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J. Biochem, 1995, Vol. 118, No. 3 521-525
© 1995 Japanese Biochemical Society

other

Release of a Soluble Form of Growth Hormone Receptors (Growth Hormone-Binding Proteins) from Human IM-9 Cells by Proteolytic Cleavage1

Yoshiro Saito, Hiderbaru Ikebuchi, Takeshi Yamazaki and Jun-ichi Sawada2

Division of Biochemistry and Immunochemistry, National Institute of Health Sciences 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158

2To whom correspondence should be addressed. Tel: +81-3-3700-1141, Fax: +81-3-3707-6950

Soluble forms of growth hormone receptors, growth hormone-binding proteins (GH-BPs), with molecular weights of 60 and 55 kDa were found to be constitutively released from human IM-9 cells. The release of the GH-BPs was not inhibited by inhibitors of protein synthesis (cycloheximide) and transport (brefeldin A). Down-regulation by human growth hormone or trypsin pretreatment of surface growth hormone receptors abolished the GH-BP release, suggesting that cell-surface human growth hormone receptors are involved in the GH-BP release. Several inhibitors of serine-, thiol-, and acid-proteases did not affect the GH-BP release. EDTA efficiently blocked the GH-BP release. This inhibition by EDTA was restored by addition of Mg2+ and Co2+. These results suggest that human GH-BPs are constitutively released by proteolytic cleavage of cell-surface growth hormone receptors by a metalloprotease.

1This study was supported in part by a grant from the Japan Health Science Foundation.


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