<i>PTEN</i> , a Putative Protein Tyrosine Phosphatase Gene Mutated in Human Brain, Breast, and Prostate Cancer

Jing Li(Columbia University), Clifford Yen(Cold Spring Harbor Laboratory), Danny Liaw(Columbia University), Katrina Podsypanina(Columbia University), Shikha Bose(Columbia University), Steven I. Wang(Columbia University), Janusz Puc(Columbia University), Christa Miliaresis(Columbia University), Linda Rodgers(Cold Spring Harbor Laboratory), W. Richard McCombie(Cold Spring Harbor Laboratory), Sandra H. Bigner(Duke University), Beppino C. Giovanella(Christus Stehlin Foundation for Cancer Research), Michael Ittmann(New York University), Ben Tycko(Columbia University), Hanina Hibshoosh(Columbia University), Michael Wigler(Cold Spring Harbor Laboratory), Ramon Parsons(Columbia University)
Science
March 28, 1997
Cited by 4,813

Abstract

Mapping of homozygous deletions on human chromosome 10q23 has led to the isolation of a candidate tumor suppressor gene, PTEN, that appears to be mutated at considerable frequency in human cancers. In preliminary screens, mutations of PTEN were detected in 31% (13/42) of glioblastoma cell lines and xenografts, 100% (4/4) of prostate cancer cell lines, 6% (4/65) of breast cancer cell lines and xenografts, and 17% (3/18) of primary glioblastomas. The predicted PTEN product has a protein tyrosine phosphatase domain and extensive homology to tensin, a protein that interacts with actin filaments at focal adhesions. These homologies suggest that PTEN may suppress tumor cell growth by antagonizing protein tyrosine kinases and may regulate tumor cell invasion and metastasis through interactions at focal adhesions.


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