Chondroitin sulphate modification in the alpha4 chain of human recombinant laminin-8 (alpha4beta1gamma1).
We have produced human laminin-8 (alpha4beta1gamma1) using recombinant technology. Approximately half of the recombinant laminin-8 (rLN-8) molecules were found to have a chondroitin sulphate modification in the alpha4 chain. The substituted and non-substituted forms were separated and tested for cell adhesion activity. Lower cell adhesion promoting activity was seen for the substituted form, but the integrin receptor utilization was similar. We also found the human rLN-8 to behave identically in cell adhesion assays compared to a human/mouse hybrid variant of rLN-8.
Kortesmaa
Jarkko
J
BioStratum AB, 17177 Stockholm, Sweden.
Doi
Masayuki
M
Patarroyo
Manuel
M
Tryggvason
Karl
K
D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002460:Cell Line; D002809:Chondroitin Sulfates / Q000737:chemistry*; D006801:Humans; D039121:Integrin alpha6beta1 / Q000378:metabolism; D007797:Laminin / Q000096:biosynthesis* / Q000737:chemistry* / Q000502:physiology; D051379:Mice; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism
D039121:Integrin alpha6beta1; D007797:Laminin; D011994:Recombinant Proteins; C110308:laminin 8; D002809:Chondroitin Sulfates