Human Latrophilin-2 is Expressed in the Cytotrophoblast and Syncytiotrophoblast of Placenta and in Endothelial Cells
- 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.
DOI: https://doi.org/10.3844/ajbbsp.2005.135.144
Copyright: © 2005 Gunda Herberth, Anke Stein, Jens Glienke, Stefan Taudien, Irina Klaman, Alexander Herr, Karl-Heinz Thierauch and Anette Sommer. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Keywords
- Adhesion-GPCR
- latrophilin-2
- placenta
- endothelial cell
- glycosylation