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Molecular cloning of the rat Tpx-1 responsible for the interaction between spermatogenic and Sertoli cells.

Authors: Maeda, T  Sakashita, M  Ohba, Y  Nakanishi, Y 
Citation: Maeda T, etal., Biochem Biophys Res Commun 1998 Jul 9;248(1):140-6.
Pubmed: (View Article at PubMed) PMID:9675100
DOI: Full-text: DOI:10.1006/bbrc.1998.8918

We previously showed in a primary culture of rat testicular cells that spermatogenic cells specifically bind to somatic Sertoli cells and that this interaction is needed for spermatogenic cells to differentiate in vitro. Adopting an expression cloning procedure, we here isolated a cDNA coding for a spermatogenic cell protein whose expression gave a cultured cell line the ability to bind to Sertoli cells. The protein, 243 amino acids with a putative N-terminal signal peptide and a C-terminal Cys-rich region, turned out to be the rat homologue of a testicular protein called Tpx-1 whose function had yet to be determined. A polyclonal antibody raised against bacterially expressed Tpx-1 significantly inhibited the binding of spermatogenic cells to Sertoli cells. The above results indicated that Tpx-1 is a testicular cell adhesion molecule responsible for the specific interaction between spermatogenic and Sertoli cells.


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CRRD Object Information
CRRD ID: 634409
Created: 2003-08-29
Species: All species
Last Modified: 2003-08-29
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.