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  • Articles  (3)
  • Life and Medical Sciences  (3)
  • 1985-1989  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Membrane association of collagenase stimulatory factor(s) from B-16 melanoma cells (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 35 (1987), S. 247-258 
    Details
    ISSN: 0730-2312
    Keywords: cell-cell interactions ; tumor invasion ; collagenase stimulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Past studies have shown that contact between tumor cells and fibroblasts results in stimulation of collagenase production by the fibroblasts. Membrane fractions prepared by differential centrifugation of sonicated B-16 melanoma cells were shown here to contain a collagenase stimulatory factor(s) (CSF). Trypsin treatment of intact B-16 cells prior to membrane fractionation led to loss of 90% of the total activity, indicating that CSF is localized on the outer surface of the cells. Stimulation of fibroblast collegenase production was also observed with dialyzed octylglucoside extracts of the B-16 membranes. Additional of exogeneous lipid, ie, a mixture of phosphatidylcholine and phosphatidylserine, to the detergent extract of the membranes followed by dialysis and centrifugation at 100,000g resulted in 80% recovery of the factor activity in the pellet containing reconstituted lipid vesicles. Fractionation of tritium-labeled, reconstituted lipid vesicles on a Sephacryl S-300 column revealed that the collagenase stimulatory factor coeluted with the radioactive lipid vesicles. The fractionated lipid vesicles lost stimulatory activity completely after trypsin treatment or heating at 65°C, indicating that the factor is a protein.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240350307
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  • 2
    Electronic Resource
    Electronic Resource
    Matrix influence on the tumor cell stimulation of fibroblast collagenase production (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 39-45 
    Details
    ISSN: 0730-2312
    Keywords: matrix ; collagenase ; tumor cells ; cell-matrix interactions ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Cocultures of rabbit fibroblasts and mouse B-16 melanoma cells produce increased levels of collagenase against type I collagen. This stimulatory effect was also found when fibroblasts were cultured in conditioned media from tumor cells. However, the level of the stimulatory factor in conditioned media was influenced by matrix deposited by fibroblasts. Thus, conditioned media collected from mono-layers of B-16 plated on fibroblast matrix consistently showed high levels of the factor activity. The influence of the matrix on the level of the factor was not removed by treating the fibroblast matrix with collagenase or chondroitinase ABC and was not reproduced by collagen-coated dishes.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280107
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  • 3
    Electronic Resource
    Electronic Resource
    Heparin and heparan sulfate binding sites on B-16 melanoma cells (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 136 (1988), S. 147-153 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have reported previously that the production of a tumor cell factor that stimulates synthesis of fibroblast collagenase is influenced by a fibroblast-deposited matrix component, possibly heparan sulfate-proteoglycan. In this study, binding sites for heparin and heparan sulfate on mouse B-16 melanoma cells have been demonstrated. Binding of 3H-heparin and 35S-heparan sulfate has been shown to occur to whole cells, isolated membranes, and to a component(s) of detergent extracts of the membranes. Scatchard analysis of binding of 3H-heparin yielded a Kd of 2-5 × 10-8 M and a Bmax of 0.5 × 107 heparin molecules bound per cell. Binding of 35S-heparan sulfate was of at least an order of magnitude lower affinity than heparin, but the Bmax was similar to that for heparin. Competition studies showed that 35S-heparan sulfate binding was inhibited totally by heparin and heparan sulfate and partially by dermatan sulfate, but no inhibition was obtained with hyaluronate or chondroitin sulfate. Binding of 3H-heparin was inhibited totally by heparin but to different extents by preparations of heparan sulfate from different tissue sources. The heparin/heparan sulfate binding activity is a protein(s) because it is destroyed by treatment with trypsin. Binding of 3H-heparin to transblots of the detergent extract of the B-16 cell membranes indicated that at least part of the binding activity is a 14,000-dalton protein.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041360119
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