The Organization and Polymerization of Bone and Dentin Collagens

Veis, Arthur; Spector, Alan; Carmichael, D. J. S.

doi:10.1097/00003086-196909000-00025

Cited by 47 publications

(15 citation statements)

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“…Thus the absence of 0-phosphoserine-and 0-phosphothreonine-containing phosphopeptides from the y-components (and higher-molecular-weight components as well), as well as the a-components of chicken bone collagen, makes it unlikely (at least in the case of chicken bone) that the phosphopeptides are synthesized as components independent and free of collagen, only later to become covalently bonded Vol. 177 to the collagen as a function of maturation (Veis et al, 1969).…”

Section: Analytical Determinationsmentioning

confidence: 99%

“…In addition to increasing the potential number of calcium-binding sites, a complex of carboxy and PO groups would have a greater affinity constant for calcium ions, with the result that the bound calcium ions would be more stable than either a simple calcium-carboxyl or a calcium-phosphate bond alone. Moreover, the complex might also serve to fix the bound calcium ions in a specific and unique stereochemical array, an important point (Glimcher & Krane, 1968;Glimcher, 1976) when one considers the postulated role of the phosphoproteins in facilitating the initiation ofcalcification in mineralized tissues (Glimcher & Krane, 1968;Veis et al, 1969;Weinstock & Leblond, 1973;Glimcher, 1976). In this 1979…”

Section: Analytical Determinationsmentioning

confidence: 99%

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Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Cohen-Solal

Lian

Kossiva

et al. 1979

Biochemical Journal

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Non-collagenous phosphoproteins, almost all of which can be extracted in EDTA at neutral pH in the presence of proteinase inhibitors, are identified in the matrix of chicken bone, and are therefore not covalently bound to collagen. Similarly, all the peptides containing y-carboxyglutamic acid are present in the EDTA extract and none in the insoluble residue, confirming that none is covalently linked to chicken bone collagen. However, organic phosphorus is also found to be present in chicken bone collagen, principally in the a2-chains. Of the total protein-bound organic phosphorus present in chicken bone matrix, approx. 80 % is associated with the non-collagenous proteins and 20 % with collagen. The soluble non-collagenous proteins contain both O-phosphoserine and 0-phosphothreonine and these account for essentially all of their organic phosphorus content. In contrast, collagen contains neither 0-phosphoserine nor 0-phosphothreonine. Indeed, no phosphorylated hydroxy amino acid, phosphoamidated amino acid or phosphorylated sugar could be identified in purified components of collagen, which contain approximately four to five atoms of organic phosphorus per molecule of collagen. Peptides containing organic phosphorus were isolated from partial acid hydrolysates and enzymic digests of purified collagen components, which contain an as-yet-unidentified cationic amino acid. These data, the very high concentrations of glutamic acid in the phosphorylated peptides, and the pH-stability of the organic phosphorus moiety in intact collagen chains strongly suggest that at least part of the organic phosphorus in collagen is present as phosphorylated glutamic acid. This would indicate that the two major chemically different protein fractions in chicken bone matrix that contain organic phosphorus may represent two distinct metabolic pools of organic phosphorus under separate biological control.Phosphoproteins have been identified as part of the non-collagenous components of the organic matrices of mineralized vertebrate tissues such as enamel (Seyer & Glimcher, 1971;Papas et al., 1977;Seyer & Glimcher, 1977a), dentine Veis & Perry, 1967;Butler, 1972;Butler et al., 1972;Veis et al., 1972;Carmichael & Dodd, 1973;Pieri et al., 1975;Menanteau et al., 1977) and bone (Spector & Glimcher, 1972;Shuttleworth & Veis, 1972) [see Leaver et al. (1975b) for a review]. There still exists, however, at least two major points of controversy with regard to bone and dentine: (1) how much, if any, of the phosphorylated protein(s) is covalently bound to the collagen, and (2), if present, Abbreviation used: P,, organic phosphate. * Present address: I.N.S.E.R.M. U12 and U18, Hc6pital des Enfants malades, Paris, France. t To whom requests for reprints should be addressed. Vol. 177 the nature of the organic phosphate moiety covalently bound to the collagen.Although evidence has been presented that none of the phosphoprotein is covalently bound to the collagen of rat dentine (Butler, 1972;Butler et al., 1972Butler et al., , 1976, equally substantia...

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Section: Analytical Determinationsmentioning

confidence: 99%

Section: Analytical Determinationsmentioning

confidence: 99%

Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Cohen-Solal

Lian

Kossiva

et al. 1979

Biochemical Journal

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“…Cornea is an unusual collagenous tissue which has a high mucopolysaccharide content (approximately 4-4.5%, dry weight) compared with that of sclera (1%) [36], skin (0.1-0.5%), dentin (0.4%), or bone (0.24%) [56]. The normal periodicity, however, suggests that the abnormal fiber diameter in this tissue may be due to a failure of fiber growth or maturation.…”

Section: Discussionmentioning

confidence: 99%

Osteogenesis Imperfecta: Morphologic and Biochemical Studies of Connective Tissue

1973

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ExtractIn iliac crest biopsies from 11 patients (ages from 4 to 22 years) with osteogenesis imperfecta, cortical thickness, osteoid width, and number of osteons were less than normal at all ages. Bone surface activity (formation and resorption), measured by quantitative microradiography, was lower than normal in younger patients; the normal pubertal decrease in surface activity was not evident in patients with osteogenesis imperfecta and, consequently, bone surface activity in the older patients was higher than in age-matched normal subjects. The ultrastructure of osteocytes, bone collagen, and scleral collagen did not differ from normal; corneal collagen fibers, however, were approximately half the diameter of normal. Total urinary hydroxyproline excretion, measured in 11 patients, was below normal in all except 2 infants (less than 12 months old). Serum parathyroid hormone levels, measured in nine patients, were normal. Long term treatment with sodium fluoride (two patients) and. treatment with magnesium oxide (three patients) did not alter bone morphology or bone surface activity. SpeculationThe supposition that in osteogenesis imperfecta the connective tissue is characterized by an immature form of collagen was not substantiated by this study. The abnormal fibrillar pattern and paucity of collagen in various connective tissues suggest a qualitative defect, related to collagen maturation, as well as a quantitative deficit in the amount of collagen produced.

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“…be linked to serine in the polypeptide chain [12,14]. Phosphoserine-containing glycoproteins have been obtained from bone [15] and teeth [16].…”

Section: Introductionmentioning

confidence: 99%

Identification of phosphoglycoproteins obtained from rat brain

1976

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The Organization and Polymerization of Bone and Dentin Collagens

Cited by 47 publications

References 0 publications

Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Osteogenesis Imperfecta: Morphologic and Biochemical Studies of Connective Tissue

Identification of phosphoglycoproteins obtained from rat brain

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