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Binding specificity of lung surfactant protein SP-D for glucosylceramide.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kuroki Y,Gasa S,Ogasawara Y,Shiratori M,Makita A,Akino T

doi

10.1016/0006-291x(92)91291-w

subject

Has Abstract

pub_date

1992-09-16 00:00:00

pages

963-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91291-W

journal_volume

187

pub_type

杂志文章

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