Research Article Open Access

Human Latrophilin-2 is Expressed in the Cytotrophoblast and Syncytiotrophoblast of Placenta and in Endothelial Cells

Gunda Herberth1, Anke Stein2, Jens Glienke3, Stefan Taudien4, Irina Klaman5, Alexander Herr6, Karl-Heinz Thierauch3 and Anette Sommer3
  • 1 UFZ-Centre for Environmental Research Leipzig-Halle Ltd., Department of Environmental Immunology, P.O. Box 500135, D-04301 Leipzig, Germany
  • 2 metaGen Pharmaceuticals GmbH, Oudenarder Str. 16, D-13347 Berlin, Germany
  • 3 Research Laboratories of Schering AG, Müllerstr. 178, D-13342 Berlin, Germany
  • 4 Institute of Molecular Biotechnology, Genome Analysis, Beutenbergstr. 11, D-07745 Jena, Germany
  • 5 Institute of Pathology, Charité Campus Benjamin-Franklin, Hindenburgdamm 30, D-12200 Berlin, Germany
  • 6 Institute of Clinical Genetics, Medical Faculty "Carl Gustav Carus", Technical University Dresden, Fetscherstr. 74, D-01307 Dresden, Germany

Abstract

Latrophilin-2 is a member of the family of adhesion-GPCRs that is characterised by a long N-terminus which contains motifs identified in proteins involved in cell adhesion. We were interested in determining the expression pattern of human latrophilin-2 and to perform a biochemical characterisation of this protein. The expression pattern of latrophilin-2 was analysed in human organs, tissues and cell lines. RT-PCR analyses detect a very strong signal for latrophilin-2 in human placenta and in situ hybridisation further showed that latrophilin-2 is predominantly expressed in the cytotrophoblast and syncytiotrophoblast. Moreover, latrophilin-2 expression is visible in adherent cells with a remarkably strong signal in microvascular endothelial cells (MVEC) and in human umbilical vein endothelial cells (HUVEC). Deglycosylation experiments using glycosidase F demonstrated that the N-terminal fragment of human latrophilin-2 is highly glycosylated. Using specific antibodies and latrophilin-2 stable cell lines we could show that human latrophilin-2 is cleaved into a 135 kDa N-terminal and a 70 kDa C-terminal fragment. It was also possible to detect the N-terminal fragment of latrophilin-2 in cell culture supernatant of HUVEC indicating that endogenous latrophilin-2 is expressed on the protein level in human vascular endothelial cells and that post-translational modification and generation of a 135 kDa N-terminal fragment takes place. The role of this fragment in the activation of the transmembrane domain of latrophilin-2 or in other cellular processes remains to be elucidated.

American Journal of Biochemistry and Biotechnology
Volume 1 No. 3, 2005, 135-144

DOI: https://doi.org/10.3844/ajbbsp.2005.135.144

Submitted On: 28 September 2005 Published On: 30 September 2005

How to Cite: Herberth, G., Stein, A., Glienke, J., Taudien, S., Klaman, I., Herr, A., Thierauch, K. & Sommer, A. (2005). Human Latrophilin-2 is Expressed in the Cytotrophoblast and Syncytiotrophoblast of Placenta and in Endothelial Cells. American Journal of Biochemistry and Biotechnology, 1(3), 135-144. https://doi.org/10.3844/ajbbsp.2005.135.144

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Keywords

  • Adhesion-GPCR
  • latrophilin-2
  • placenta
  • endothelial cell
  • glycosylation