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Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis.

Publication ,  Journal Article
Li, JC; Samy, ET; Grima, J; Chung, SS; Mruk, D; Lee, WM; Silvestrini, B; Cheng, CY
Published in: Journal of Cellular Physiology
December 2000

The full-length cDNA encoding the entire open reading frame (ORF) of rat myotubularin (rMTM) was isolated from a rat testis expression library by PCR. Among the three approximately 2.9-kb cDNAs that were sequenced, one clone was different from the other two clones. It contained seven extra amino acids of FVVLNLQ; this short stretch of extra sequence was found between Gln(421) and Phe(422) within the SET (Suvar3-9, Enhancer-of-zeste, Trithorax) interacting domain (SID) of rMTM. The rMTM ORF had 1,713 bp encoding for a 571 amino acid polypeptide and a calculated molecular weight of 65.8 kDa. A comparison between its deduced amino acid sequence and the GenBank database using BLAST revealed a 53.1% identity with human myotubularin protein (hMTM1), which is a member of the protein tyrosine phosphatase (PTP) family associated with X-linked myotubular myopathy. A 22 amino acid peptide NH(2)-TKVNERYELCDTYPALLAVPAN was synthesized based on the deduced amino acid sequence of rMTM and used for antibody production. By using immunoblot analysis, a 66-kDa protein was indeed detected in both Sertoli and germ-cell cytosols. rMTM mRNA was found in various tissues but was predominantly expressed in the testis, ovary, and skeletal muscle. Sertoli cell rMTM expression was stimulated by germ cells and enhanced when inter-Sertoli junctions were being assembled in vitro. A drastic reduction in testicular rMTM steady-state mRNA level correlated with the depletion of germ cells from the testis in vivo following either glycerol or lonidamine treatment. These results indicate that rMTM is a rat homologue of hMTM1 that may be a useful marker in monitoring the events of cell-cell interactions in the testis.

Duke Scholars

Published In

Journal of Cellular Physiology

ISSN

0021-9541

Publication Date

December 2000

Volume

185

Issue

3

Start / End Page

366 / 385

Location

united states

Related Subject Headings

  • Biochemistry & Molecular Biology
  • 1116 Medical Physiology
  • 0601 Biochemistry and Cell Biology
 

Citation

APA
Chicago
ICMJE
MLA
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Li, J. C., Samy, E. T., Grima, J., Chung, S. S., Mruk, D., Lee, W. M., … Cheng, C. Y. (2000). Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis. Journal of Cellular Physiology, 185(3), 366–385.
Li, J. C., E. T. Samy, J. Grima, S. S. Chung, D. Mruk, W. M. Lee, B. Silvestrini, and C. Y. Cheng. “Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis.Journal of Cellular Physiology 185, no. 3 (December 2000): 366–85.
Li JC, Samy ET, Grima J, Chung SS, Mruk D, Lee WM, et al. Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis. Journal of Cellular Physiology. 2000 Dec;185(3):366–85.
Li JC, Samy ET, Grima J, Chung SS, Mruk D, Lee WM, Silvestrini B, Cheng CY. Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis. Journal of Cellular Physiology. 2000 Dec;185(3):366–385.
Journal cover image

Published In

Journal of Cellular Physiology

ISSN

0021-9541

Publication Date

December 2000

Volume

185

Issue

3

Start / End Page

366 / 385

Location

united states

Related Subject Headings

  • Biochemistry & Molecular Biology
  • 1116 Medical Physiology
  • 0601 Biochemistry and Cell Biology