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PMID: 1722330 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Cytotactin binding: inhibition of stimulated proliferation and intracellular alkalinization in fibroblasts.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 24 ·1991-12-15 ·Pages 11403-7

Crossin KL

Abstract

Cytotactin is an extracellular matrix protein that is dynamically and transiently expressed in a place-dependent fashion during development by glial cells, fibroblasts, and several other cell types. In the present study, the effects of cytotactin on cell proliferation were examined in fibroblastic cells in culture. NIH 3T3 mouse cells plated on tissue culture substrata in the presence of soluble cytotactin remained rounded for longer periods than untreated control cells, similar to their response to cytotactin-coated substrates. These rounding effects could be prevented by pretreatment of the cells with nocodazole, a microtubule-disrupting agent. Cytotactin inhibited the proliferation of fibroblasts in culture in a dose- and time-dependent manner, and this inhibition occurred even after nocodazole treatment. In addition, the presence of cytotactin inhibited proliferation stimulated by growth factors or tumor promoter. These effects on cell growth were accompanied by an early inhibition of the intracellular alkalinization that normally occurs upon mitogenic stimulation by a number of growth-promoting agents. Together these observations suggest that cytotactin is an endogenous cell surface modulatory protein and provide a possible mechanism whereby cytotactin may contribute to pattern formation during development, regeneration, tumorigenesis, and wound healing.

MeSH Terms
3T3 Cells Animals Brain Cell Adhesion Molecules, Neuronal/isolation & purification,metabolism,physiology Cell Division/drug effects Chick Embryo DNA Replication/drug effects Epidermal Growth Factor/pharmacology Extracellular Matrix Extracellular Matrix Proteins/isolation & purification,metabolism,physiology Fibroblast Growth Factor 1/pharmacology Fibroblast Growth Factor 2/pharmacology Growth Substances/pharmacology Hydrogen-Ion Concentration Kinetics Mice Platelet-Derived Growth Factor/pharmacology Tenascin Tetradecanoylphorbol Acetate/pharmacology Thymidine/metabolism
Chemicals
Cell Adhesion Molecules, Neuronal Extracellular Matrix Proteins Growth Substances Platelet-Derived Growth Factor Tenascin Fibroblast Growth Factor 2 Fibroblast Growth Factor 1 Epidermal Growth Factor Tetradecanoylphorbol Acetate Thymidine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Crossin K L
Rockefeller University, New York, NY 10021.
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42 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.24.11403
Published
1991-12-15
Pages
11403-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC53143
Subset
IM
Grants
NIDDK NIH HHS · DK04256 · United States
External Links
PubMed source DOI: 10.1073/pnas.88.24.11403 PMC Full Text View journal details
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