Molecular cloning and sequence analysis of the aggrecan interglobular domain from porcine, equine, bovine and ovine cartilage: comparison of proteinase-susceptible regions and sites of keratan sulfate substitution.
Oligonucleotide primers which were designed based on identical peptide sequences flanking the interglobular domain (IGD) of human, bovine and rat aggrecan were used in RT-PCR reactions containing human, porcine, equine, bovine and ovine cartilage RNA. Novel cDNAs encoding the IGD of the latter four species were obtained and sequenced. The deduced amino acid sequences for these cDNAs were aligned and compared with those described for six other species. Amino acid sequences surrounding the major proteolytic cleavage sites in the IGD are highly conserved, with some species-specific substitutions. Similarly, known sites of keratan sulfate attachment in the IGD are highly conserved in all species. The results provide essential amino acid sequence data for species commonly used in model systems of cartilage degeneration.
Flannery
C R
CR
Connective Tissue Biology Laboratories, School of Molecular and Medical Biosciences, University of Wales, Cardiff, UK.
Little
C B
CB
Caterson
B
B
D053674:Aggrecans; D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry*; D002417:Cattle; D003001:Cloning, Molecular; D017124:Conserved Sequence; D004285:Dogs; D016326:Extracellular Matrix Proteins; D006736:Horses; D006801:Humans; D007632:Keratan Sulfate / Q000378:metabolism*; D037181:Lectins, C-Type; D051379:Mice; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011509:Proteoglycans / Q000737:chemistry / Q000235:genetics*; D011817:Rabbits; D051381:Rats; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012756:Sheep; D013552:Swine
C508320:Acan protein, mouse; C508321:Acan protein, rat; D053674:Aggrecans; D016326:Extracellular Matrix Proteins; D037181:Lectins, C-Type; D011509:Proteoglycans; D007632:Keratan Sulfate