STRUCTURE-FUNCTION-RELATIONSHIPS OF BOVINE PULMONARY SURFACTANT PROTEINS - SP-B AND SP-C

被引：72

作者：

TAKAHASHI, A ^{[1
]}

WARING, AJ ^{[1
]}

AMIRKHANIAN, J ^{[1
]}

FAN, B ^{[1
]}

TAEUSCH, HW ^{[1
]}

机构：

[1] KING DREW MED CTR,DEPT PEDIAT,12021 S WILMINGTON AVE,LOS ANGELES,CA 90059

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1044卷 / 01期

关键词：

Proteolipid; Pulmonary surfactant; Surface tension;

D O I：

10.1016/0005-2760(90)90216-K

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：

Pulmonary surfactant contains at least three unique proteins: SP-A, SP-B and SP-C. SP-B and SP-C from bovine surfactant are markedly hydrophobic and have molecular masses between 3 and 26 kDa. We identify surfactant proteins under nonreducing conditions on polyacrylamide gels with approximate molecular mass of 5, 14, 26 kDa (SP-5, 14, 26) when organic solvent-soluble material is eluted from a Sephadex LH-20 size exclusion column followed by separation on a high-performance reverse-phase chromatography system. These bands correspond to monomeric SP-C, oligomeric SP-C and oligomeric SP-B, respectively. Computer analysis (Eisenberg-hydrophobic moment) of sequences for these proteins suggests that SP-B contains surface-seeking amphiphilic segments. In contrast, SP-C resembles a more hydrophobic transmembrane anchoring peptide. Dispersions containing dipalmitoylphosphatidylcholine, phosphatidylglycerol, palmitic acid and multimeric SP-B and SP-C duplicate the surface activity of natural surfactant when assayed in a pulsating bubble surfactometer. We speculate that oligomers of SP-B and monomers and oligomers of SP-C may act cooperatively in affecting surfactant function. An important function of SP-B and SP-C may be to affect the ordering of surfactant lipids so that rates of transport of surfactant lipids to the hypophase surface in the alveoli are enhanced. © 1990.

引用

页码：43 / 49

页数：7

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