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PMID: 2491959 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Domains of laminin with growth-factor activity.

Cell ·Vol. 56 ·No. 1 ·1989-01-13 ·Pages 93-101

Panayotou G, End P, Aumailley M, Timpl R, Engel J

Abstract

Laminin and fragments (1, 1-4) containing the inner rod-like segments from its short arms, which consist of cysteine-rich, "EGF-like" repeats, stimulated thymidine incorporation in cultured cells possessing EGF receptors but had no effect on a cell line lacking this receptor. The response was comparable to that of EGF concerning effective concentrations, magnitude, time dependence, and synergistic enhancement by insulin. Other fragments (4 and 8) were inactive. Laminin and its active fragments could not compete with the binding of EGF to cells. There was no correlation between growth promotion and attachment of cells to a high affinity binding site present on laminin fragment 8. The data indicate that mitogenic effects induced by laminin and EGF proceed in some steps via related pathways and that different domains of laminin are involved in growth promotion and in adhesion and spreading of cells.

MeSH Terms
Amino Acid Sequence Animals Cell Adhesion Cell Division/drug effects Cells, Cultured/cytology Epidermal Growth Factor/pharmacology Extracellular Matrix/physiology Growth Substances/physiology Laminin/physiology,ultrastructure Membrane Glycoproteins Membrane Proteins/pharmacology Mice Peptide Fragments/pharmacology Solubility Structure-Activity Relationship Time Factors
Chemicals
Growth Substances Laminin Membrane Glycoproteins Membrane Proteins Peptide Fragments nidogen Epidermal Growth Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Panayotou G
National Institute for Medical Research, London, England.
End P
Aumailley M
Timpl R
Engel J
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1989-01-13
Pages
93-101
Language
English
Region
United States
NLM ID
0413066
Subset
IM
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