Linked Life Data

1534126

Source:http://linkedlifedata.com/resource/pubmed/id/1534126

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1992-6-23
pubmed:abstractText
Previous research on growth hormone-releasing factor analogues has used pituitary cell culture assay systems to evaluate in vitro their biological activity. However, binding assay systems in which receptor affinity and peptide stability can be assessed independently have been lacking so far. Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues. Acylation of the N-terminus of hGRF(1-29)NH2 generally decreased its affinity (relative affinity to hGRF(1-29)NH2 (RA), 26-85%). Replacement of the C-terminal carboxamide by a free carboxylic function decreased affinity likely by diminishing its proteolytic stability (RA, 57%). Removal of Tyr1, Ser9, Lys12, Val13, Gly15, Gln16, or Lys21 drastically decreased its affinity (RA, less than 3%). Multiple amino acid deletions in the segment 13-21 of hGRF(1-29)NH2 also led to a loss of affinity as did replacing segment 13-15, 16-18, or 19-21 by an octanoyl moiety (RA, less than 1%). Removal of Asn8, Gln24, Asp25, Ile26, Met27, and Ser28 or Arg29 had less effect on GRF receptor affinity (RA, 5-33%). Removal of Met27 or Ser28 only slightly affected hGRF(1-29)NH2 affinity (RA, 62-78%). Altogether, these results indicate that the amino acids contained in the segment 13-21 are more important than those of 24-29 to insure high affinity receptor binding or to maintain an optimal conformation to allow GRF binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1864-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Affinity of human growth hormone-releasing factor (1-29)NH2 analogues for GRF binding sites in rat adenopituitary.
pubmed:affiliation
Neuroendocrinology Laboratory, Notre-Dame Hospital Research Center, Montreal, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't