Tissue‐specific molecular heterogeneity of human growth hormone‐releasing hormone receptor protein

FEBS Letters

Saito, Shiro²  Zhang, Chen-Yu²  Fujinaka, Yuichi²  Okura, Toshihiro²  Yokogoshi, Yutaka²  Kitagawa, Kouki¹ 

[1] Department of Chemistry and Pharmaceutical Technology, Niigata College of Pharmacy, 5-13-2 Kamishimei, Niigata 950-21, Japan;First Department of Internal Medicine, School of Medicine, The University of Tokushima, 3-18 Kuramoto-cho, Tokushima 770, Japan

关键词: GHRH;    GHRH receptor;    Anti-peptide antibody;    Molecular heterogeneity;    Immunoblotting;    Kidney;    GH;    growth hormone;    GHRH;    growth hormone-releasing hormone;   

DOI  :  10.1016/0014-5793(96)00917-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A site-directed anti-peptide antibody (anti-hGHRHRc18) was generated against the cytoplasmic tail of human GHRH receptor. The dissociation constant (K _d ) and the antibody binding site (AbT) of anti-hGHRHRc18 were 2.5 nmol/l and 0.54 nmol/l, respectively. In an immunoblotting experiment, affinity-purified anti-hGHRHRc18 specifically recognized a single 50-kDa protein in human pituitary. In a screening of the expression of GHRH receptor protein in extra-pituitary tissues, only human kidney showed a single 52-kDa protein. Our results suggest that the GHRH receptor protein exhibits tissue-specific molecular heterogeneity.

【 授权许可】

Unknown