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Updated: Aug 12, 2026

Synthesis of Thermogelling Poly(N-isopropylacrylamide)-graft-chondroitin Sulfate Composites with Alginate Microparticles for Tissue Engineering
Published on: October 26, 2016
Modification of the laminin alpha 4 chain by chondroitin sulfate attachment to its N-terminal domain
1Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany. sasaki@biochem.mpg.de
Abstract:
The N-terminal domain of laminin alpha 4 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 alpha 4 chain present in extracts of adult mouse tissues. Antibodies to the fragment were useful to demonstrate a relatively high content of alpha 4 in several tissues and for the immunolocalization in various blood vessels, some basement membranes and interstitial regions.
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