Elisabeth Falkenstein

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According to the traditional model, steroid hormones bind to intracellular receptors and subsequently modulate transcription and protein synthesis, thus triggering genomic events finally responsible for delayed effects. Based upon similarities in molecular structure, specific receptors for steroids, vitamin D(3) derivatives, thyroid hormone, retinoids, and(More)
Steroids may exert their action in living cells by several ways: 1). the well-known genomic pathway, involving hormone binding to cytosolic (classic) receptors and subsequent modulation of gene expression followed by protein synthesis. 2). Alternatively, pathways are operating that do not act on the genome, therefore indicating nongenomic action. Although(More)
We have cloned two human putative steroid binding membrane proteins, termed Hpr6.6 and Dg6. Hpr6.6 is the human homolog of a previously cloned porcine progesterone binding protein. Both proteins contain a putative transmembrane domain and a highly conserved stretch of 58 amino acids. Hpr6.6 mRNA is expressed predominantly in liver and kidney, whereas Dg6(More)
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 of 194 amino acids with a transmembrane segment. This protein is likely to represent the first steroid membrane receptor or a part of it for which sequence(More)
A coiling-inducing factor was isolated from tendrils of Bryonia dioica Jacq. and identified by infrared, 1H-, 13C-nuclear magnetic resonance and mass spectrometry as α-linolenic acid. When applied to detached tendrils, exogenous α-linolenic acid, but not linoleic acid or oleic acid, induced tendril coiling. Further investigations showed that metabolites of(More)
In addition to the classical genomic steroid actions on modulation of transcription and protein synthesis, rapid, nongenomic effects have been described for various steroids. These effects on cellular signaling and function are supposed to be transmitted by membrane binding sites unrelated to the classical intracellular receptors. Recently, a high affinity(More)
Progesterone is one of the physiological inducers of the acrosome reaction in mammalian spermatozoa. The receptor that responds to progesterone is not yet identified, and its properties differ in many aspects from the properties of the classic nuclear progesterone receptor, suggesting the participation of a novel or non-classic receptor. In this study, we(More)
Rapid, nongenomic effects of steroids are likely to be mediated by membrane receptors not by intracellular steroid receptors. We recently identified a progesterone membrane binding protein (mPR) from human liver. The corresponding hmpr gene is comprised of 3 exons and 2 introns. The promoter sequence of hmpr lacks a typical TATA box but contains instead a(More)
There is increasing evidence for rapid effects of steroids that are incompatible with the classical model of genomic steroid action. To address the diversity of mechanisms for rapid steroid signaling described over the past years, a classification of rapid steroid effects has been proposed to promote the discussion and understanding of nongenomic steroid(More)
A chemically synthesized 15-mer oligopeptide derived from the N terminus of high affinity progesterone-binding membrane site(s) from porcine liver was used to generate site-specific antibodies. Western blotting experiments confirmed the specificity of the anti-peptide serum obtained. In further investigations this antiserum was used for the identification(More)