Studies on the protein-bound chondroitin sulphate of bovine cortical bone

Herring, G. M.

doi:10.1042/bj1070041

Cited by 84 publications

(30 citation statements)

References 31 publications

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“…There have been indications that a spectrum of bone proteins exists, but to date, very few of them have been purified or characterized [1][2][3][4][5][6][7][8][9][10]. Four plasma proteins, albumin, a-l-acid glycoprorein, a-2-HS glycoprotein, and IgE, have been shown to be specifically concentrated in bone from plasma, although the mechanism of this concentration is unclear [10][11][12][13].…”

Section: Discussionmentioning

confidence: 97%

Identification of the noncollagenous proteins of bovine bone by two-dimensional gel electrophoresis

et al. 1984

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We have characterized the noncollagenous proteins of bovine bone using two high-resolution gel electrophoretic techniques. Proteins were extracted from bone tissue by extended dialysis against 0.5 M EDTA. In some cases, a preextraction was done in guanidine HCl. Bovine plasma was also examined to identify the proteins in bone that might also be present in blood. We have scored 160 major, reproducible spots on our standard preparation bone map. These comprise about 40 individual protein groups. There are many more minor spots present which puts the total number present over 200. Of these groups, 15 are not present on plasma maps. Bone proteins identified in this way include actin, bone Gla-protein, and osteonectin. The remainder are unknown. Bone Gla-protein is present in bovine bone in four isoelectric forms, pI = 3.95-4.50. Electroblotting analysis of EDTA and guanidine HCl extracted material failed to reveal any higher molecular weight immunologically reactive species. The plasma proteins found in bone include, but are not limited to albumin, apo A-I lipoprotein, IgG, IgM, transferrin, alpha-2-HS-glycoprotein, and hemoglobin. Extraction with guanidine HCl plus EDTA significantly enriches the yield for the nonplasma proteins but does not appear to extract any additional bone proteins.

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Section: Discussionmentioning

confidence: 97%

Identification of the noncollagenous proteins of bovine bone by two-dimensional gel electrophoresis

et al. 1984

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“…The glycosaminoglycan composition of bone has been studied in a variety of different species, including dog, ox, sheep, and man, and chondroitin sulfate was found to be the predominant glycosaminoglycan in these species (Herring, 1968;Hjertquist and Vejlens, 1968;Vejlens, 1971;Dickson, 1974;Engfeldt and Hjerpe, 1976). Despite this apparent uniformity, rabbit bone differs in that it contains a significant amount of keratan sulfate in addition to chondroitin sulfate (Masubuchi et al, 1975;Diamond et al, 1982;Fisher et al, 1987).…”

Section: Introductionmentioning

confidence: 91%

A Biochemical and Immunohistochemical Study of the Proteoglycans of Alveolar Bone

Bartold

1990

J Dent Res

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The purpose of this investigation was to study the proteoglycans in alveolar bone of three animal species. Alveolar bone was obtained from humans, pigs, and rabbits. Portions were fixed, sectioned, and stained with monoclonal antibodies against keratan sulfate and chondroitin sulfate. In other samples, biochemical analyses were performed. After removal of the organic matrix by 4 mol/L guanidinium HCl extraction in the presence of proteinase inhibitors, proteoglycans in the mineralized matrix were extracted with 4 mol/L guanidinium HCl/0.5 mol/L EDTA/proteinase inhibitors, and characterized on the basis of their glycosaminoglycan content (cellulose acetate membrane electrophoresis), charge (DEAE-Sephacel and hydroxylapatite chromatography), size (Sepharose CL-6B chromatography and agarose/polyacrylamide gel electrophoresis), and amino acid content. The results indicated that keratan sulfate could be detected immunohistochemically and biochemically in rabbit bone only. The predominant glycosaminoglycan in pig and human alveolar bone was chondroitin sulfate, although some hyaluronate, dermatan sulfate, and heparan sulfate were also detected. The proteoglycans were found to be slightly smaller than gingival proteoglycans, but similar to those in cementum, dentin, and other bones. In addition to intact proteoglycans, some free glycosaminoglycan chains were also extracted from the mineralized matrix. Amino acid analyses showed some subtle differences between alveolar bone proteoglycan and those of the soft tissues of the periodontium.

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“…EDTA extraction was carried out according to the basic method of Herring [8]. with the following modifications: dia lysis tubes were of 3.500 cutoff: the following protease inhibitors were used: 5 mM benzamidine/HCl.…”

Section: Methodsmentioning

confidence: 99%

Biochemical Anatomy of Human Bone: Comparative Study of Compact and Spongy Bone in Femur, Rib and Iliac Crest

Mbuyi-Muamba¹,

Dequeker²

1987

Cells Tissues Organs

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Using EDTA extraction procedure, compact and spongy bone from human femur, rib and iliac crest were compared in terms of their content in collagen, sialoprotein, proteoglycan and carbohydrate. The bone matrix sizes displayed significant variations, the femur having the smallest size and iliac crest the largest one. No significant difference in the matrix size has been found between the spongy and compact bone. The EDTA extractability of the spongy bone was higher than that of the compact bone, with femur showing the lowest extractability. The collagen content of the 3 bones studied was similar although the femur had slightly lower values. The sialic and uronic acids and hexose contents were higher in the femur than in the rib and iliac crest. The collagen/hexose, collagen/sialic acid and collagen/uronic acid ratios in the bone matrix were highest in the iliac crest and lowest in the femur, suggesting that alterations in the amounts of bone matrix can affect the mechanical properties of different parts of the bony skeleton and vice versa.

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Studies on the protein-bound chondroitin sulphate of bovine cortical bone

Cited by 84 publications

References 31 publications

Identification of the noncollagenous proteins of bovine bone by two-dimensional gel electrophoresis

Identification of the noncollagenous proteins of bovine bone by two-dimensional gel electrophoresis

A Biochemical and Immunohistochemical Study of the Proteoglycans of Alveolar Bone

Biochemical Anatomy of Human Bone: Comparative Study of Compact and Spongy Bone in Femur, Rib and Iliac Crest

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