Mitogenic activity of peptides related to the sequence of human Fibroblast Growth Factor‐1

Linear synthetic peptides related to the human Fibroblast Growth Factor‐1 (hFGF‐1) segment [112‐147] were tested for their capacity of mimicking FGF mitogenic activity, binding to heparin‐Sepharose columns, stimulating DNA synthesis and competing with hFGF‐1 for the cellular receptors. The results o...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry and molecular biology international 1996-08, Vol.39 (6), p.1237-1244
Main Authors: Oyama, Sérgio, Miranda, Maria Terêsa M., Toma, Izaura N., Viviani, Wladia, Gambarini, Angelo G.
Format: Article
Language:English
Subjects:
3T3 Cells
Amino Acid Sequence
Animals
Binding Sites
Chromatography, Agarose
DNA - biosynthesis
FGF
FGF receptor
Fibroblast Growth Factor 1 - chemical synthesis
Fibroblast Growth Factor 1 - chemistry
Fibroblast Growth Factor 1 - pharmacology
Heparin
Humans
Mice
mitogenesis
Mitosis - drug effects
Molecular Sequence Data
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Peptide Fragments - pharmacology
Peptides - chemical synthesis
Peptides - chemistry
Peptides - pharmacology
Receptors, Cell Surface - metabolism
synthetic peptides
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Linear synthetic peptides related to the human Fibroblast Growth Factor‐1 (hFGF‐1) segment [112‐147] were tested for their capacity of mimicking FGF mitogenic activity, binding to heparin‐Sepharose columns, stimulating DNA synthesis and competing with hFGF‐1 for the cellular receptors. The results obtained indicated that the activity of these compounds is dependent on the presence of the sequence WFVGLK in their structures. The affinity for the cellular receptors increased when this sequence was elongated in order to incorporate amino acid residues that are important for FGF‐heparin binding.
ISSN:1521-6543
1039-9712
1521-6551
DOI:10.1080/15216549600201432