Research Article Open Access

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

Gunda Herberth1, Anke Stein1, Jens Glienke1, Stefan Taudien2, Irina Klaman3, Alexander Herr4, Karl-Heinz Thierauch2 and Anette Sommer2
  • 1 Institute of Molecular Biotechnology, Germany
  • 2 Research Laboratories of Schering AG, Germany
  • 3 Institute of Pathology, Germany
  • 4 Technical University Dresden, Germany


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


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.

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