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J. Silnutzer, D. Barnes (1984)
A biologically active thrombin cleavage product of human serum spreading factor.Biochemical and biophysical research communications, 118 1
David Barnes, Jürgen Bosch, Hideo Masui, Kaoru Miyazaki, Gordon Sato (1981)
The culture of human tumor cells in serum-free medium.Methods in enzymology, 79 Pt B
D. Barnes, J. Silnutzer, C. See, M. Shaffer (1983)
Characterization of human serum spreading factor with monoclonal antibody.Proceedings of the National Academy of Sciences of the United States of America, 80 5
Suzuki (1984)
15307J. Biol. Chem., 259
D. Barnes (1982)
Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum-free cell cultureThe Journal of Cell Biology, 93
L. Fryklund, H. Sievertsson (1978)
Primary structure of somatomedin B A growth hormone‐dependent serum factor with protease inhibiting activityFEBS Letters, 87
Leffert (1978)
87Nat. Canc. Inst. Monogr., 48
D. Barnes, G. Sato (1979)
Growth of a human mammary tumour cell line in a serum-free mediumNature, 281
K. Olden, R. Pratt, K. Yamada (1979)
Role of carbohydrate in biological function of the adhesive glycoprotein fibronectin.Proceedings of the National Academy of Sciences of the United States of America, 76 7
D. Barnes, L. Mousetis, B. Amos, J. Silnutzer (1984)
Glass-bead affinity chromatography of cell attachment and spreading-promoting factors of human serum.Analytical biochemistry, 137 1
Foley for plasma samples from hypothyroid patients, and Drs. H. Kleinman and G. Martin for a gift of mouse laminin. This work was supported by NIH-NCI
Foidart (1980)
525Lab. Invest., 42
R. Yalow, K. Hall, R. Luft (1975)
Radioimmunoassay of somatomedin B. Application to clinical and physiologic studies.The Journal of clinical investigation, 55 1
R. Holmes (1967)
PREPARATION FROM HUMAN SERUM OF AN ALPHA-ONE PROTEIN WHICH INDUCES THE IMMEDIATE GROWTH OF UNADAPTED CELLS IN VITROThe Journal of Cell Biology, 32
D. Barnes (1984)
Attachment Factors in Cell Culture
Hoshi (1985)
125In Vitro, 21
Barnes (1980)
47J. Cell. Biochem., 14
Barnes (1982)
937C. S. H. Conf. on Cell Prolif., 9
D. Barnes, T. Foley, M. Shaffer, J. Silnutzer (1984)
Human serum spreading factor: relationship to somatomedin B.The Journal of clinical endocrinology and metabolism, 59 5
H. Leffert, K. Koch, B. Rubalcava, S. Sell, T. Moran, R. Boorstein (1978)
Hepatocyte growth control: in vitro approach to problems of liver regeneration and function.National Cancer Institute monograph, 48
D. Barnes, G. Sato (1980)
Methods for growth of cultured cells in serum-free medium.Analytical biochemistry, 102 2
Simonton (1985)
63Lab. Invest., 52
Staffan Johansson, Lena Kjéllen, Magnus Höök, R. Timpl (1981)
Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteinsThe Journal of Cell Biology, 90
P. Knox, S. Griffiths (1979)
A cell spreading factor in human serum that is not cold-insoluble globulin.Experimental cell research, 123 2
J. McGowan, A. Strain, N. Bucher (1981)
DNA synthesis in primary cultures of adult rat hepatocytes in a defined medium: Effects of epidermal growth factor, insulin, glucagon, and cyclic‐AMPJournal of Cellular Physiology, 108
(1982)
Role of attachment factors in mediating the attachment , distribution , and differentiation of cells
Barnes (1985)
9117J. Biol. Chem., 260
K. Stenn (1981)
Epibolin: a protein of human plasma that supports epithelial cell movement.Proceedings of the National Academy of Sciences of the United States of America, 78 11
(1985)
Distribution and immunolocalization of serum spreading factor in human tissue
V. Patel, H. Lodish (1984)
Loss of adhesion of murine erythroleukemia cells to fibronectin during erythroid differentiation.Science, 224 4652
Barnes (1983)
12548J. Biol. Chem., 258
(1982)
Serum spreading factor : effects in rat ovary cells and mouse embryonal carcinoma cells in serum - free media
Grotendorst (1982)
403C. S. H. Conf. on Cell Prolif., 9
Tamkun (1983)
4641J. Biol. Chem., 258
D. Barnes, J. Reing, B. Amos (1985)
Heparin-binding properties of human serum spreading factor.The Journal of biological chemistry, 260 16
D. Barnes, J. Silnutzer (1983)
Isolation of human serum spreading factor.The Journal of biological chemistry, 258 20
Basara (1985)
2487Cancer Research, 45
Shaffer (1984)
783J. Lab. Clin. Med., 103
J. Enenstein, L. Furcht (1984)
Isolation and characterization of epinectin, a novel adhesion protein for epithelial cellsThe Journal of Cell Biology, 99
Silnutzer (1984a)
245Cell Culture Meth. for Mol. and Cell Biol., 1
H. Lodish, N. Kong, M. Snider, G. Strous (1983)
Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic ratesNature, 304
J. Tamkun, R. Hynes (1983)
Plasma fibronectin is synthesized and secreted by hepatocytes.The Journal of biological chemistry, 258 7
F. Grinnell (1978)
Cellular adhesiveness and extracellular substrata.International review of cytology, 53
B. Knowles, C. Howe, D. Aden (1980)
Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen.Science, 209 4455
D. Barnes, G. Sato (1980)
Serum-free cell culture: a unifying approachCell, 22
K. Yamada (1983)
Cell surface interactions with extracellular materials.Annual review of biochemistry, 52
M. Basara, J. McCarthy, D. Barnes, L. Furcht (1985)
Stimulation of haptotaxis and migration of tumor cells by serum spreading factor.Cancer research, 45 6
(1978)
Primary structure of somato - medin B
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
Silnutzer (1985)
73In Vitro, 21
David Barnes, Richard Wolfe, G. Serrero, Don McClure, Gordon Sato (1980)
Effects of a serum spreading factor on growth and morphology of cells in serum-free medium.Journal of supramolecular structure, 14 1
S. Suzuki, M. Pierschbacher, E. Hayman, K. Nguyen, Y. Ohgren, E. Ruoslahti (1984)
Domain structure of vitronectin. Alignment of active sites.The Journal of biological chemistry, 259 24
M. Shaffer, T. Foley, D. Barnes (1984)
Quantitation of spreading factor in human biologic fluids.The Journal of laboratory and clinical medicine, 103 5
Edward, G. Hayman, Eva Engvall, Erin A'HEARN, David, Barnes Michael, Pierschbacher (1982)
Cell attachment on replicas of SDS polyacrylamide gels reveals two adhesive plasma proteinsThe Journal of Cell Biology, 95
J. Foidart, J. Berman, L. Paglia, S. Rennard, S. Abe, A. Perantoni, G. Martin (1980)
Synthesis of fibronectin, laminin, and several collagens by a liver-derived epithelial line.Laboratory investigation; a journal of technical methods and pathology, 42 5
E. Hayman, M. Pierschbacher, Y. Ohgren, E. Ruoslahti (1983)
Serum spreading factor (vitronectin) is present at the cell surface and in tissues.Proceedings of the National Academy of Sciences of the United States of America, 80 13
R. Hynes, K. Yamada (1982)
Fibronectins: multifunctional modular glycoproteinsThe Journal of Cell Biology, 95
10.1002/jcp.1041250206.abs Human serum spreading factor (SF) is a cell adhesion and spreading‐promoting glycoprotein purified from serum or plasma that mediates effects in a wide variety of animal cell culture systems. HepG2 human hepatoma cells were found to synthesize and secrete SF into culture medium. Quantitative immunoassay of the protein indicated a concentration of about 1 μg/ml in 48 hr‐conditioned medium from confluent cultures. Although fibronectin also was synthesized and secreted into the culture medium, HepG2 cell spreading was observed in response to human serum SF, but not in response to human plasma fibronectin. Immunoprecipitation of SF from culture medium of cells metabolically‐labeled with leucine, fucose or glucosamine identified a single from of the molecule of approximately 70,000 daltons. Treatment of cultures with tunicamycin inhibited incorporation of fucose and glucosamine into immunoprecipitated SF, but did not prevent synthesis and secretion of the protein. Electrophoretic analysis and cell spreading assays showed that SF secreted by tunicamycin‐treated HepG2 cells was of molecular weight (mw) approximately 60,000, and was biologically active.
Journal of Cellular Physiology – Wiley
Published: Nov 1, 1985
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