Determination of alpha-subunit contact regions of human follicle-stimulating hormone beta-subunit using synthetic peptides

Follicle-stimulating hormone (FSH) is a glycoprotein hormone composed of two different subunits designated FSH-alpha and FSH-beta. Using synthetic peptides corresponding to the primary structure of human (h) FSH-beta subunit, we previously identified two regions of the beta-subunit, hFSH-(33-53) and...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-02, Vol.266 (5), p.2759-2762
Main Authors: T A Santa-Coloma, L E Reichert, Jr
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Follicle Stimulating Hormone - genetics
Follicle Stimulating Hormone - metabolism
Fundamental and applied biological sciences. Psychology
Humans
Molecular Sequence Data
Peptides - metabolism
Protein hormones. Growth factors. Cytokines
Proteins
Receptors, FSH - genetics
Receptors, FSH - metabolism
Sequence Alignment
Substrate Specificity
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Summary:Follicle-stimulating hormone (FSH) is a glycoprotein hormone composed of two different subunits designated FSH-alpha and FSH-beta. Using synthetic peptides corresponding to the primary structure of human (h) FSH-beta subunit, we previously identified two regions of the beta-subunit, hFSH-(33-53) and hFSH-(81-95), as receptor binding regions. In this report, we tested the ability of synthetic peptides to interact with hFSH-alpha-subunit. Synthetic peptides corresponding to hFSH-beta-(11-25), (41-55), (51-65), and (101-111) were able to bind specifically radioiodinated hFSH-alpha-subunit, suggesting that they represent regions of interaction with the alpha-subunit. These experimental results were in agreement with the location of alpha-subunit contact regions predicted by sequence analysis. Peptides of hFSH-beta-subunit showing maximum specific binding to the alpha-subunit were those possessing minimum interaction with receptor whereas those not binding to alpha-subunit corresponded to regions shown to interact with receptor (hFSH-beta-(33-53) and hFSH-beta-(81-95]. The hFSH-beta-subunit, therefore, seems to have two discontinuous receptor binding regions flanked by three alpha-subunit contact regions.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)49910-3