Modification of the laminin α4 chain by chondroitin sulfate attachment to its N‐terminal domain

FEBS Letters

Mann, Karlheinz¹  Sasaki, Takako¹  Timpl, Rupert¹ 

[1] Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany

关键词: Basement membrane;    Laminin;    Proteoglycan;    Tissue expression;   

DOI  :  10.1016/S0014-5793(01)02812-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The N-terminal domain of laminin α4 chains corresponds to a short rod-like structure which after recombinant production was found to be modified by chondroitin sulfate. Substitution occurred mainly to a single serine in its N-terminal ASGDG sequence. A similar yet partial modification was also demonstrated for the α4 chain present in extracts of adult mouse tissues. Antibodies to the fragment were useful to demonstrate a relatively high content of α4 in several tissues and for the immunolocalization in various blood vessels, some basement membranes and interstitial regions.

【 授权许可】

Unknown