FEBS Letters | |
Chemical cross‐linking leads to two high molecular mass aggregates of rat α 1 β 1 integrin differing in their conformation but not in their composition | |
Hofmann, Werner1  Löster, Klemens1  Baum, Oliver1  Reutter, Werner1  | |
[1] Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Arnimallee 22, D-14195 Berlin-Dahlem, Germany | |
关键词: Chemical cross-linking; Rat α 1 β 1 integrin; DSS; disuccinimidylsuberate; DSP; dithiobis(succinimidylpropionate); DTT; dithiothreitol; mAb; monoclonal antibody; M r; relative molecular mass; | |
DOI : 10.1016/0014-5793(95)01053-H | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
In order to detect protein interactions of the collagen/laminin receptor α 1 β 1 integrin, covalent chemical cross-linking was performed with the homo-bifunctional, amine reactive reagents DSS (disuccinimidylsuberate) and DSP (dithiobis(succinimidylpropionate)). After cross-linking of the 190 kDa rat α 1 integrin subunit, immunoblotting revealed two additional, immunoreactive, high molecular mass complexes (M r 240/290 k). Generation of the 240/290 kDa aggregates depended on the presence of the intact tertiary protein structure. As shown with immunoaffinity purified proteins, the 240/290 kDa aggregates consist exclusively of α 1 and β 1 integrin subunits. No other cross-linked proteins associated with the α 1 or β 1 subunit were detected. In contrast to the non-cross-linkable α 1 β 1 integrin, the 240/290 kDa aggregates presumably represent active forms of the adhesion receptor, because both bound in vitro to collagen I and IV. This ability of α 1 β 1 integrin to cross-link and produce two additional high molecular mass forms is shared by rat α 9 β 1 integrin. Thus, the cross-linking approach directly indicates that β 1 integrins occur in different conformations caused by variations in the folding and/or spatial arrangement of their subunits.
【 授权许可】
Unknown
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