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Chondroitin sulphate modification in the alpha4 chain of human recombinant laminin-8 (alpha4beta1gamma1).
- Source :
-
Matrix biology : journal of the International Society for Matrix Biology [Matrix Biol] 2002 Oct; Vol. 21 (6), pp. 483-6. - Publication Year :
- 2002
-
Abstract
- 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.<br /> (Copyright 2002 Elsevier Science B.V. and International Society of Matrix Biology)
- Subjects :
- Animals
Cell Adhesion physiology
Cell Line
Humans
Integrin alpha6beta1 metabolism
Laminin physiology
Mice
Protein Multimerization
Recombinant Proteins biosynthesis
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Chondroitin Sulfates chemistry
Laminin biosynthesis
Laminin chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0945-053X
- Volume :
- 21
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Matrix biology : journal of the International Society for Matrix Biology
- Publication Type :
- Academic Journal
- Accession number :
- 12392759
- Full Text :
- https://doi.org/10.1016/s0945-053x(02)00052-5