-
[show abstract]
[hide abstract]
ABSTRACT: As a further step toward characterizing the major nuclear glycoproteins from hamster liver and Kirkman-Robbins hepatoma (Lipińska A. and Gaczyński M. Int. J. Biochem. 4, 1385-1390, 1992) its intranuclear localization was studied. The glycoprotein patterns of examined nuclear fractions of hamster liver and hepatoma revealed some cell specificity observed especially in nuclear matrix preparations. Our results show the extensive presence of envelope glycoproteins in the nuclear matrix.
Comparative biochemistry and physiology. Biochemistry and molecular biology. 07/1994; 108(2):199-207.
-
[show abstract]
[hide abstract]
ABSTRACT: The search for cancer specific nuclear proteins, stimulated by the supposition that transition from the normal to the neoplastic state resulting from disturbances in the control mechanisms of gene expression, indicated that non-histone protein of MW 48 kD is much more abundant in animal tumour cells than in normal liver (Krajewska et al., 1990). A non-histone component of MW 48 kD was assessed for changes during chemically induced carcinogenesis. Rats were treated with the hepatocarcinogen thioacetamide (TAA) and the expression of the polypeptide studied, in total nuclear protein and nonhistone protein fractions, was tested by Western blot technique in the presence of antibodies developed against a component of MW 48 kD from Kirkman-Robbins hepatoma. It was demonstrated that TAA-induced hepatocarcinogenesis was accompanied by the expression of non-histone protein of MW 48 kD at a significantly elevated level. A clear and distinct change in the expression of the component studied in the spleen of TAA-treated rats was also observed. These results support the suggestion that over-expression of non-histone protein of MW 48 kD could contribute to neoplastic transformation.
Cytobios 02/1993; 75(301):103-12.
-
[show abstract]
[hide abstract]
ABSTRACT: 1. Glycoproteins recognized by Concanavalin A (ConA) have been identified in nuclei and nuclear fractions differing in sensitivity to micrococcal nuclease digestion from hamster liver and Kirkman-Robbins hepatoma. 2. The major ConA binding proteins from hamster liver and Kirkman-Robbins hepatoma nuclei have molecular weights about 27,000 and 57,000, and 38,000 and 49,000, respectively. 3. A distinct distribution of glycoproteins between fractions differing in sensitivity to nuclease digestion has not been observed.
International Journal of Biochemistry 10/1992; 24(9):1385-90.
-
[show abstract]
[hide abstract]
ABSTRACT: 1. As a further step toward characterizing nonhistone protein of mol. wt 48,000 which was found to be much more abundant in animal tumour cells than in normal ones [Krajewska W.M., Lipínska A., Marszatek M., Kiliańska Z., Wojtkowiak Z. and Kłyszejko-Stefanowicz L. Cell. Biochem. Funct. 8, 79-89 (1990)] its intranuclear localization in hamster liver and Kirkman-Robbins hepatoma was studied. The protein was identified by immunoblotting technique in the presence of antibodies against polypeptide of mol. wt about 48,000 from Kirkman-Robbins hepatoma. 2. Distribution of antigen with mol. wt of 48,000 in nuclear fractions representing different levels of nuclear material organization, i.e. in nucleoli, nuclease-sensitive and nuclease-resistant fractions, and extensive nuclease digestion products separated by size on Bio-Gel A-50m; implied the structural role of this component. 3. Fractionation of endogenously digested nuclei into low salt extract, high salt extract and nuclear matrix revealed that in normal liver the antigen studied is associated with nuclear matrix while in hepatoma this component appeared in high salt extract. 4. These results suggest that polypeptide with mol. wt of 48,000 is a shuttling protein which may be involved in reorganization of nuclear matrix during neoplastic transformation.
International Journal of Biochemistry 06/1992; 24(5):759-67.
-
[show abstract]
[hide abstract]
ABSTRACT: One- and two-dimensional gel electrophoretic analysis of nuclear proteins of Kirkman-Robbins hepatoma was used to study the effects of the tumour growth inhibitors methotrexate (MTX) and acyclonucleoside (DHPQtB) on protein composition. MTX and DHPQtB inhibited Kirkman-Robbins hepatoma growth by 89.2 +/- 3.5% and 16.3 +/- 6.1% respectively. The biosynthesis and/or metabolism of some polypeptide spots was affected by these antitumour agents, especially among components with molecular wt/isoelectric points of 52,000-64,000/4.9-5.5, 69,000-78,000/5.0-5.9 and 88,000-100,000/5.1-5.9.
Cytobios 02/1992; 70(281):91-100.
-
[show abstract]
[hide abstract]
ABSTRACT: 1. Analysis of immunoblots of one- and two-dimensional electropherograms of non-histone proteins from Kirkman-Robbins hepatoma, Morris hepatoma 7777, regenerating liver and normal liver demonstrated the presence of elevated level of nuclear antigen with mol. wt of 48,000 and pI of 5.4 in tumour cells. 2. Small amounts only were detected in proliferating and quiescent cells suggesting that different expression of this component may reflect biochemical events related to malignant transformation rather than to general cell activation.
International Journal of Biochemistry 02/1991; 23(2):195-201.
-
[show abstract]
[hide abstract]
ABSTRACT: Using two-dimensional (2-D) electrophoresis, two non-histone chromatin protein fractions (NHCP1 and NHCP2) from three animal tumours (Kirkman-Robbins hepatoma, Morris hepatoma 7777 and Ehrlich ascites cells) and normal hamster liver were analyzed. Apart from many common components several tissue specific polypeptides of the NHCP1 and NHCP2 fractions were detected. It was found that some spots present in electropherograms of non-histone proteins of tumour cells (M X 10(-3)/pI): 17-24/4.9-6.5 (NHCP1 and NHCP2); 34-41/4.9-6.0 (HCP1 and NHCP2); 44-46/5.3-7.5 (HCP2); 46-49/5.0-7.5 (NHCP1); 49/5.9-7.5 (NHCP2) and 102-134/5.6-7.0 (NHCP1) were absent from normal liver.
Acta biochimica Polonica 02/1990; 37(2):267-75. · 1.49 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Two groups of nonhistone chromatin proteins tightly bound to DNA were isolated from hamster liver and Kirkman-Robbins hepatoma with the use of hydroxyapatite columns: 1. NP proteins which can be briefly defined as nonhistone chromatin proteins, nondissociable from DNA in 5 M urea, and 2. a group of proteins nondissociable in 2 M KCl and thus believed to be nonelectrostatically bound to DNA. The proteins were characterized by their amino acid analysis, SDS-polyacrylamide gel electrophoresis and their influence on template activity of DNA. Some differences in electrophoretic patterns and template activity inhibition were found between the latter group of proteins from liver and hepatoma.
Neoplasma 02/1983; 30(3):309-16. · 1.44 Impact Factor
-
[show abstract]
[hide abstract]
ABSTRACT: Nuclear phosphoproteins from Syrian hamster liver and Kirkman-Robbins hepatoma were obtained by phenol method of TENG et al. and their chemical composition was investigated. Amino acid composition of phosphoproteins from both tissues resembled each other to a great extent. There was almost twice more phosphorus in the preparations from hepatoma than in the ones from liver. Using two electrophoretic techniques: SDS-polyacrylamide gel electrophoresis and isoelectric focusing some differences between the examined proteins of neoplastic and normal tissue were found. Three additional fractions (molecular weights 29 000, 89 000 and 93 000, respectively) could be observed in case of hepatoma proteins in comparison with the ones from liver. The phosphoproteins of Kirkman-Robbins hepatoma revealed three additional bands with isoelectric points 6.6, and 7.1.
Neoplasma 02/1980; 27(6):653-9. · 1.44 Impact Factor
-
International journal of radiation biology and related studies in physics, chemistry, and medicine 07/1978; 33(6):609-13. · 1.86 Impact Factor
