6533b860fe1ef96bd12c3b90

RESEARCH PRODUCT

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

Rupert TimplMercedes CostellTakako SasakiKarlheinz Mann

subject

ProteasesBasement membraneRecombinant proteinmedicine.medical_treatmentMolecular Sequence DataBiophysicsPerlecanBiochemistrySubstrate SpecificityStructural BiologyLamininEndopeptidasesGeneticsmedicineAnimalsAmino Acid SequenceBinding siteSite-directed mutagenesisMolecular BiologyGlycosaminoglycansSite-directed mutagenesisBinding SitesProteasebiologyChemistryMutagenesisCell BiologyRecombinant ProteinsBiochemistryProteoglycanProteoglycanProteolysisMutagenesis Site-Directedbiology.proteinProteoglycansHeparitin SulfateLamininHeparan Sulfate ProteoglycansProtein Binding

description

AbstractGlycosaminoglycan 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.

yearjournalcountryeditionlanguage
1998-09-18FEBS Letters
10.1016/s0014-5793(98)01063-1http://dx.doi.org/10.1016/S0014-5793(98)01063-1