Molecular cloning of the ovine pituitary growth hormone releasin

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

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536 231, 435 691, 435 6, 435 912, 530350, C12N 1512, C12N 1510, C07K 1472

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active

058521879

ABSTRACT:
Growth hormone releasing hormone (GHRH) receptor binding has been characterized using a unique binding assay utilizing iodinated GHRH probes. Photoaffinity GHRH probes have been constructed which allow for photolabeling and characterization of the receptor. In addition, high affinity biotinylated GHRH analogs have been constructed. Solubilization of GHRH-R/GHRH complexes and extraction of specifically bound GHRH using a mild detergent solution, followed by affinity chromatography, leads to a substantially purified GHRH-R isolate. Electrophoretic treatment of the GHRH-R isolate produces GHRH-R of sufficient purity to conduct sequencing of the receptor. Cloning of a gene encoding for polypeptides (protein or fragments thereof) having GHRH-R activity is accomplished using a bacterial host, and the cloned gene is expressed in a mammalian cell line. In addition, molecular cloning of the ovine GHRH-R is provided.

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Wu et al., The effect of GH-releasing peptide-2 (GHRP-2 or KP 102) on GH secretion from primary cultured ovine pituitary cells can be abolished by specific GH-releasing factor (GRF) receptor antagonist, J. Endocrinol., 140: R9-13, 1994.
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