Rat Protein Tyrosine Phosphatase eta  Suppresses the Neoplastic Phenotype of Retrovirally Transformed Thyroid Cells through the Stabilization of p27Kip1

doi:10.1128/MCB.20.24.9236-9246.2000

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Molecular and Cellular Biology, December 2000, p. 9236-9246, Vol. 20, No. 24
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Rat Protein Tyrosine Phosphatase $eta$ Suppresses the Neoplastic Phenotype of Retrovirally Transformed Thyroid Cells through the Stabilization of p27^Kip1

Francesco Trapasso,¹ Rodolfo Iuliano,¹ Angelo Boccia,² Antonella Stella,¹ Roberta Visconti,³ Paola Bruni,² Gustavo Baldassarre,² Massimo Santoro,³ Giuseppe Viglietto,² and Alfredo Fusco^*^,¹

Dipartimento di Medicina Sperimentale e Clinica, Facoltà di Medicina e Chirurgia di Catanzaro, Università degli Studi di Catanzaro "Magna Graecia," 88100 Catanzaro,¹ and Istituto dei Tumori di Napoli² and Centro di Endocrinologia ed Oncologia Sperimentale del CNR, Dipartimento di Biologia e Patologia Cellulare e Molecolare, Facoltà di Medicina e Chirurgia, Università di Napoli "Federico II,"³ 80131 Naples, Italy

Received 15 March 2000/Returned for modification 13 June 2000/Accepted 27 September 2000

The r-PTP $eta$ gene encodes a rat receptor-type protein tyrosine phosphatase whose expression is negatively regulated by neoplasticcell transformation. Here we first demonstrate a dramatic reductionin DEP-1/HPTP $eta$ (the human homolog of r-PTP $eta$ ) expression in a panelof human thyroid carcinomas. Subsequently, we show that the reexpressionof the r-PTP $eta$ gene in highly malignant rat thyroid cells transformedby retroviruses carrying the v-mos and v-ras-Ki oncogenes suppressestheir malignant phenotype. Cell cycle analysis demonstrated thatr-PTP $eta$ caused G₁ growth arrest and increased the cyclin-dependentkinase inhibitor p27^Kip1 protein level by reducing the proteasome-dependent degradationrate. We propose that the r-PTP $eta$ tumor suppressor activity ismediated by p27^Kip1 protein stabilization, because suppression of p27^Kip1 protein synthesis using p27-specific antisense oligonucleotidesblocked the growth-inhibitory effect induced by r-PTP $eta$ . Furthermore,we provide evidence that in v-mos- or v-ras-Ki-transformed thyroidcells, the p27^Kip1 protein level was regulated by the mitogen-activated protein(MAP) kinase pathway and that r-PTP $eta$ regulated p27^Kip1 stability by preventing v-mos- or v-ras-Ki-induced MAP kinaseactivation.

^* Corresponding author. Mailing address: Dipartimento di Biologia e Patologia Cellulare e Molecolare, Facoltà di Medicina eChirurgia, Università di Napoli "Federico II," via Pansini 5,80131 Naples, Italy. Phone: 39 081 7463056. Fax: 39 081 7463037.E-mail: afusco{at}napoli.com.

Molecular and Cellular Biology, December 2000, p. 9236-9246, Vol. 20, No. 24
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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Rat Protein Tyrosine Phosphatase Suppresses the Neoplastic Phenotype of Retrovirally Transformed Thyroid Cells through the Stabilization of p27Kip1

Rat Protein Tyrosine Phosphatase $eta$ Suppresses the Neoplastic Phenotype of Retrovirally Transformed Thyroid Cells through the Stabilization of p27^Kip1