scholarly journals Involvement of Cell Surface Heparan Sulfate in the Density-Dependent Inhibition of Cell Proliferation

1981 ◽  
Vol 6 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Kozi Matuoka ◽  
Youji Mitsui
Keyword(s):  
Cell Proliferation ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Density Dependent ◽  
Dependent Inhibition

scholarly journals Cell proliferation and cell density of mesenchyme in the maxillary process and adjacent regions during facial development in the chick embryo

Development ◽  
1978 ◽  
Vol 46 (1) ◽  
pp. 65-74
Author(s):  
Robert Minkoff ◽  
Amy J. Kuntz
Keyword(s):  
Cell Proliferation ◽  
Cell Density ◽  
Regulatory Mechanism ◽  
Satisfactory Explanation ◽  
Density Dependent ◽  
Dna Labeling ◽  
Inhibition Of Growth ◽  
Developmental Age ◽  
Dependent Inhibition ◽  
Facial Development

Cell proliferation, as measured by DNA labeling indices was analyzed during the early development of the maxillary process. Chick embryos were labeled with [3H]thymidine for .1 h and processed for autoradiography. The percentage of labeled mesenchymal cells was determined within delineated areas in the maxillary processes and in adjacent regions. Analysis of labeling indices in each of the areas at successive stages of development demonstrated a pattern of declining rates of cell proliferation with advancing developmental age. Cell proliferation in adjacent regions declined earlier and, in some instances, faster than it did in the maxillary process. Cell density was measured in the maxillary process and the roof of the stomodeum and was found to be higher in the maxillary process throughout the period studied. Cell density and cell proliferation data were analyzed with reference to the operation of ‘density-dependent inhibition’ of growth as a regulatory mechanism for the observed changes. ‘Density-dependent inhibition’ of growth was not a satisfactory explanation for the observed differences between the maxillary process and adjacent regions.

Analysis of cellular interactions in density-dependent inhibition of 3T3 Cell proliferation

1982 ◽  
Vol 9 (2) ◽  
pp. 75-82 ◽  
Author(s):  
G. Adam ◽  
U. Steiner ◽  
H. Maier ◽  
S. Ullrich
Keyword(s):  
Cell Proliferation ◽  
Cellular Interactions ◽  
Density Dependent ◽  
Dependent Inhibition

scholarly journals The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation.

1995 ◽  
Vol 182 (1) ◽  
pp. 219-231 ◽  
Author(s):  
A D Luster ◽  
S M Greenberg ◽  
P Leder
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Binding Site ◽  
Platelet Factor 4 ◽  
Endothelial Cell Proliferation ◽  
Specific Cell ◽  
Platelet Factor ◽  
Self Aggregation

IP-10 is a member of the chemokine family of cytokines and is induced in a variety of cells in response to interferon gamma and lipopolysaccharide. The self-aggregation common to many chemokines, including IP-10, has hindered the identification of a specific IP-10 receptor. Using an IP-10 alkaline phosphatase fusion protein that fortuitously blocks this self-aggregation, we have identified an IP-10 binding site on a variety of cells including endothelial, epithelial, and hematopoietic cells. This binding site has a Kd of 25 nM, is inhibited by recombinant murine or human IP-10, and is dependent on the presence of cell surface heparan sulfate proteoglycans (HSPG). This conclusion is based on the findings that IP-10 binding to cells is: (a) inhibited by heparin and heparan sulfate; (b) sensitive to a 1 M NaCl wash; (c) eliminated by treatment with heparinase and trypsin; and (d) absent on mutant CHO cells that do not express cell surface HSPG. Platelet factor 4 (PF4), but not IL-8, monocyte chemoattractant protein-1, RANTES, monocyte inflammatory protein (MIP)-1 alpha, or MIP-1 beta, can compete effectively with IP-10 for binding to the cell surface. Furthermore, IP-10 shares with PF4 the ability to inhibit endothelial cell proliferation (IC50 = 150 nM). These studies demonstrate specificity in the interaction of chemokines and HSPG, and they define IP-10 and PF4 as a distinct subset of chemokines sharing an HSPG-binding site and angiostatic properties.

scholarly journals Relationship of transformation, cell density, and growth control to the cellular distribution of newly synthesized glycosaminoglycan.

1976 ◽  
Vol 71 (1) ◽  
pp. 280-294 ◽  
Author(s):  
R H Cohn ◽  
J J Cassiman ◽  
M R Bernfield
Keyword(s):  
Hyaluronic Acid ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Cell Density ◽  
Growth Control ◽  
Cellular Distribution ◽  
High Cell ◽  
Density Dependent ◽  
Relationship Of

Mouse 3T3 cells and their Simian Virus 40-transformed derivatives (3T3SV) were used to assess the relationship of transfromation, cell density, and growth control to the cellular distribution of newly synthesized glycosaminoglycan (GAG). Glucosamine- and galactosamine-containing GAG were labeled equivalently by [3H=A1-glucose regardless of culture type, allowing incorporation into the various GAG to be compared under all conditions studied. Three components of each culture type were examined: the cells, which contain the bulk of newly synthesized GAG and are enriched in chondroitin sulfate and heparan sulfate; cell surface materials released by trypsin, which contain predominantly hyaluronic acid; and the media , which contain predominantly hyaluronic acid and undersulfated chondroitin sulfate. Increased cell density and viral transformation reduce incorporation into GAG relative to the incorporation into other polysaccharides. Transformation, however, does not substantially alter the type or distribution of newly synthesized GAG; the relative amounts and cellular distributions were very similar in 3T3 and 3T3SV cultures growing at similar rates at low densities. On the other hand, increased cell density as well as density-dependent growth inhibition modified the type and distribution of newly synthesized GAG. At high cell densities both cell types showed reduced incorporation into hyaluronate and an increase in cellular GAG due to enhanced labeling of chondroitin sulfate and heparan sulfate. These changes were more marked in confluent 3T3 cultures which also differed in showing substantially more GAG label in the medium and in chondroitin-6-sulfate and heparan sulfate at the cell surface. Since cell density and possibly density-dependent inhibition of growth but not viral transformation are major factors controlling the cellular distribution and type of newly synthesized GAG, differences due to GAG's in the culture behavior of normal and transformed cells may occur only at high cell density. The density-induced GAG alterations most likely involved are increased condroitin-6-sulfate and heparan sulfate and decreased hyaluronic acid at the cell surface.

scholarly journals Molecular cloning of the major cell surface heparan sulfate proteoglycan from rat liver.

1992 ◽  
Vol 267 (6) ◽  
pp. 3894-3900
Author(s):  
A Pierce ◽  
M Lyon ◽  
I.N. Hampson ◽  
G.J. Cowling ◽  
J.T. Gallagher
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Molecular Cloning ◽  
Rat Liver ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan

scholarly journals Atypical role of sprouty in p21 dependent inhibition of cell proliferation in colorectal cancer

2015 ◽  
Vol 55 (9) ◽  
pp. 1355-1368 ◽  
Author(s):  
Qiong Zhang ◽  
Katherine Shim ◽  
Kevin Wright ◽  
Alexander Jurkevich ◽  
Sharad Khare
Keyword(s):  
Colorectal Cancer ◽  
Cell Proliferation ◽  
Dependent Inhibition
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