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A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S.
Affinity purified antibodies to human sex hormone binding globulin (SHBG) were used in screening a human liver cDNA library, constructed in the expression vector lambda gt11. One clone, identified as producing recombinant SHBG, carried a cDNA insert of 1.1 kb. The nucleotide sequence of the insert had an open reading frame coding for 356 amino acid residues. The coding sequence was followed by a short 3'-region of 19 non-translated nucleotides and a poly(A) tail. Confirmation that the cDNA clone represented human SHBG was obtained by the finding of a complete agreement in amino acid sequence with several peptide fragments generated from purified SHBG by proteolytic cleavage. The primary structure of SHBG shows a considerable homology to that of protein S, a vitamin K-dependent protein with functions in the coagulation system.
PMID: 2956126 [PubMed - indexed for MEDLINE]
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Cited by 7 PubMed Central articles
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Implication of protein S thrombin-sensitive region with membrane binding via conformational changes in the gamma-carboxyglutamic acid-rich domain.
Borgel D, Gaussem P, Garbay C, Bachelot-Loza C, Kaabache T, Liu WQ, Brohard-Bohn B, Le Bonniec B, Aiach M, Gandrille S.
Biochem J. 2001 Dec 1; 360(Pt 2):499-506.
[Biochem J. 2001]
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Characterization of mini-protein S, a recombinant variant of protein S that lacks the sex hormone binding globulin-like domain.
Van Wijnen M, Stam JG, Chang GT, Meijers JC, Reitsma PH, Bertina RM, Bouma BN.
Biochem J. 1998 Feb 15; 330 ( Pt 1):389-96.
[Biochem J. 1998]
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The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade.
Manfioletti G, Brancolini C, Avanzi G, Schneider C.
Mol Cell Biol. 1993 Aug; 13(8):4976-85.
[Mol Cell Biol. 1993]
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