Transport Mechanism of Basic Fibroblast Growth Factor(bFGF) Through the Blood-brain Barrier.
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Accession number;00A0997677
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| Title;Transport Mechanism of Basic Fibroblast Growth Factor(bFGF) Through the Blood-brain Barrier. |
| Author;
DEGUCHI YOSHIHARU
(Univ. of Shizuoka, Sch. of Pharm. Sci.)
OKUTSU HIROSHI
(Univ. of Shizuoka, Sch. of Pharm. Sci.)
YUGE TAKURO
(Kaken Pharm. Co., Ltd.)
FURUKAWA AKIHIKO
(Kaken Pharm. Co., Ltd.)
OTSUKI SUMIO
(Tohoku Univ., Grad. Sch.)
HOSOYA KEN'ICHI
(Tohoku Univ., Grad. Sch.)
TERASAKI TETSUYA
(Tohoku Univ., Grad. Sch.)
MORIMOTO KAZUHIRO
(Hokkaido Inst. of Pharm. Sci.)
KIMURA RYOHEI
(Univ. of Shizuoka, Sch. of Pharm. Sci.)
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Journal Title;Xenobiotic Metabolism and Disposition
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Journal Code:X0758A
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ISSN:0916-1139
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VOL.15;NO.Supplement;PAGE.S104-S105(2000)
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| Figure&Table&Reference;FIG.1, TBL.1, REF.8 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;This study was carried out to investigate the transport mechanism of basic fibroblast growth factors(bFGF) through blood-brain barriers(BBB). Following an internal carotid artery perfusion, 125I-bFGF was transcytosed through the BBB from blood into brain parenchyma. The saturable binding of 125I-bFGF to the isolated bovine brain capillaries(Kd=40nM, and Bmax=200pmol/mg) was significantly inhibited by unlabelled bFGF, poly-L-lysine, heparin and glycosaminoglycans with a sulfate residue. The heparin-resistant binding of 125I-bFGF to the conditionally immortalized mouse brain capillary endothelial cell lines(TM-BBB) was saturable and showed significant dependence on temperature and medium osmolarity. This binding was effectively inhibited in cells treated with heparinase, sodium chlorate and an antibody specific to perlecan, a HSPG. Finally, RT-PCR analysis revealed expression of perlecan, and FGF receptors(FGFR1 and FGFR2) mRNA in TM-BBB. These results are consistent with the conclusions, 1) 125I-bFGF is transcytosed through the BBB, and 2) transport of 125I-bFGF through the BBB may be, in part, ascribed to endocytosis mechanism that is triggered by binding to HSPG. (author abst.) |
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