Modification of the laminin alpha 4 chain by chondroitin sulfate attachment to its N-terminal domain.
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.
Sasaki
T
T
Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany. sasaki@biochem.mpg.de
Mann
K
K
Timpl
R
R
D000818:Animals; D000906:Antibodies; D019765:Chondroitin ABC Lyase / Q000378:metabolism; D002809:Chondroitin Sulfates / Q000235:genetics* / Q000276:immunology; D005455:Fluorescent Antibody Technique; D007106:Immune Sera; D007797:Laminin / Q000235:genetics* / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D010446:Peptide Fragments / Q000235:genetics; D011817:Rabbits; D011863:Radioimmunoassay; D011994:Recombinant Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D014018:Tissue Distribution
D000906:Antibodies; D007106:Immune Sera; C501370:Lama4 protein, mouse; D007797:Laminin; D010446:Peptide Fragments; D011994:Recombinant Proteins; D002809:Chondroitin Sulfates; D019765:Chondroitin ABC Lyase