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  • 1
    Electronic Resource
    Electronic Resource
    Dysfunction of protein kinase FA/GSK-3α in lymphocytes of patients with schizophrenic disorder (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 108-116 
    Details
    ISSN: 0730-2312
    Keywords: schizophrenic disorder ; lymphocytes ; kinase FA/GSK-3α ; impaired protein phosphatase activation ; immunoblotting ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: As compared to normal people, the lymphocytes of patients with schizophrenia were found to have an impairment of ATP. Mg-dependent protein phosphatase activation. More importantly, the impaired protein phosphatase activation in the lymphocytes of schizophrenic patients could be consistently and completely restored to normal by exogenous pure protein kinase FA/glycogen synthase kinase-3α (kinase FA/GSK-3α) (the activating factor of ATP.Mg-dependent protein phosphatase), indicating that the molecular mechanism for the impaired protein phosphatase activation in schizophrenic patients may be due to a functional loss of kinase FA/GSK-3α immunoblotting and kinase activity analysis in an anti-kinase FA/GSK-3α immunoprecipitate further demonstrate that both cellular activities and protein levels of kinase FA/GSK-3α in the lymphocytes of schizophrenic patients were greatly impared as compared to normal controls. Statistical analysis revealed that the lymphocytes isolated from 37 normal people contain kinase FA/GSK-3α activity in the high levels of 14.8 ± 2.4 units/mg of cell protein, whereas the lymphocytes of 48 patients with schizophrenic disorder contain kinase FA/GSK-3α activity in the low levels of 2.8 ± 1.6 units/mg, indicating that the different levels of kinase FA/GSK-3α activity between schizophrenic patients and normal people are statistically significant. Taken together, the results provide intial evidence that patients with schizophrenic disorder may have a common impairment in the protein levels and cellular activities of kinase FA/GSK-3α, a multisubstrate protein kinase and a multisubstrate protein phosphatase activator in their lymphocytes. © 1995 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590112
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Overexpression of protein kinase FA/GSK-3α (a proline-directed protein kinase) correlates with human hepatoma dedifferentiation/progression (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 61 (1996), S. 238-245 
    Details
    ISSN: 0730-2312
    Keywords: human hepatoma ; dedifferentiation/progression ; PDPK ; overexpression ; kinase FA/GSK-3α ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Computer analysis of protein phosphorylation sites sequence revealed that transcriptional factors and viral oncoproteins are prime targets for regulation of proline-directed protein phosphorylation, suggesting an association of the proline-directed protein kinase (PDPK) family with neoplastic transformation and tumorigenesis. In this report, an immunoprecipitate activity assay of protein kinase FA/glycogen synthase kinase-3α (kinase FA/GSK-3α) (a member of PDPK family) has been optimized for human hepatoma and used to demonstrate for the first time significantly increased (P 〈 0.01) activity in poorly differentiated SK-Hep-1 hepatoma (24.2 ± 2.8 units/mg) and moderately differentiated Mahlavu hepatoma (14.5 ± 2.2 units/mg) when compared to well differentiated Hep 3B hepatoma (8.0 ± 2.4 units/mg). Immunoblotting analysis revealed that increased activity of kinase FA/GSK-3α is due to overexpression of the protein. Elevated kinase FA/GSK-3α expression in human hepatoma biopsies relative to normal liver tissue was found to be even more profound. This kinase appeared to be ∼fivefold overexpressed in well differentiated hepatoma and ∼13-fold overexpressed in poorly differentiated hepatoma when compared to normal liver tissue. Taken together, the results provide initial evidence that overexpression of kinase FA/GSK-3α is involved in human hepatoma dedifferentiation/progression. Since kinase FA/GSK-3α is a PDPK, the results further support a potential role of this kinase in human liver tumorigenesis, especially in its dedifferentiation/progression. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Overexpression of cellular activity and protein level of protein kinase FA/GSK-3α correlates with human thyroid tumor cell dedifferentiation (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 58 (1995), S. 474-480 
    Details
    ISSN: 0730-2312
    Keywords: kinase FA/GSK-3α ; overexpression ; thyroid ; tumor cell dedifferentiation ; carcinogenesis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Computer analysis of protein phosphorylation sites sequence revealed that transcriptional factors and viral oncoproteins are prime targets for regulation of proline-directed protein phosphorylation, suggesting an association of the proline-directed protein kinase (PDPK) family with neoplastic transformation and tumorigenesis. In this report, an immunoprecipitate activity assay of protein kinase FA/glycogen synthase kinase-3α (kinase FA/GSK-3α) (a member of the PDPK family) has been optimized for human thyroid tissue and used to demonstrate for the first time significantly increased (P 〈 0.001) activity in thyroid carcinoma (24.2 ± 2.8 units/mg of protein) (n = 7), thyroid adenoma (14.5 ± 2.2 units/mg of protein) (n = 6), and thyroid hyperplasia (8.0 ± 2.4 units/mg of protein) (n = 5) when compared to five normal controls (4.1 ± 1.8 units/mg of protein). Immunoblotting analysis further revealed that increased activity of kinase FA/GSK-3α in thyroid tumor cells is due to overexpression of protein level and cellular activity of kinase FA/GSK-3α is involved in human thyroid tumor cell dedifferentiation, supporting an association of PDPK with neoplastic transformation and tumorigenesis. Since kinase FA/GSK-3α may function as a possible regulator of transcription factors/protooncogenes, kinase FA/GSK-3α may therefore play an important role in thyroid cell carcinogenesis, especially in its differentiation.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240580410
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Association of protein kinase FA/GSK-3α (a proline-directed kinase and a regulator of protooncogenes) with human cervical carcinoma dedifferentiation/progression (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 59 (1995), S. 143-150 
    Details
    ISSN: 0730-2312
    Keywords: cervical carcinoma progression ; kinase FA/GSK-3α ; overexpression ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Computer analysis of protein phosphorylation-sites sequence revealed that most transcriptional factors and viral oncoproteins are prime targets for regulation of proline-directed protein phosphorylation, suggesting an association of proline-directed protein kinase (PDPK) family with neoplastic transformation and tumorigenesis. In this report, an immunoprecipitate activity assay of protein kinase FA/glycogen synthase kinase-3α (kinase FA/GSK-3α) (a particular member of PDPK family) has been optimized for human cervical tissue and used to demonstrate for the first time significantly increased (P 〈 0.001) activity in poorly differentiated cervical carcinoma (82.8 ± 6.6 U/mg of protein), moderately differentiated carcinoma (36.2 ± 3.4 U/mg of protein), and well-differentiated carcinoma (18.3 ± 2.4 U/mg of protein) from 36 human cervical carcinoma samples when compared to 12 normal controls (4.9 ± 0.6 U/mg of protein). Immunoblotting analysis further revealed that increased activity of kinase FA/GSK-3α in cervical carcinoma is due to overexpression of protein synthesis of the kinase. Taken together, the results provide initial evidence that overexpression of protein synthesis of the kinase. Taken together, the results provide initial evidence that overexpression of protein synthesis and cellular activity of kinase FA/GSK-3α may be involved in human cervical carcinoma dedifferentiation/progression, supporting an association of proline-directed protein kinase with neoplastic transformation and tumorigenesis. Since protein kinase FA/GSK-3α may function as a possible regulator of transcription factors/proto-oncogenes, the results further suggest that kinase FA/GSK-3α may play a potential role in human cervical carcinogenesis, especially in its dedifferentiation and progression. © 1995 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240590203
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    Paper (German National Licenses)
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