Isolation and characterization of a collagen fibril-associated dermatan sulphate proteoglycan from bovine lung.
Dermatan sulphate proteoglycans have been extracted from bovine lung with 2.0 M CaCl2 and isolated using CsCl density gradient centrifugation, DEAE ion-exchange chromatography, gel chromatography and preparative sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Ultrastructurally these proteoglycans are specifically associated with collagen fibrils. Dermatan sulphate (Mr 15.10(3)-35.10(3), with a strong prevalence for the higher Mr) is link via an O-glycosidic bond to a protein core, which is rich in Asx, Glx and Leu. Of the total uronic acid, 91% is iduronic acid. A part of the glucuronic acid residues is located near the protein core and a large cluster of disaccharides is devoid of glucuronic acid residues. An inhibition enzyme immunoassay has been developed to quantitate the proteoglycan. A model for the interaction between dermatan sulphate proteoglycans and collagen fibrils is proposed.
van Kuppevelt
T H
TH
Department of Chemical Cytology, University of Nijmegen, The Netherlands.
Janssen
H M
HM
van Beuningen
H M
HM
Cheung
K S
KS
Schijen
M M
MM
Kuyper
C M
CM
Veerkamp
J H
JH
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002807:Chondroitin / Q000031:analogs & derivatives*; D011508:Chondroitin Sulfate Proteoglycans / Q000302:isolation & purification*; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000378:metabolism*; D003871:Dermatan Sulfate / Q000302:isolation & purification*; D007124:Immunoenzyme Techniques; D008168:Lung / Q000032:analysis*; D008854:Microscopy, Electron; D008970:Molecular Weight; D011509:Proteoglycans / Q000302:isolation & purification*
D000596:Amino Acids; D011508:Chondroitin Sulfate Proteoglycans; D011509:Proteoglycans; C032649:dermatan sulfate proteoglycan; D003871:Dermatan Sulfate; D002807:Chondroitin; D003094:Collagen