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Microfibril-associated glycoprotein: characterization of the bovine gene and of the recombinantly expressed protein.

Abstract：

:Microfibrils having a diameter of 10-12 nm, found either in association with elastin or independently, are an important component of the extracellular matrix of many tissues. Because isolation of native proteins composing the microfibrils has proven difficult, information on structure/function relationships is limited. In order to extend our understanding of the 31-kDa microfibril-associated glycoprotein (MAGP), the bovine gene has been cloned and characterized and the protein has been expressed in a eukaryotic system. The compact coding portion of the gene is contained in 4.5 kbp of genomic DNA and does not appear to share any domain motifs with other known proteins. The size, amino acid composition, and sequence of the amino terminus of the secreted recombinant protein (rMAGP) all agree with values predicted by the nucleotide sequence of the cDNA used in the expression vector. The rMAGP reacts with a monospecific antibody prepared against a defined amino acid sequence of the natural molecule and reacts specifically with recombinantly produced tropoelastin, suggesting that rMAGP will be a useful reagent with which to study its interaction with other extracellular matrix components.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Bashir MM,Abrams WR,Rosenbloom J,Kucich U,Bacarra M,Han MD,Brown-Augsberger P,Mecham R,Rosenbloom J

doi

10.1021/bi00168a026

subject

Has Abstract

pub_date

1994-01-18 00:00:00

pages

593-600

issue

2

eissn

0006-2960

issn

1520-4995

journal_volume

33

pub_type

杂志文章

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