Abstract:
:Receptor binding analysis was performed in the renal medulla from 2-month-old rats, an extrapituitary tissue containing the highest level of GHRH receptor mRNA. At 4 degrees C, in the presence of a cocktail of protease inhibitors, binding of [125I-Tyr(10)]hGHRH (1-44)NH(2) to medullary homogenates was specific, time-dependent, reversible and saturable (K(d): 28 nM; B(max): 30 fmol/mgprot.). In these experimental conditions, no change of binding parameters could be detected in the course of aging. The structure-affinity profile was different in the two tissues and chemical cross-linking revealed the presence of 65-, 55- and 38-kDa 125I-GHRH-labeled complexes in the renal medulla compared to 65-, 47- and 28-kDa radioactive complexes in the anterior pituitary. It is suggested that GHRH binding sites, and possibly the receptor, may be different in the two tissues.
journal_name
Peptidesjournal_title
Peptidesauthors
Boulanger L,Girard N,Strecko J,Gaudreau Pdoi
10.1016/s0196-9781(02)00029-3subject
Has Abstractpub_date
2002-06-01 00:00:00pages
1187-94issue
6eissn
0196-9781issn
1873-5169pii
S0196978102000293journal_volume
23pub_type
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