The hypothalamic paraventricular nucleus (PVN) and supraoptic nucleus (SON) are primary sites of biosynthesis of several neuroendocrine hormone precursors, including provasopressin (pro-AVP), pro-oxytocin (pro-OT), and procorticotrophin-releasing hormone (pro-CRH), which require post-translational processing to yield active products. Using in situ hybridization, we observed PC1 and PC5 mRNAs in PVN and SON magnocellular neurons, while PC2 mRNA was observed in both magnocellular and parvocellular PVN neurons as well as magnocellular SON neurons. Similar to furin, PC7 mRNA was expressed throughout the PVN and SON, whereas PACE4 mRNA levels were undetectable. Both immunohistochemical and Western blot studies were performed to demonstrate the presence of PC proteins and forms in the PVN and SON. Using double-labeling in situ hybridization, we examined the cellular colocalization of each PC mRNA with pro-AVP, pro-OT, and pro-CRH mRNAs in PVN and SON. PC1 mRNA was colocalized with both AVP and OT mRNA in PVN and SON magnocellular neurons. All AVP, OT, and CRH neurons expressed PC2. In contrast, PC5 mRNA was colocalized only with OT mRNA. We examined the effects of adrenalectomy (ADX) on PVN PC mRNA levels. PC1 mRNA levels were increased selectively within CRH/AVP parvocellular neurons but were unchanged in PVN magnocellular AVP or OT neurons. These results established the anatomical organization of each convertase and proneuropeptide substrates in the PVN and SON and suggested potential roles for each enzyme under resting and stimulated conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0270-6474
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
563-75
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8987779-Adrenalectomy, pubmed-meshheading:8987779-Animals, pubmed-meshheading:8987779-Arginine Vasopressin, pubmed-meshheading:8987779-Aspartic Acid Endopeptidases, pubmed-meshheading:8987779-Corticosterone, pubmed-meshheading:8987779-Corticotropin-Releasing Hormone, pubmed-meshheading:8987779-Dexamethasone, pubmed-meshheading:8987779-Enzyme Induction, pubmed-meshheading:8987779-Glucocorticoids, pubmed-meshheading:8987779-Male, pubmed-meshheading:8987779-Nerve Tissue Proteins, pubmed-meshheading:8987779-Neurons, pubmed-meshheading:8987779-Organ Specificity, pubmed-meshheading:8987779-Oxytocin, pubmed-meshheading:8987779-Paraventricular Hypothalamic Nucleus, pubmed-meshheading:8987779-Proprotein Convertases, pubmed-meshheading:8987779-RNA, Messenger, pubmed-meshheading:8987779-Rats, pubmed-meshheading:8987779-Rats, Sprague-Dawley, pubmed-meshheading:8987779-Supraoptic Nucleus
pubmed:year
1997
pubmed:articleTitle
Cellular localization of the prohormone convertases in the hypothalamic paraventricular and supraoptic nuclei: selective regulation of PC1 in corticotrophin-releasing hormone parvocellular neurons mediated by glucocorticoids.
pubmed:affiliation
J. A. DeSève Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montréal, Québec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't