Inhibition of glycosaminoglycan modification of perlecan domain I by site‐directed mutagenesis changes protease sensitivity and laminin‐1 binding activity

FEBS Letters

Mann, Karlheinz²  Sasaki, Takako²  Costell, Mercedes¹  Timpl, Rupert² 

[1] Departement Bioquimica y Biologia Molecular, Facultad de Ciencias Biologicas, Universidad de Valencia, Burjassot, Spain;Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany

关键词: Basement membrane;    Proteoglycan;    Proteolysis;    Recombinant protein;    Site-directed mutagenesis;   

DOI  :  10.1016/S0014-5793(98)01063-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Glycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.

【 授权许可】

Unknown