Abstract: Having determined the complete amino acid sequence of a cytosolic phosphatase purified from bovine liver, we studied the role of this enzyme (referred to as 'PTPase') in the control of cell proliferation. We used NIH/3T3 fibroblasts, both normal and transformed by the oncogenes v-erbB, v-src, and v-raf: a synthetic gene coding for PTPase was transfected into, and overexpressed in, normal and transformed NIH/3T3 cells with resulting inhibition of cell growth. Inhibition of proliferation correlated with the level of foreign PTPase; growth in soft agar was also inhibited in transformants overexpressing the enzyme. However, PTPase overexpression did not inhibit the rapid turnover of inositol lipids stimulated by platelet-derived growth factor. We conclude that this novel PTPase is active on cell type-specific signalling substrates that control normal and transformed fibroblast proliferation.
Negative growth control by a novel low M(r) phosphotyrosine protein phosphatase in normal and transformed cells / M. Ruggiero; C. Pazzagli; S. Rigacci; L. Magnelli; G. Raugei; A. Berti; VP. Chiarugi; JH.Pierce; G. Camici; G. Ramponi. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 326:(1993), pp. 294-298. [10.1016/0014-5793(93)81811-D]
Negative growth control by a novel low M(r) phosphotyrosine protein phosphatase in normal and transformed cells
RUGGIERO, MARCO;RIGACCI, STEFANIA;MAGNELLI, LUCIA;RAUGEI, GIOVANNI;BERTI, ANDREA;CHIARUGI, VINCENZO;CAMICI, GUIDO;RAMPONI, GIAMPIETRO
1993
Abstract
Abstract: Having determined the complete amino acid sequence of a cytosolic phosphatase purified from bovine liver, we studied the role of this enzyme (referred to as 'PTPase') in the control of cell proliferation. We used NIH/3T3 fibroblasts, both normal and transformed by the oncogenes v-erbB, v-src, and v-raf: a synthetic gene coding for PTPase was transfected into, and overexpressed in, normal and transformed NIH/3T3 cells with resulting inhibition of cell growth. Inhibition of proliferation correlated with the level of foreign PTPase; growth in soft agar was also inhibited in transformants overexpressing the enzyme. However, PTPase overexpression did not inhibit the rapid turnover of inositol lipids stimulated by platelet-derived growth factor. We conclude that this novel PTPase is active on cell type-specific signalling substrates that control normal and transformed fibroblast proliferation.File | Dimensione | Formato | |
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