Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1988-4-21
pubmed:abstractText
The binding of 125I-VIP to human lung cancer cell lines was investigated. Radiolabeled VIP bound to adenocarcinoma, squamous cell carcinoma, large cell carcinoma and small cell lung cancer (SCLC) cell lines. As SCLC cell line NCI-N592 bound radiolabeled VIP well, its binding was further characterized. 125I-VIP bound to membranes in a specific and time dependent manner. 125I-VIP bound with high (Kd = 0.8 nM) and moderate affinity (Kd = 66 nM) to two classes of sites. Pharmacology studies indicated that the order of peptide potency was VIP much greater than PHI greater than secretin greater than VIP10-28. Because VIP receptors are present on human lung cancer cells, VIP may function as a regulatory peptide in lung cancer.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0196-9781
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1101-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
High affinity binding of VIP to human lung cancer cell lines.
pubmed:affiliation
Department of Biochemistry, George Washington University School of Medicine and Health Sciences, Washington, DC 20037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.