Identification of a hormonally regulated protein tyrosine phosphatase associated with bone and testicular differentiation.

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DOI: 10.1016/S0021-9258(18)43864-1

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摘要: Absence of the tyrosine kinase activity c-src and c-fms results in impairment bone remodeling. Such dysfunction underscores importance phosphorylation, yet role protein phosphatases metabolism remains unexamined. We have isolated cDNA for a novel receptor-like phosphatase expressed testis named osteotesticular (OST-PTP). The deduced 1711-residue possesses an extracellular domain with 10 fibronectin type III repeats cytoplasmic region two catalytic domains. In primary rat osteoblasts, 5.8-kilobase OST-PTP transcript is up-regulated differentiating cultures down-regulated late stage mineralizing cultures. addition, presumed alternate 4.8-5.0 kilobases, which may lack PTP domains, present proliferating but not detectable at other stages. Parathyroid hormone, modulator function, as well cyclic AMP analogues, increase mRNA 5-8-fold UMR 106 cells. situ hybridization adult revealed stage-specific expression OST-PTP. function signaling pathways during remodeling, serve broader cell interactions associated differentiation testis.

参考文章(51)
N. X. Krueger, M. Streuli, H. Saito, Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. The EMBO Journal. ,vol. 9, pp. 3241- 3252 ,(1990) , 10.1002/J.1460-2075.1990.TB07523.X
T Florio, M.G. Pan, B Newman, R.E. Hershberger, O Civelli, P.J. Stork, Dopaminergic inhibition of DNA synthesis in pituitary tumor cells is associated with phosphotyrosine phosphatase activity. Journal of Biological Chemistry. ,vol. 267, pp. 24169- 24172 ,(1992) , 10.1016/S0021-9258(18)35744-2
M. Kozak, Structural features in eukaryotic mRNAs that modulate the initiation of translation. Journal of Biological Chemistry. ,vol. 266, pp. 19867- 19870 ,(1991) , 10.1016/S0021-9258(18)54860-2
D.A. Pot, T.A. Woodford, E. Remboutsika, R.S. Haun, J.E. Dixon, Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase. Journal of Biological Chemistry. ,vol. 266, pp. 19688- 19696 ,(1991) , 10.1016/S0021-9258(18)55047-X
M Noda, K Yoon, G A Rodan, Cyclic AMP-mediated stabilization of osteocalcin mRNA in rat osteoblast-like cells treated with parathyroid hormone. Journal of Biological Chemistry. ,vol. 263, pp. 18574- 18577 ,(1988) , 10.1016/S0021-9258(19)81398-4
A.R. Kornblihtt, K. Umezawa, K. Vibe-Pedersen, F.E. Baralle, Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene. The EMBO Journal. ,vol. 4, pp. 1755- 1759 ,(1985) , 10.1002/J.1460-2075.1985.TB03847.X
J.B. Levy, P.D. Canoll, O. Silvennoinen, G. Barnea, B. Morse, A.M. Honegger, J.T. Huang, L.A. Cannizzaro, S.H. Park, T. Druck, The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system. Journal of Biological Chemistry. ,vol. 268, pp. 10573- 10581 ,(1993) , 10.1016/S0021-9258(18)82237-2
M.F. Gebbink, G.C. Zondag, R.W. Wubbolts, R.L. Beijersbergen, I. van Etten, W.H. Moolenaar, Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase Journal of Biological Chemistry. ,vol. 268, pp. 16101- 16104 ,(1993) , 10.1016/S0021-9258(19)85392-9