Characterization of a cDNA coding for sex steroid‐binding protein of human plasma

  title={Characterization of a cDNA coding for sex steroid‐binding protein of human plasma},
  author={B G Que and Philip H. P{\'e}tra},
  journal={FEBS Letters},
The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs.
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.
Human sex hormone-binding globulin gene expression- multiple promoters and complex alternative splicing
It is reported that transcriptional expression of the human SHBG gene is far more complex than previously described, and new and important questions are raised regarding the role of novel alternatively spliced transcripts, their function in hormonally responsive tissues including the breast and prostate, and the role that aberrant SH BG gene expression may play in cancer.
Homologous sequences in steroidogenic enzymes, steroid receptors and a steroid binding protein suggest a consensus steroid-binding sequence.
A more general consensus sequence of LPLLL +/- 000KDRE0LKRL +/- PV, where +/- refers to any charged amino acid, and 0 refers to an uncharged amino acid is proposed, which strongly suggests this sequence is necessary, if not sufficient, for a steroid binding site in many proteins.
Human testosterone-binding globulin is a dimer composed of two identical protomers that are differentially glycosylated.
Affinity-purified human testosterone-binding globulin (hTeBG) is composed of two subunits, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, electrophoretic transfer, and immunochemical localization with a monoclonal antibody raised against rat androgen-binding protein.


Characterization of a cDNA coding for human factor XII (Hageman factor).
The amino acid and DNA sequences in human factor XII showed considerable homology with the corresponding domains in other serine proteases, including prothrombin, plAsminogen, tissue plasminogen activator, and urokinase.
Isolation and analysis of a cDNA coding for human C1 inhibitor.
  • B. G. Que, P. Pétra
  • Biology, Chemistry
    Biochemical and biophysical research communications
  • 1986
Cloning and characterization of human liver cDNA encoding a protein S precursor.
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.
The cDNA for the β-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3′-untranslated region
Analysis of the βHCG cDNA nucleotide sequence suggests that this extension may have arisen by the loss of the termination codon of an ancestral β-like gene so that most of what was previously the 3′-untranslated region now codes for protein.
Amino acid sequence of the sex steroid binding protein of human blood plasma.
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.
Characterization of protein S, a gamma-carboxyglutamic acid containing protein from bovine and human plasma.
Results indicate that Protein S from bovine or human plasma shows many similarities to the other vitamin K dependent proteins present in plasma.
Immunocytochemical localization of the sex steroid-binding protein of plasma in tissues of the adult monkey Macaca nemestrina.
  • S. Bordin, P. Pétra
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1980
The sex steroid-binding protein (SBP) present in the serum of the monkey Macaca nemestrina is shown to exist in cells of tissue involved in reproduction. The localization was demonstrated by