The influence of lysozyme on the appearance of epiphyseal cartilage in organ culture

Kuettner, Klaus E.; Soble, L. W.; Eisenstein, Reuben; Yaeger, James A.

doi:10.1007/bf02279198

Cited by 23 publications

(15 citation statements)

References 21 publications

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“…These authors have also shown that lysozyme can exert profound effects upon the growth of cartilage explants in tissue culture (9,10) and that some of these effects are shared by protamine, another highly cationic substance. They concluded that lysozyme in these tissues was nonlysosomal and primarily extracellular (21,22).…”

Section: Discussionmentioning

confidence: 99%

“…This finding was confirmed by Meyer and Hahnel (7), who noted the "remarkable" lysozyme content of human and guinea pig rib cartilage. Recently, lysozyme has been identified in canine and bovine cartilages (8), and the effect of lysozyme on the growth of cartilage explants in tissue culture has been studied (9,10). The present paper reports quantitative data on the lysozyme content of human cartilage and examines the factors which affect the binding of lysozyme within cartilage and which control release of lysozyme when cartilage is incubated in vitro.…”

Section: Introductionmentioning

confidence: 99%

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Human cartilage lysozyme

Greenwald¹,

Josephson²,

Diamond³

et al. 1972

J. Clin. Invest.

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A B S T R A C T 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 Ag lysozyme per mg of cartilage; for five samples of hyaline cartilage from peripheral joints the range was 0.80-3.03 Ag 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 P-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.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Human cartilage lysozyme

Greenwald¹,

Josephson²,

Diamond³

et al. 1972

J. Clin. Invest.

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“…It has been suggested that this role involves regulation of the reactivity of certain of the anionic polysacchariderich macromolecules of cartilage by the cationic lysozyme molecule (12)(13)(14) .…”

Section: Introductionmentioning

confidence: 99%

Lysozyme in Epiphyseal Cartilage

Kuettner

Eisenstein

Soble

et al. 1971

The Journal of Cell Biology

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The localization of chick embryonic lysozyme was determined by two techniques : by studying the rate of release from the tissue during sequential enzymatic digestion and by immunocytochemistry . Both techniques indicate that, in this tissue, lysozyme is primarily extracellular . Cartilage lysozyme was isolated and partially characterized and found to be identical with egg white lysozyme in its immunologic and enzymatic behavior . In addition, a method for the isolation of large numbers of viable chondrocytes is described .As a further step in the study of the role of lysozyme in cartilage, a series of experiments on intact cartilage and isolated chondrocytes from chick embryos was undertaken to determine its precise distribution as well as to partly characterize it . We here report data from this study indicating that over 99% of chick embryonic cartilage lysozyme is extracellular. In addition, certain properties of cartilage lysozyme, including its immunologic identity with hen's egg white lysozyme, are described as well as a digestion procedure for the isolation of chondrocytes in sufficient numbers for biochemical assays .

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“…During the course of a series of studies which had as their aim the elucidation of the role of lysozyme in cartilage metabolism (1)(2)(3)(4), it was found that, when egg white lysozyme (LYS) was added to organ cultures of ossifying cartilage (cartilage which contains an epiphyseal growth plate) but not nonossifying cartilage (cartilage which does not contain a growth plate), the lysozyme bound to cartilage matrix in specific anatomic sites . In recent years a number of techniques, including staining with lanthanum and bismuth salts (5,6), ruthenium red (7), and colloidal iron (8), as well as the addition of cetylpyridinium chloride to fixatives (9), have been used for the visualization of mucopolysaccharides for electron microscopy .…”

mentioning

confidence: 99%

“…It is known to precipitate cartilage polysaccharides and their parent mucoproteins under physiological conditions (11) and to complex with these compounds when added to organ cultures of preosseous cartilage (2-4) . It does not degrade mammalian polysaccharides (12) and does not significantly affect the growth or calcification of epiphyseal cartilage in organ culture (2)(3)(4) . The technique of short-term organ culture in the presence of added LYS also appeared to offer the advantage that the problem of diffusion of the molecule into the tissue during the process of fixation, which occurs with some other techniques, might be considerably mitigated .…”

mentioning

confidence: 99%

Electron Microscopic Studies of Cartilage Matrix Using Lysozyme as a Vital Stain

Eisenstein

Arsenis

Kuettner

1970

The Journal of Cell Biology

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During the course of a series of studies which had as their aim the elucidation of the role of lysozyme in cartilage metabolism (1-4), it was found that, when egg white lysozyme (LYS) was added to organ cultures of ossifying cartilage (cartilage which contains an epiphyseal growth plate) but not nonossifying cartilage (cartilage which does not contain a growth plate), the lysozyme bound to cartilage matrix in specific anatomic sites . In recent years a number of techniques, including staining with lanthanum and bismuth salts (5, 6), ruthenium red (7), and colloidal iron (8), as well as the addition of cetylpyridinium chloride to fixatives (9), have been used for the visualization of mucopolysaccharides for electron microscopy . The rationale of most of these methods, where they are not completely empirical,

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The influence of lysozyme on the appearance of epiphyseal cartilage in organ culture

Cited by 23 publications

References 21 publications

Human cartilage lysozyme

Human cartilage lysozyme

Lysozyme in Epiphyseal Cartilage

Electron Microscopic Studies of Cartilage Matrix Using Lysozyme as a Vital Stain

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