Characterization of two Preparations of Antibodies to Basic Fibroblast Growth Factor which Exhibit Distinct Patterns of Immunolocalization
作者:
KardamiElissavet,
MurphyLiam J.,
LiuLei,
PaduaRaymond R.,
FandrichRobert R.,
期刊:
Growth Factors
(Taylor Available online 1990)
卷期:
Volume 4,
issue 1
页码: 69-80
ISSN:0897-7194
年代: 1990
DOI:10.3109/08977199009011012
出版商: Taylor&Francis
关键词: Basic fibroblast growth factor;affinity-purified antibodies;differential immunolocalization;amino-terminal epitopes;heart
数据来源: Taylor
摘要:
AbstractImmunoglobulins reactive against basic fibroblast growth factor (bFGF) were obtained from the serum of a single rabbit immunized against residues [1-24] of bFGF conjugated to keyhole limpet hemocyanin (KLH). Pure immunoglobulin preparations no. 1 and no. 2 were prepared using different affinity chromatography columns and preabsorption to KLH-coupled Sepharose for preparation no. 1. Both preparations no. 1 and no. 2 were specific for bFGF inin vitroassays. Competition with synthetic peptides suggests that preparations no. 1 and no. 2 recognize predominantly epitope(s) within residues [16-24]bFGF or residues [1-10]bFGF, respectively,in situFurthermore, no. 2 (but not no. 1) antibodies can react with tissue-(heparin-)-bound antigen. When used in indirect immunofluorescence for bFGF in frozen heart sections, preparation no. 1 stained predominantly muscle intercalated discs (IcDs); muscle nuclei were also stained, in an overall punctate fashion. Preparation no. 2 stained muscle nuclei strongly, in association with the nuclear envelope; it also stained basement-membrane associated bFGF. Differences in immunostaining were also observed in uterine smooth muscle and kidney sections but not in skeletal muscle. It is plausible that accessibility of various epitopes within the amino-terminal region depends strongly on the local interactions of bFGF. Our data illustrate the importance of using several different antibodies to localize bFGF in a tissue
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