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Identification of a region critical for proteolysis of the human growth hormone receptor.

Abstract：

:Release of soluble growth hormone binding protein (GHBP) corresponding to the extracellular domain of the GH receptor (GHR) occurs via distinct mechanisms depending on species. In human, proteolysis of full length GHR results in liberation of GHBP into the extracellular medium. A putative protease responsive for GHR cleavage has been identified, however, the residues involved are still unknown. In this study, using the mutational approach to the extracellular domain of the human GHR, we demonstrated that deletion of three residues located close to the transmembrane domain abolishes constitutive GHBP shedding without change in cellular GH binding. Deletion also significantly decreased the phorbol 12-myristate 13-acetate (PMA)-induced release of GHBP and the accumulation of membrane-anchored remnant proteins. Taken together, these results suggest that integrity of the juxtamembrane region of GHR is necessary for its biochemical cleavage and that a common mechanism is involved in constitutive and PMA-induced shedding.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Conte F,Salles JP,Raynal P,Fernandez L,Molinas C,Tauber M,Bieth E

doi

10.1006/bbrc.2001.6261

subject

Has Abstract

pub_date

2002-01-18 00:00:00

pages

851-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X01962618

journal_volume

290

pub_type

杂志文章

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