Studies of the proteins, peptides and free amino acids of mature bovine enamel

Glimcher, M J; Levine, Philip T.

doi:10.1042/bj0980742

Cited by 55 publications

(24 citation statements)

References 14 publications

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“…Light microscopic radioautographs of ameloblasts treated with LACA (E) (1-3), control odontoblasts (C) (4-9), and LACAtreated odontoblasts (E) (10)(11)(12). It should be noted that silver grains are concentrated over the supranuclear cytoplasm of LACAtreated ameloblasts at 20 min but begin to appear over Tomes' processes (TP) at 30 min, and are almost completely located over enamel matrix (EM) at 2 h. A similar pattern is observed in control odontoblasts (4)(5)(6)(7)(8)(9). Note early concentration of grains over the supranuclear cytoplasm at 10 min (5) and Golgi complex (G) (6 and 7) at 20 and 30 min.…”

Section: Itsupporting

confidence: 65%

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Comparative radioautographic study of the effects of L-azetidine-2-carboxylic acid on matrix secretion and golgi of the mouse incisor

Cho

Garant

1984

Calcif Tissue Int

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The effect of a proline analog, L-azetidine-2-carboxylic acid (LACA), on protein matrix secretion by odontoblasts and ameloblasts was compared by light and electron microscopic radioautography after injection of 3H-glycine in young mice. LACA inhibited the secretion of dentin matrix with consequent accumulation of 3H-glycine labeled procollagen in the cisternae of the rough endoplasmic reticulum. In contrast, LACA had no apparent effect on ameloblasts as enamel matrix continued to be packaged in the Golgi apparatus and secreted from Tomes' process within 30 min after injection of the radioprecursor. Electron microscopy revealed that LACA did not cause any change in ameloblast ultrastructure but produced a marked alteration of the odontoblast Golgi complex. All odontoblast Golgi saccules and collagen secretion granules disappeared within 2 h after LACA administration. Odontoblast Golgi cisternae, however, appeared not to be affected. These observations confirm previous studies conducted in this laboratory showing that Golgi saccules in collagen-secreting cells are the initial staging areas for the formation of secretory granules. These results also indicate that a close correlation exists between form and function in the Golgi apparatus of collagen-secreting cells.

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Section: Itsupporting

confidence: 65%

“…The amino acid composition of the EDTA--insoluble components of the organic matrix of bovine enamel--contains 23% proline and 39% glycine [9].…”

mentioning

confidence: 99%

Comparative radioautographic study of the effects of L-azetidine-2-carboxylic acid on matrix secretion and golgi of the mouse incisor

Cho

Garant

1984

Calcif Tissue Int

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“…The proposed technique is superior to the original superficial enamel etching technique described by Glimcher and Levine (1966), which also used EDTA and HCl to extract bovine mature enamel proteins. In this classical study, large amounts of teeth were used as starting material (2000e5000 teeth), and the time needed to dissolve the teeth was long (days).…”

Section: Resultsmentioning

confidence: 98%

“…However, the starting material was large (seven thousand teeth!) and the results reported no specific peptide sequences, but rather the most abundant amino acids found (Glimcher and Levine, 1966).…”

Section: Introductionmentioning

confidence: 86%

New techniques for the recovery of small amounts of mature enamel proteins

Porto

Laure

Sousa

et al. 2011

Journal of Archaeological Science

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“…The hydrolysates were either analysed directly or after precipitation of most of the calcium and phosphorus by adjusting the pH (Glimcher & Levine, 1966 Chen et al (1956). In some instances a small correction for the phospholipidphosphorus content was necessary, owing to the presence of a small amount of O-phosphoserine and O-phosphothreonine in the phospholipid extract.…”

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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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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Studies of the proteins, peptides and free amino acids of mature bovine enamel

Cited by 55 publications

References 14 publications

Comparative radioautographic study of the effects of L-azetidine-2-carboxylic acid on matrix secretion and golgi of the mouse incisor

Comparative radioautographic study of the effects of L-azetidine-2-carboxylic acid on matrix secretion and golgi of the mouse incisor

New techniques for the recovery of small amounts of mature enamel proteins

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

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