BINDING-SPECIFICITY OF LUNG SURFACTANT PROTEIN SP-D FOR GLUCOSYLCERAMIDE

被引：43
|
作者：
KUROKI, Y
GASA, S
OGASAWARA, Y
SHIRATORI, M
MAKITA, A
AKINO, T
机构：
[1] HOKKAIDO UNIV,SCH MED,INST CANC,BIOCHEM LAB,ELECT ENGN & ELECTR,SAPPORO,HOKKAIDO 060,JAPAN
[2] SAPPORO MED COLL,DEPT CHEM,CHUO KU,SAPPORO,HOKKAIDO 060,JAPAN
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 187卷 / 02期
关键词：
D O I：
10.1016/0006-291X(92)91291-W
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The specificities of the binding of lung surfactant protein SP-D to glycolipids were examined using 125I-labeled SP-D as a probe. When the binding study was performed on TLC plates, SP-D bound exclusively to GlcCer, whereas it failed to bind to GalCer, GM1, GM2, asialo-GM1, asialo-GM2, sulfatide, Forssman antigen, ceramide dihexoside, ceramide trihexoside, globoside, paragloboside or ceramide. Excess native SP-D competed with 125I-SP-D for the binding to GlcCer. Antibody to rat SP-D inhibited 125I-SP-D binding to GlcCer. Ca2+ was absolutely required for the binding of SP-D to GlcCer; Mg2+ failed to substitute for Ca2+. SP-D bound to ceramide monohexoside in glycolipids isolated from rat lung and bronchoalveolar lavage fluids of rats. © 1992.
引用
收藏
页码：963 / 969
页数：7
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