29 Protein???polysaccharides of Cartilage and Bone in Health and Disease

Campo, Robert D.

doi:10.1097/00003086-197001000-00030

Cited by 57 publications

(12 citation statements)

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“…Nevertheless, this does not mean that PGs containing C4-S and/or DS, C6-S and KS are intact, since the possibility of proteolysis of the PG core protein or a change in molecular conformation cannot be ruled out. This interpretation is consistent with previous results, indicating that some cartilage PGs may constitute the nucleating site after their degradation with enzymes (Campo, 1970). Therefore, it is probable that the concentration of reactive macromolecules in bone nodules occurs at sites of initial mineralization.…”

Section: Resultssupporting

confidence: 93%

Immunoelectron microscopic studies of glycosaminoglycans in the metaphyseal bone trabeculae of growing rats

et al. 1992

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The types and distribution of glycosaminoglycans (GAGs) were studied immunocytochemically in osteoid, mineralized bone matrix, and cartilage matrix of growing rat metaphyseal bone after aldehyde fixation and EDTA demineralization, using four monoclonal antibodies (mAbs 1-B-5, 2-B-6, 3-B-3 and 5-D-4). These mAbs specifically recognize epitopes in non-sulphated chondroitin (C0-S); chondroitin 4-sulphate (C4-S) and dermatan sulphate (DS); chondroitin 6-sulphate (C6-S) and C0-S; and keratan sulphate (KS) respectively. In osteoid, all mAbs except 1-B-5 weakly stained matrix material on and between collagen fibrils, and moderately stained organic material corresponding to bone nodules, which are known sites of mineralization. However, the staining of osteoid abruptly decreased at the mineralization front; weak staining was confined mostly to the organic material of bone nodules in mineralized bone matrix, with very weak or no staining of the rest of the bone matrix. This staining progressively decreased toward the mineralized cartilage matrix and became negative. The mineralized cartilage matrix and lamina limitans reacted strongly with all mAbs except 5-D-4. These results indicate that osteoid contains sulphated proteoglycans containing C4-S and/or DS, C6-S and KS, and subsequent bone matrix mineralization appears to require accumulation of these macromolecules within bone nodules and eventual loss of these substances for complete mineralization, whereas proteoglycans containing C0-S, C4-S and/or DS, and C6-S still exist in mineralized cartilage matrix and lamina limitans.

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Section: Resultssupporting

confidence: 93%

Immunoelectron microscopic studies of glycosaminoglycans in the metaphyseal bone trabeculae of growing rats

et al. 1992

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“…These observations support the hypotheses that proteoglycans sequester calcium but prevent its precipitation in situ; calcium is then released for deposition at calcifying sites when proteoglycans are removed by lysosomal enzymes [7]. Alternatively, some degraded proteoglycans may constitute the nucleating site for calcification [6,8].…”

Section: Discussionsupporting

confidence: 77%

Ultrastructural cytochemistry of complex carbohydrates in osteoblasts, osteoid, and bone matrix

et al. 1983

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Glycosaminoglycans (GAGs) and glycoproteins are essential components for osteogenesis. We have examined rat osteoblasts, osteoid, transitional zone, and fully calcified bone matrix, utilizing Spicer's high-iron diaminethiocarbohydrazide-silver protein (HID-TCH-SP) method for sulfated glycoconjugates and Thiéry's periodate-TCH-SP (PA-TCH-SP) method for vicinal glycol-containing glycoconjugates. HID-TCH-SP stained cytoplasmic granules of osteoblasts. Stain deposits in the extracellular matrix were observed in decreasing amounts in osteoid, the transitional zone, and fully calcified bone matrix. Enzyme digestion with testicular hyaluronidase removed most HID-TCH-SP stain deposits. PA-TCH-SP staining was observed with increasing intensity in rough endoplasmic reticulum, Golgi saccules, and cytoplasmic granules. Collagen fibrils in osteoid were weakly stained with PA-TCH-SP, and their staining appeared even weaker in fully calcified bone matrix. In contrast, collagen fibrils in calcified cartilage stained intensely with the PA-TCH-SP method. Focal circular profiles (0.1-0.5 mumol in diameter), which lacked collagen fibrils but reacted moderately with PA-TCH-SP, were frequently seen in the transitional zone and fully calcified bone matrix, but were only occasionally present in osteoid. The presence of testicular hyaluronidase-resistant GAG and acid phosphatase in these focal areas suggests that they represent sites of GAG degradation. The eventual loss of HID-TCH-SP staining in the bone matrix suggests that removal of sulfated glycoconjugates may be a requisite for expansion of initial calcification sites and/or complete calcification.

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“…Mature cartilage is relatively avascular tissue that contains very few cells and consists almost entirely of an extracellular matrix composed of water, collagen, and protein polysaccharide complexes (13) . It has not been established whether the avascularity of cartilage is due to a physical or chemical block (14) .…”

Section: Discussionmentioning

confidence: 99%

Inhibition of tumor angiogenesis mediated by cartilage.

Brem¹,

Folkman²

1975

The Journal of Experimental Medicine

312

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Capillary proliferation induced by tumor is shown to be inhibited by neonatal scapular cartilage. Using the rabbit cornea as an assay, the cartilage implant decreased the rate of capillary growth, induced by tumor, by an average of 75%. Vascularization was prevented completely in 28% of tumors. The inhibitory effect of small cartilage implants operates over distances of up to 2.0 mm and displays a gradient from the cartilage source. The experiments suggest that the cartilage inhibitor does not antagonize tumor angiogenesis factor, but appears to inhibit capillary proliferation directly. The inhibitory material does not elicit an inflammatory response in either the rabbit cornea or in the chick chorioallantoic membrane. Thus with further purification, it may prove useful as a means of maintining tumor dormancy by "antiangiogenesis."

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29 Protein???polysaccharides of Cartilage and Bone in Health and Disease

Cited by 57 publications

References 0 publications

Immunoelectron microscopic studies of glycosaminoglycans in the metaphyseal bone trabeculae of growing rats

Immunoelectron microscopic studies of glycosaminoglycans in the metaphyseal bone trabeculae of growing rats

Ultrastructural cytochemistry of complex carbohydrates in osteoblasts, osteoid, and bone matrix

Inhibition of tumor angiogenesis mediated by cartilage.

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