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

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...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1997-03, Vol.275 (5308), p.1943-1947
Main Authors: Li, Jing, Yen, Clifford, Liaw, Danny, Podsypanina, Katrina, Bose, Shikha, Wang, Steven I., Puc, Janusz, Miliaresis, Christa, Rodgers, Linda, McCombie, Richard, Bigner, Sandra H., Giovanella, Beppino C., Ittmann, Michael, Tycko, Ben, Hibshoosh, Hanina, Wigler, Michael H., Parsons, Ramon
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Brain
Brain Neoplasms - genetics
Breast Neoplasms - genetics
Cancer
Cell lines
Chromosome Mapping
Chromosomes, Human, Pair 10
DNA
Exons
Female
Frameshift Mutation
Genes
Genes, Tumor Suppressor
Genetic mutation
Glioblastoma
Glioblastoma - genetics
Heterologous transplantation
Humans
Male
Medical sciences
Microfilament Proteins - chemistry
Molecular Sequence Data
Mutation
Neoplasm Transplantation
Neoplasms - genetics
Neurology
Phosphatases
Phosphoric Monoester Hydrolases
Phosphotyrosine - metabolism
Prostate cancer
Prostatic Neoplasms - genetics
Protein Tyrosine Phosphatases - chemistry
Protein Tyrosine Phosphatases - genetics
Protein Tyrosine Phosphatases - physiology
Protein-Tyrosine Kinases - antagonists & inhibitors
Proteins
PTEN Phosphohydrolase
Sequence Deletion
Sequence Homology, Amino Acid
Tensins
Transplantation, Heterologous
Tumor cell line
Tumor Cells, Cultured
Tumor Suppressor Proteins
Tumors
Tumors of the nervous system. Phacomatoses
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Description
Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.275.5308.1943