A cDNA coding for human sex hormone binding globulin Homology to vitamin K‐dependent protein S

@article{Gershagen1987ACC,
  title={A cDNA coding for human sex hormone binding globulin Homology to vitamin K‐dependent protein S},
  author={Sten Gershagen and Per Fernlund and {\AA}ke Lundwall},
  journal={FEBS Letters},
  year={1987},
  volume={220}
}
The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs.
TLDR
Southern blots of human placental DNA and cloned genomic DNA fragments indicate that sex hormone-binding globulin (SHBG) and its related testicular cDNAs are the products of a single gene.
Molecular analysis of the gene for vitamin K dependent protein S and its pseudogene. Cloning and partial gene organization.
TLDR
The structure of the two protein S genes and a comparison with the vitamin K dependent clotting factors support a model for their origin by exon shuffling and recruitment of the 3' part of the gene from an ancestor shared with the sex hormone binding globulin.
Expression of completely γ‐carboxylated and β‐hydroxylated recombinant human vitamin‐K‐dependent protein S with full biological activity
TLDR
Protein S is the most extensively post-translationally modified vitamin-K-dependent protein, and all the modifications were carried out in the recombinant DNA system yielding a recombinant protein S with full biological activity.
A Region of Vitamin K-dependent Protein S That Binds to C4b Binding Protein (C4BP) Identified Using Bacteriophage Peptide Display Libraries*
TLDR
The results suggest that residues 447–460 constitute a portion of protein S that is important for the interaction with C4BP, and may have implications for patients suffering from thrombosis, by directing the design of drugs that disrupt protein S binding to C4 BP.
Expression of sex hormone-binding globulin exon VII splicing variant messenger RNA in human uterine endometrial cancers.
TLDR
The results suggest that dedifferentiation of endometrial cancers might induce a reduction in their estrogen-dependent properties via intracellular SHBG.
Organization of the human protein S genes.
TLDR
Human genomic clones that span the entire protein S expressed gene (PS alpha) and the 3' two-thirds of the protein S pseudogene (PS beta) have been isolated and characterized, suggesting divergence of the two genes is a relatively recent event.
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References

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Rat androgen-binding protein: evidence for identical subunits and amino acid sequence homology with human sex hormone-binding globulin.
The cDNA for rat androgen-binding protein (ABP) was previously isolated from a bacteriophage lambda gt11 rat testis cDNA library and its identity was confirmed by epitope selection. Hybrid-arrested
Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation.
TLDR
A human liver cDNA library constructed in bacteriophage lambda gt11 was screened with DNA fragments from a full-length bovine cDNA clone encoding protein S, finding the COOH-terminal portion of human protein S does not show any resemblance to serine proteases.
Primary structure of bovine vitamin K-dependent protein S.
TLDR
The nucleotide sequence of a full-length cDNA clone, obtained from a bovine liver library, was determined and the amino acid sequence was deduced and it was shown that the protein has a leader sequence, 41 amino acid residues long.
Cloning and characterization of human liver cDNA encoding a protein S precursor.
TLDR
Human liver cDNA encoding a protein S precursor was isolated from two cDNA libraries by two different techniques and compared with homologous vitamin K-dependent plasma proteins shows that it is composed of the following domains.
Amino acid sequence of the sex steroid binding protein of human blood plasma.
TLDR
The amino acid sequence of the sex steroid binding protein (SBP) from human plasma has been determined and shows no homology either with the cDNA-derived sequences of the estrogen and glucocorticoid receptors found by others to be homologous with each other or with any other protein sequence in the 1986 data base.
Localization of thrombin cleavage sites in the amino-terminal region of bovine protein S.
TLDR
The sequence of the 100 amino-terminal amino acid residues and localized the thrombin cleavage sites are determined and protein S is found to be highly homologous to the corresponding parts in the other vitamin K-dependent clotting factors.
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