Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2 Pt 1
pubmed:dateCreated
1993-4-2
pubmed:abstractText
Vasoactive intestinal peptide (VIP) receptors were characterized in epithelial plasma membranes from human small intestine. Native VIP inhibited the binding of 125I-labeled VIP to jejunal membranes, and Scatchard analysis of these data was consistent with the existence of one class of receptor with a dissociation constant of 42 pM and a maximal binding of 256 fmol/mg membrane protein. VIP stimulated adenylyl cyclase activity in human jejunal membranes in the 0.01 nM-1 microM range [half-maximal effective dose = 0.7 nM]. Coupling of VIP receptors with a Gs protein was further assessed by the ability of GTP (10(-8) to 10(-3) M) to inhibit 125I-VIP binding to membranes. 125I-VIP binding was seven to eight times higher in villus cells than in crypt cells. Finally, 125I-VIP binding was detectable throughout the small and large intestines with the highest binding in jejunum. Among the natural peptides structurally related to VIP, some inhibited 125I-VIP binding with the following order of potency: VIP = pituitary adenylate cyclase-activating peptide (PACAP)-27 = PACAP-38 > helodermin >> peptide histidine methionineamide = human growth hormone-releasing factor > secretin. The same order of potency of peptides for inhibiting 125I-VIP or 125I-labeled PACAP was observed, supporting that the two tracers bound to a common VIP-PACAP receptor site. This order of potency was also observed for the stimulation of adenylyl cyclase activity by these peptides. 125I-VIP was cross-linked to membranes using disuccinimidyl suberate. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, one single band of 70,000 mol wt was observed.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
E294-300
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8383439-Binding, Competitive, pubmed-meshheading:8383439-Cell Aging, pubmed-meshheading:8383439-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8383439-Epithelium, pubmed-meshheading:8383439-Humans, pubmed-meshheading:8383439-Intestinal Mucosa, pubmed-meshheading:8383439-Jejunum, pubmed-meshheading:8383439-Neuropeptides, pubmed-meshheading:8383439-Pituitary Adenylate Cyclase-Activating Polypeptide, pubmed-meshheading:8383439-Receptors, Cell Surface, pubmed-meshheading:8383439-Receptors, Gastrointestinal Hormone, pubmed-meshheading:8383439-Receptors, Pituitary Adenylate Cyclase-Activating..., pubmed-meshheading:8383439-Receptors, Pituitary Hormone, pubmed-meshheading:8383439-Receptors, Vasoactive Intestinal Peptide, pubmed-meshheading:8383439-Tissue Distribution, pubmed-meshheading:8383439-Vasoactive Intestinal Peptide
pubmed:year
1993
pubmed:articleTitle
Characterization of a common VIP-PACAP receptor in human small intestinal epithelium.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale, Unité 239, Faculté de Médecine X. Bichat, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't