Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum

  title={Characterization of high affinity progesterone-binding membrane proteins by an anti-peptide antiserum},
  author={Christiane Meyer and Roland M. Schmid and Kerstin Schmieding and Elisabeth Falkenstein and Martin Wehling},
Chemical modification and structural analysis of the progesterone membrane binding protein from porcine liver membranes
Evidence for an involvement of carboxyl-, tryptophan- and methionine residues in [3H]progesterone binding to porcine liver microsomes is given and it is shown that mPR can form disulfide-linked homodimers.
Identification of a 71 kDa protein as a putative non-genomic membrane progesterone receptor in boar spermatozoa.
Ligand blot assays performed in the presence of free progesterone, RU486 or estrogen revealed that binding of peroxidase-conjugated progester one to the 71 kDa protein was inhibited by free progestersone and RU486 in a dose-dependent manner but not by estrogen, which further confirms that progesterOne binds to the71 kDaprotein specifically.
Novel, Membrane-Intrinsic Receptors for Progesterone and Aldosterone
In 1972, binding of [3H] aldosterone to plasma membranes from rat kidney with Kd ~ 100 nM was reported [1]. In a similar system, solubilization of binding activity was performed, but no further
Cloning and tissue expression of two putative steroid membrane receptors.
The two proteins, Hpr6.6 and Dg6, are the first putative steroid membrane receptors cloned from man and contain a putative transmembrane domain and a highly conserved stretch of 58 amino acids.


Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes.
The purified fraction as identified by maximum specific progesterone-binding activity contained two major polypeptides of apparent molecular masses that showed an identical amino terminus without significant identity in the amino acid sequence to any known protein primary structure.
A specific membrane binding protein for progesterone in rat brain: sex differences and induction by estrogen.
  • S. Tischkau, V. D. Ramirez
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1993
Results show a reversible sex difference in the specific binding of progesterone to synaptosomal membrane sites in the central nervous system of male and female rats which is dependent on estrogen.
High-affinity binding of progesterone to the plasma membrane of Xenopus oocytes: characteristics of binding and hormonal and developmental control.
Progesterone binding activity was observed in membrane preparations from whole ovaries and defolliculated oocytes but not in those from somatic cells, indicating that progesterone binding is restricted to the oocyte membrane.
Binding of progesterone to specific sites in isolated hepatic cells and purified plasma membrane fraction.
It is observed that specific progesterone binding to hepatocytes and plasma membrane is independent from the alpha and beta adrenergic receptors and from P-site adenosine receptor.
Characterization and solubilization of novel aldosterone-binding proteins in porcine liver microsomes.
Using the radioligand [1,2,6,7-3H]aldosterone ([3H], specific binding sites for aldosterone were identified and characterized in microsomal preparations from porcine liver, and have unique pharmacological properties, which are similar to those found for a Aldosterone membrane binding in human lymphocytes and pig kidney.
Partial purification and characterization of oestrogen receptors in subfractions of hepatocyte plasma membranes.
A moderate degree of positive co-operativity in the interaction of hormone with plasma membranes was shown, and oestradiol-binding sites and activities of plasma-membrane marker enzymes were distributed predominantly into cytosol.
Characterization of specific binding sites for corticosterone in mouse liver plasma membrane.
The specific binding of [3H]corticosterone to mouse liver purified plasma membrane fractions is a saturable, reversible, and temperature-dependent process and the high-affinity binding site is different from nuclear glucocorticoid, nuclear progesterone, and Na+, K(+)-ATPase digitalis receptors.
Binding of Progesterone to Nerve Cell Membranes of Rat Brain Using Progesterone Conjugated to 125I‐Bovine Serum Albumin as a Ligand
The present data indicate that progester one‐125I‐bovine serum albumin conjugate can be used as a ligand to study progesterone‐membrane receptor interactions.
Full-length cDNA sequence of a progesterone membrane-binding protein from porcine vascular smooth muscle cells.
A full-length cDNA clone for a progesterone membrane binding protein from porcine vascular smooth muscle cells was isolated and the complete nucleotide sequence determined. The cDNA encodes a protein