Isolation and characterization of small proteoglycans from different zones of the porcine knee meniscus. 1997

P G Scott, and T Nakano, and C M Dodd
Department of Biochemistry, University of Alberta, Edmonton, Canada. Scottp@gpu.srv.ualberta.ca

Pig knee menisci were dissected into three zones of equal width representing inner, i.e. medial (zone 1), middle (zone 2) and outer, i.e. lateral (zone 3) tissue. Proteoglycans (PGs) were extracted with guanidinium chloride, isolated by ion-exchange chromatography and separated into two groups ('small' and 'large') by gel filtration. The small PGs were further fractionated by hydrophobic-interaction chromatography on Octyl-Sepharose. The PG eluting earliest from Octyl-Sepharose was identified as decorin on the basis of the size of the protein core produced by digestion with chondroitinase ABC, its recognition by monoclonal antibodies raised against bovine decorin and its N-terminal sequence, 23 of 24 amino acids of which were identified. Decorin represented about 23%, 28% and 32% of the total small PG recovered from Octyl-Sepharose from zones 1, 2 and 3, respectively. The major small PG in the meniscus, eluting from Octyl-Sepharose after decorin, was identified as biglycan by the size of core, recognition by a polyclonal antiserum raised against bovine biglycan and sequence of the N-terminal 26 amino acids. Biglycan accounted for approximately 53%, 52% and 38% of PG recovered from zones 1, 2 and 3, respectively. The glycosaminoglycan chains on both decorin and biglycan were identified as dermatan sulphate by their susceptibility to chondroitinase-B. Stains-All staining of SDS gels of Octyl-Sepharose eluates revealed the presence of a third small PG eluting slightly later than biglycan. This PG was purified by a further cycle of chromatography on Octyl-Sepharose and identified as fibromodulin on the basis of its amino acid composition and the N-terminal sequence obtained after digestion with pyroglutamate aminopeptidase. It was obtained in highest amounts from the inner (zone 1) tissue, which also yielded more biglycan and less decorin. Fibromodulin from the meniscus was shown to inhibit the formation of fibrils from a solution of type I collagen, independently of the effects of decorin. These results support the concept that the distributions and characteristics of the small PGs in knee meniscus reflect regional adaptation to functional demands.

UI MeSH Term Description Entries
D008592 Menisci, Tibial The interarticular fibrocartilages of the superior surface of the tibia. Lateral Menisci,Medial Menisci,Menisci, Lateral,Menisci, Medial,Semilunar Cartilages,Tibial Menisci,Meniscus, Medial,Meniscus, Tibial,Tibial Meniscus,Cartilage, Semilunar,Cartilages, Semilunar,Lateral Meniscus,Medial Meniscus,Meniscus, Lateral,Semilunar Cartilage
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011509 Proteoglycans Glycoproteins which have a very high polysaccharide content. Proteoglycan,Proteoglycan Type H
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013552 Swine Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA). Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog

Related Publications

P G Scott, and T Nakano, and C M Dodd
May 1979, The Journal of biological chemistry,
P G Scott, and T Nakano, and C M Dodd
November 1990, Journal of chromatography,
P G Scott, and T Nakano, and C M Dodd
February 1979, The Journal of biological chemistry,
P G Scott, and T Nakano, and C M Dodd
August 1986, Biochimica et biophysica acta,
P G Scott, and T Nakano, and C M Dodd
January 1982, Methods in enzymology,
P G Scott, and T Nakano, and C M Dodd
February 1978, The Journal of biological chemistry,
P G Scott, and T Nakano, and C M Dodd
July 1977, The Journal of biological chemistry,
P G Scott, and T Nakano, and C M Dodd
August 1980, The Journal of biological chemistry,
P G Scott, and T Nakano, and C M Dodd
January 1994, Methods in enzymology,
P G Scott, and T Nakano, and C M Dodd
January 1987, Methods in enzymology,
Copied contents to your clipboard!