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PMID: 4266092 Published · ppublish English Journal Article

Proteoglycans of the knee-joint cartilage of young normal and lame pigs.

The Biochemical journal ·Vol. 130 ·No. 1 ·1972-11-00 ·Pages 181-7

Sĭmůnek Z, Muir H

Abstract

Intensive rearing, and restricted activity, induce rapid growth in pigs, but they often become lame. Groups of normal and lame pigs reared intensively were killed when 10 or 25 weeks old. Although there were no differences in the overall composition of the knee-joint cartilage of lame and sound animals, the proteoglycans in the cartilage of the lame pigs were extracted more easily by a standardized sequential procedure and contained a higher proportion of molecules of smaller size as assessed by gel chromatography on 6% agarose and Sepharose 4B. These increased at the expense of both the larger and mediumsized molecules. Differences were most evident at 10 weeks of age, when there was twice as much of the smaller proteoglycans in the cartilage of lame pigs. Despite these size-differences, the compositions of the proteoglycans in corresponding sequential extracts of cartilage of lame and normal groups were the same, as were the changes in chemical composition that accompany development. Proteoglycans from lame animals may have undergone limited proteolysis, thus decreasing their size without changing their composition detectably. As the differences between normal and lame groups were greater at 10 weeks than at 25 weeks of age, the first weeks after birth (when the greatest changes occur in the proteoglycans and in the cartilage) may be a critical period in the maturation of articular cartilage in this species. At this time, rapid gain in weight produced by intensive rearing may be too great for the immature cartilage to bear.

MeSH Terms
Age Factors Agriculture Animal Nutritional Physiological Phenomena Animals Cartilage, Articular/analysis Chromatography Glycosaminoglycans/analysis Hexosamines/analysis Hexoses/analysis Hindlimb Joint Diseases/veterinary Pentoses/analysis Polysaccharides Proteins/analysis Swine/growth & development Swine Diseases/metabolism Uronic Acids/analysis
Chemicals
Glycosaminoglycans Hexosamines Hexoses Pentoses Polysaccharides Proteins Uronic Acids
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sĭmůnek Z
Muir H
References (24)
24 references, click to expand
  1. The chondroitin 4-sulfate-protein linkage.
    J Biol Chem. 1966 May 10;241(9):2113-9 PMID: 4287762
  2. Estimation of pentoses and methylpentoses in biopolymers, in particular of fucose and xylose.
    Anal Biochem. 1966 Dec;17(3):495-501 PMID: 5965984
  3. Proteinpolysaccharide complex from bovine nasal cartilage. A comparison of low and high shear extraction procedures.
    J Biol Chem. 1969 Jan 10;244(1):77-87 PMID: 4237578
  4. Specific inhibition of cartilage breakdown.
    Nature. 1969 Apr 19;222(5190):285-6 PMID: 5778401
  5. Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates.
    J Biol Chem. 1969 May 10;244(9):2384-96 PMID: 5783840
  6. The correlation of fixed negative charge with glycosaminoglycan content of human articular cartilage.
    Biochim Biophys Acta. 1969 May 6;177(3):492-500 PMID: 4239606
  7. Locomotory disturbance in pigs.
    Br Vet J. 1969 Jul;125(7):354-65 PMID: 5817823
  8. Studies on protein-polysaccharides from pig laryngeal cartilage. Heterogeneity, fractionation and characterization.
    Biochem J. 1969 Aug;113(5):885-94 PMID: 4241689
  9. Studies on protein-polysaccharides from pig laryngeal cartilage. Extraction and purification.
    Biochem J. 1969 Aug;113(5):879-84 PMID: 4241780
  10. Characterization of protein-polysaccharides of articular cartilage from mature and immature pigs.
    Biochem J. 1969 Oct;114(4):871-6 PMID: 4241960
  11. The distribution of collagen in human articular cartilage with some of its physiological implications.
    J Bone Joint Surg Br. 1970 Aug;52(3):554-63 PMID: 4247851
  12. The characterization of a protein-polysaccharide isolated from Kurloff cells of the guinea pig.
    Biochem J. 1970 Aug;118(5):783-90 PMID: 4248962
  13. Proteoglycans of cartilage: an assessment of their structure.
    Biochim Biophys Acta. 1971 Feb 16;229(2):529-34 PMID: 5102885
  14. Leg weakness in pigs.
    Vet Rec. 1971 Jul 17;89(3):81-5 PMID: 5105211
  15. Heterogeneity of protein-polysaccharides of porcine articular cartilage. The sequential extraction of chondroitin sulphate-proteins with iso-osmotic neutral sodium acetate.
    Biochem J. 1971 Jan;121(2):261-70 PMID: 5117031
  16. Heterogeneity of protein-polysaccharides of porcine articular cartilage. The chondroitin sulphate proteins associaterd with collagen.
    Biochem J. 1971 Aug;123(5):747-55 PMID: 4330908
  17. Cathepsin D. Characteristics of immunoinhibition and the confirmation of a role in cartilage breakdown.
    Biochem J. 1971 Jun;123(1):1-13 PMID: 4256870
  18. Biosynthesis of proteoglycans in cartilage slices. Fractionation by gel chromatography and equilibrium density-gradient centrifugation.
    Biochem J. 1972 Feb;126(4):791-803 PMID: 4262896
  19. Changes in the protein-polysaccharides of pig articular cartilage during prenatal life, development and old age.
    Biochem J. 1972 Feb;126(3):515-23 PMID: 4263036
  20. Sodium chondroitin sulfate-protein complexes of cartilage. I. Molecular weight and shape.
    Arch Biochem Biophys. 1958 Mar;74(1):158-74 PMID: 13522234
  21. Studies on the mode of action of excess of vitamin A. 3. Release of a bound protease by the action of vitamin A.
    Biochem J. 1961 Jun;79:509-12 PMID: 13722984
  22. The chemistry of connective tissues. 6. The constitution of the chondroitin sulphate-protein complex in cartilage.
    Biochem J. 1961 Apr;79:15-26 PMID: 13733048
  23. Studies on the mode of action of excess of vitamin A. 6. Lysosomal protease and the degradation of cartilage matrix.
    Biochem J. 1963 May;87:403-8 PMID: 13962852
  24. ARTHROPATHY IN PIGS.
    Proc R Soc Med. 1965 May;58:369-70 PMID: 14283894
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1972-11-00
Pages
181-7
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1174314
Subset
IM
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