scholarly journals The effects of fibronectin on the migration of human foreskin fibroblasts and Syrian hamster melanoma cells into three-dimensional gels of native collagen fibres

1981 ◽  
Vol 48 (1) ◽  
pp. 301-314
Author(s):  
S.L. Schor ◽  
A.M. Schor ◽  
G.W. Bazill

The effects of fibronectin on the migration of human skin fibroblasts and Syrian hamster melanoma cells into 3-dimensional gels of native collagen fibres have been examined. Cell migration into the 3-dimensional gel was measured by plating cells on the gel surface and then determining the percentage of cells within the gel at various times thereafter by direct microscopic examination. We find that fibronectin bound to collagen inhibits the migration of human skin fibroblasts and stimulates the migration of melanoma cells into the gel matrix. Fibronectin had no apparent effect on cell adhesion to the collagen gels, proliferation or morphology under the conditions studied.

1983 ◽  
Vol 215 (1) ◽  
pp. 107-116 ◽  
Author(s):  
J T Gallagher ◽  
N Gasiunas ◽  
S L Schor

Human skin fibroblasts cultured on collagen gels produced two dermatan sulphate species, one, enriched in iduronic acid residues, that bound specifically to the collagenous fibres of the gel, the other, enriched in glucuronic acid, that accumulated in the culture medium. Collagen-binding and collagen-non-binding dermatan sulphates were also produced by cells grown on plastic surfaces, but in these cultures each constituent was released into the growth medium. Net synthesis of dermatan sulphate was 3-fold higher in cells maintained on collagen gels. In contrast, heparan sulphate synthesis was not influenced by the nature of the culture surface. The concentration of heparan sulphate in surface-membrane extracts was similar for cells grown on plastic and on collagen gels, but cells cultured on collagen showed a notable increase in the content of surface-membrane dermatan sulphate. The patterns of synthesis and distribution of sulphated glycosaminoglycans observed in skin fibroblasts maintained on collagen gels may reflect differentiated cellular functions.


1985 ◽  
Vol 79 (1) ◽  
pp. 67-81 ◽  
Author(s):  
C. Guidry ◽  
F. Grinnell

During reorganization of collagen gels by human skin fibroblasts the total protein content of the gels remained approximately constant. Only 5% of the collagen was degraded, although the volume of the gels decreased by 85% or more. It could be concluded, therefore, that gel reorganization required physical rearrangement of pre-existing collagen fibrils rather than degradation of the original collagen and resynthesis of a new matrix. Collagen molecules in the gels were not covalently crosslinked or otherwise modified enzymically during gel reorganization, as determined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis and collagen repolymerization studies. Serum was required for gel reorganization and, in the absence of serum, cell spreading was predominantly filipodial, i.e. there was little cytoplasmic reorganization. At the electron-microscopic level it was found that many more collagen fibrils became associated with the cells in the presence of serum than in its absence. Serum was also found to promote the synthesis and secretion of proteins by the cells, and conditioned medium could take the place of serum in promoting gel reorganization. The involvement of cell-secreted factors was also demonstrated by the ability of cycloheximide to inhibit gel reorganization. Finally, when gel reorganization was stopped by adding cytochalasin D to the incubations or removing cells by detergent treatment, a small but significant re-expansion of the collagen fibrils was observed. Consequently, a portion of the collagen that had been physically reorganized by the gels was unstable and could not hold its position without continued force exerted by the cells.


DNA Repair ◽  
2008 ◽  
Vol 7 (6) ◽  
pp. 912-921 ◽  
Author(s):  
Wolfgang Eiberger ◽  
Beate Volkmer ◽  
Rachel Amouroux ◽  
Claudine Dhérin ◽  
J. Pablo Radicella ◽  
...  

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 117-LB
Author(s):  
LUKE R. LEMMERMAN ◽  
MARIA ANGELICA RINCON-BENAVIDES ◽  
SARAH A. TERSEY ◽  
BRITANI N. BLACKSTONE ◽  
HEATHER M. POWELL ◽  
...  

Author(s):  
Ok Kyung Kim ◽  
Da-Eun Nam ◽  
Min-Jae Lee ◽  
Namgil Kang ◽  
Jae-Youn Lim ◽  
...  

1983 ◽  
Vol 116 (1) ◽  
pp. 154-161 ◽  
Author(s):  
Ronald P.J. Oude Elferink ◽  
Erik Harms ◽  
Anneke Strijland ◽  
Joseph M. Tager

1984 ◽  
Vol 12 (2) ◽  
pp. 89-97
Author(s):  
Graham R. Elliott ◽  
H.E. Amos ◽  
James W. Bridges

The rate of growth of normal human skin fibroblasts was inhibited in a dose related, reversible, fashion by practolol (N-4-(2-hydroxy)-3 (1-methyl)-aminopropoxyphenylacetamine) (ID50 1.35 ± 0.14 x 10-3M), propranolol (1-(isopropylamino)-3(1-naphthyl-oxy)-2-propranolol) (ID50 0.145 ± 0.02 x 10-3M) and paracetamol (N-(4-hydroxyphenyl) acetamide) (ID50 0.85 ± 0.2 x 10-3M). Skin fibroblasts isolated from a psoriasis patient were more sensitive towards practolol (ID50 0.48 ± 0.14 x 10-3M) and propranolol (ID50 0.032 ± 0.002 x 10-3M), but less sensitive towards paracetamol (ID50 1.3 ± 0.07 x 10-3M). In vitro generated metabolites of practolol, using normal or Arochlor 1254-pretreated hamster liver preparations, and structural analogues of practolol had no effect upon the growth of either cell type.


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