A Novel Disulfide Pattern in Laminin-Type Epidermal Growth Factor-like (LE) Modules of Laminin β1 and γ1 Chains

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• 作者：Stefan Kalkhof ; Konstanze Witte ; Christian H. Ihling ; Mathias Q. Mller ; Manuel V. Keller ; Sebastian Haehn ; Neil Smyth ; Mats Paulsson ; Andrea Sinz
• 刊名：Biochemistry
• 出版年：2010
• 出版时间：September 28, 2010
• 年：2010
• 卷：49
• 期：38
• 页码：8359-8366
• 全文大小：1002K
• 年卷期：v.49,no.38(September 28, 2010)
• ISSN：1520-4995

文摘

In-depth mass spectrometric analysis of disulfide bond patterns in recombinant mouse laminin β1 and γ1 chain N-terminal fragments comprising the laminin N-terminal (LN) domain and the first four laminin epidermal growth factor-like (LE) domains revealed a novel disulfide pattern for LE domains. This showed a (2−3, 4−5, 6−7, 8−1) connectivity with the last cysteine of one LE domain being connected to the first cysteine of the following LE domain. The same pattern was also found in E4, the N-terminal β1 chain fragment derived by elastase digestion of mouse EHS tumor laminin-111, showing that this pattern occurs in native laminin. The strictly linear pattern with an interdomain disulfide has not been described previously for EGF domains. The N-terminal portions of laminin short arms, consisting of the LN domain and LE domains 1−4, are essential for laminin−laminin self-interactions, whereas the internal LE domains 7−9 in the laminin γ1 chain harbor the nidogen binding site and have a conventional disulfide pattern. This suggests that LE domains differing in function also differ in their disulfide patterns.