Linked Life Data

11956180

Source:http://linkedlifedata.com/resource/pubmed/id/11956180

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-4-16
pubmed:abstractText
Ghrelin is an acylated peptide recently isolated from rat stomach that potently stimulates GH release in vitro and in vivo in rat and man. Ghrelin specifically activates the receptor for the growth hormone secretagogues (GHS-Rla), and it has been proposed as the endogenous ligand mimicked by these synthetic compounds. Very recently, it was shown in cells transfected with the GHS-Rla that short acylated peptides encompassing the first 4-5 residues of ghrelin were capable of increasing intracellular calcium almost as efficiently as the full-length ghrelin. In the present study, we demonstrate that truncated analogs of ghrelin are ineffective in stimulating GH release in neonatal rats and do not displace radiolabelled ghrelin from binding sites in membranes from human hypothalamus and pituitary. In conclusion, our data demonstrate that the ability of short ghrelins to stimulate the GHS-Rla in transfected cells is not predictive of their capability to stimulate GH secretion in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
143
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1968-71
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Short ghrelin peptides neither displace ghrelin binding in vitro nor stimulate GH release in vivo.
pubmed:affiliation
Department of Experimental and Environmental Medicine and Biotechnologies, University of Milano-Bicocca, Milan, Italy. antonio.torsello@unimib.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't