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  • 1
    Publication Date: 1997-03-28
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J -- Yen, C -- Liaw, D -- Podsypanina, K -- Bose, S -- Wang, S I -- Puc, J -- Miliaresis, C -- Rodgers, L -- McCombie, R -- Bigner, S H -- Giovanella, B C -- Ittmann, M -- Tycko, B -- Hibshoosh, H -- Wigler, M H -- Parsons, R -- 5R35 CA39829/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1943-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians & Surgeons, Columbia University, 630 West 168 Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072974" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Brain Neoplasms/genetics ; Breast Neoplasms/genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 10 ; Female ; Frameshift Mutation ; *Genes, Tumor Suppressor ; Glioblastoma/genetics ; Humans ; Male ; Microfilament Proteins/chemistry ; Molecular Sequence Data ; *Mutation ; Neoplasm Transplantation ; Neoplasms/*genetics ; PTEN Phosphohydrolase ; *Phosphoric Monoester Hydrolases ; Phosphotyrosine/metabolism ; Prostatic Neoplasms/genetics ; Protein Tyrosine Phosphatases/chemistry/*genetics/physiology ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Sequence Deletion ; Sequence Homology, Amino Acid ; Transplantation, Heterologous ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 2449-2454 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 919-928 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Trypsin was immobilized on sand using five different methods. Attempts were made to attach amino-functional groups onto sand using 3-aminopropyltriethoxysilane, hexamethylenetetramine, hexamethylenediamine, and melamine. Glutaraldehyde was used as a bifunctional agent in all the methods. Methods for the estimation of the proteolytic 1activity and protein content of immobilized trypsin were standardized. The maximum retained activity was observed for trypsin immobilized on sand via 3-aminopropytriethoxysilane and glutaraldehyde. Immobilized trypsin showed a shift in the pH optimum toward the acidic side over that of soluble trypsin in all five cases. The optimum temperature for both native and immobilized trypsin prepared by the silane-glutaraldehyde method was found to be 45°C. However, the pH and thermal stabilities of immobilized trypsin were observed to be better than that of the native enzyme.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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