Skip to main content
NCBI home page
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1972 Sep;51(9):2264–2270. doi: 10.1172/JCI107035

Human cartilage lysozyme

Robert A Greenwald 1, Alan S Josephson 1, Herbert S Diamond 1, Ambrose Tsang 1
PMCID: PMC292390  PMID: 4639012

Abstract

The lysozyme content of human cartilage was measured by incubation of lyophilized, powdered cartilage in a variety of buffers and salt solutions, and the factors controlling the binding of lysozyme within cartilage were studied. Lysozyme was extracted from hyaline cartilage by buffers of pH greater than 9.0 by solutions 1 M in monovalent cations, and by solutions 0.12-0.40 M in divalent cations. The ability of cations to extract lysozyme from cartilage agreed with their known affinities for binding to chondroitin sulfate. The total extractable lysozyme content of five samples of human costal cartilage ranged from 1.45 to 3.36 μg lysozyme per mg of cartilage; for five samples of hyaline cartilage from peripheral joints the range was 0.80-3.03 μg lysozyme per mg of cartilage. Cartilage incubated in excess exogenous lysozyme could bind 0.053 equivalents of lysozyme per equivalent of chondroitin sulfate. Fibrocartilage and synovium from knee joints yielded no detectable lysozyme, despite the fact that synovium, a tissue rich in lysosomes, contained measurable quantities of β-glucuronidase. Lysozyme extraction from cartilage was not augmented by incubation with streptolysin S. When incubation was carried out with mild extraction techniques, lysozyme extraction from cartilage tended to parallel uronic acid release, both as a function of time and from one specimen to another. The active material as lysozyme. Lysozyme occurs in human hyaline cartilage as a counterion to polyanionic glycosaminoglycans. Carextracted from cartilage met five criteria for identification tilage lysozyme appears to be extracellular and nonlysosomal. Degradation of cartilage may contribute to the increased serum and synovial fluid lysozyme levels often present in patients with rheumatoid arthritis.

Full text

PDF
2264

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BALL J., CHAPMAN J. A., MUIRDEN K. D. THE UPTAKE OF IRON IN RABBIT SYNOVIAL TISSUE FOLLOWING INTRA-ARTICULAR INJECTION OF IRON DEXTRAN. A LIGHT AND ELECTRON MICROSCOPE STUDY. J Cell Biol. 1964 Aug;22:351–364. doi: 10.1083/jcb.22.2.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARLAND P., NOVIKOFF A. B., HAMERMAN D. FINE STRUCTURE AND CYTOCHEMISTRY OF THE RHEUMATOID SYNOVIAL MEMBRANE, WITH SPECIAL REFERENCE TO LYSOSOMES. Am J Pathol. 1964 May;44:853–866. [PMC free article] [PubMed] [Google Scholar]
  3. Bonavida B., Sapse A. T., Sercarz E. E. Human tear lysozyme. I. Purification, physicochemical, and immunochemical characterization. J Lab Clin Med. 1967 Dec;70(6):951–962. [PubMed] [Google Scholar]
  4. COHN Z. A., HIRSCH J. G. The isolation and properties of the specific cytoplasmic granules of rabbit polymorphonuclear leucocytes. J Exp Med. 1960 Dec 1;112:983–1004. doi: 10.1084/jem.112.6.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Davies R. C., Neuberger A., Wilson B. M. The dependence of lysozyme activity on pH and ionic strength. Biochim Biophys Acta. 1969 Apr 22;178(2):294–305. doi: 10.1016/0005-2744(69)90397-0. [DOI] [PubMed] [Google Scholar]
  6. Eisenstein R., Kuettner K. C. An ultrastructural organization of cartilage matrix as revealed through the use of lysozyme. Calcif Tissue Res. 1970;(Suppl):137–138. doi: 10.1007/BF02152393. [DOI] [PubMed] [Google Scholar]
  7. Hamerman D. Cartilage changes in the rheumatoid joint. Clin Orthop Relat Res. 1969 May-Jun;64:91–97. [PubMed] [Google Scholar]
  8. JOLLES P. RECENT DEVELOPMENTS IN THE STUDY OF LYSOZYMES. Angew Chem Int Ed Engl. 1964 Jan;3:28–36. doi: 10.1002/anie.196400281. [DOI] [PubMed] [Google Scholar]
  9. Kuettner K. E., Guenther H. L., Ray R. D., Schumacher G. F. Lysozyme in preosseous cartilage. Calcif Tissue Res. 1968 Mar 27;1(4):298–305. doi: 10.1007/BF02008101. [DOI] [PubMed] [Google Scholar]
  10. Kuettner K. E., Soble L. W., Eisenstein R., Yaeger J. A. The influence of lysozyme on the appearance of epiphyseal cartilage in organ culture. Calcif Tissue Res. 1968 Jul 15;2(1):93–105. doi: 10.1007/BF02279198. [DOI] [PubMed] [Google Scholar]
  11. Kuettner K. E., Soble L. W., Guenther H. L., Croxen R. L., Eisenstein R. Lysozyme in epiphyseal cartilage. I. The nature of the morphologic response of cartilage in culture to exogenous lysozym. Calcif Tissue Res. 1970;5(1):56–63. doi: 10.1007/BF02017534. [DOI] [PubMed] [Google Scholar]
  12. Kuettner K. E., Sorgente N., Arsenis C., Eisenstein R. Cartilage lysozyme, an extracellular basic (cationic) protein. Isr J Med Sci. 1971 Mar;7(3):407–409. [PubMed] [Google Scholar]
  13. Pruzanski W., Saito S., Ogryzlo M. A. The significance of lysozyme (muramidase) in rheumatoid arthritis. I. Levels in serum and synovial fluid. Arthritis Rheum. 1970 Jul-Aug;13(4):389–399. doi: 10.1002/art.1780130405. [DOI] [PubMed] [Google Scholar]
  14. WEISSMANN G., KEISER H., BERNHEIMER A. W. STUDIES ON LYSOSOMES. III. THE EFFECTS OF STREPTOLYSINS O AND S ON THE RELEASE OF ACID HYDROLASES FROM A GRANULAR FRACTION OF RABBIT LIVER. J Exp Med. 1963 Aug 1;118:205–222. doi: 10.1084/jem.118.2.205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Weissmann G. Lysosome. N Engl J Med. 1965 Nov 11;273(20):1084–contd. doi: 10.1056/NEJM196511112732006. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES