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Biomedical subjects

M J Glimcher

Publications and source records attributed to M J Glimcher.

At least 37 records · Page 2Linked to original sources
PubMed1977

Evidence for the presence of numerous protein components in immature bovine dental enamel.

The proteins and peptides of immature enamel were extracted from freshly slaughtered bovine embryos in solutions containing protease inhibitors. No detectable differences were noted in the number of components, their overall amino acid composition, or molecular weights from the proteins and peptides extracted 12-16 h postmortem in solutions which contained no protease inhibitors. These data indicate that the large number of components found in developing bovine enamel is not due to proteolysis occurring during their isolation. Significant amounts of protein components having molecular weights greater than approximately 15,000 were not detected. Therefore, if the ameloblasts initially synthesize only a few high molecular weight protein species, the present data imply that in vivo degradation of the high molecular weight enamel proteins occurs very rapidly after their synthesis and precedes the massive loss of protein which accompanies the final stages of enamel mineralization and maturation.

Amelogenesis↗
PubMed1977

Isolation, characterization and partial amino acid sequence of a phosphorylated polypeptide (E4) from bovine embryonic dental enamel.

A phosphorylated polypeptide (E4) of molecular weight 5000-6000, has been isolated from bovine embryonic enamel by Bio-Gel P-10 gel filtration and DE-52 ion-exchange chromatography. The peptide contains three serine residues all of which are phosphorylated. All three O-phosphoserine residues are in glutamic acid-O-phosphoserine-tyrosine sequences that are distributed relatively evenly along the polypeptide chain. Although it was not possible to sequence the entire polypeptide chain directly by automatic peptide sequencing, a partial sequence and peptide map was constructed on the basis of the sequence and composition of peptides derived by cyanogen bromide, trypsin and chymotrypsin digestion. The presence of glutamic acid, tyrosine and leucine adjacent to and near the O-phosphoserine residues may be important in calcium binding and in mineralization.

Amino Acid Sequence↗
PubMed1977

The presence of protein-bound gamma-carboxyglutamic acid in calcium-containing renal calculi.

The amino acid gamma-carboxyglutamic acid (Gla) is found in four blood-clotting proteins, in a bone protein, in kidney protein, and in the protein present in various ectopic calcifications. This paper reports the presence of Gla in the EDTA-soluble, nondialyzable proteins of calcium-containing renal calculi including calcium oxalate, hydroxyapatite, and mixed stores of apatite and struvite (MgNH4PO4). Calculi composed of pure struvite and those composed of only uric acid or cystine do not contain Gla. From calcium oxalate and hydroxyapatite stontes, a protein of about 17,000 daltons was obtained which contained about 40 residues of Gla per 1,000 amino acids. The amino acid composition of this protein had no apparent relationship to the Gla-containing bone protein or to the similarly-sized F1 fragment of prothrombin which contains about 64 residues of Gla per 1,000 amino acid residues. The Gla-rich protein in calcium-containing renal stones thus may be a different Gla-containing protein. These data as well as other studies demonstrating the presence of Gla in pathologically calcified tissues not normally containing Gla suggest that the Gla-containing proteins may be of considerable pathophysiological significance.

Adult↗
PubMed1977

Histologic and biochemical identification and characterization of an elastin in cartilage.

Histochemical and chemical techniques have been used to identify, isolate and characterize elastin from certain bovine cartilages. The results strongly suggest that in addition to fibroblasts and smooth muscle cells, chondroblasts also synthesize elastin. Some of the possible functions of elastin in elastic cartilages are discussed and the possiblity of a new type of elastin perhaps unique to cartilage is suggested.

Amino Acids↗
PubMed1977

Organization and cellular biology of the perichondrial ossification groove of ranvier: a morphological study in rabbits.

The perichondrial ossification groove of Ranvier, a circumferential groove in the periphery of the epiphyseal cartilage, was studied in rabbits whose ages ranged from one week to eight months using light and electron microscopy, autoradiography after labeling with 3H-thymidine, 3H-proline, and 3H-glucosamine, and histochemical staining for proteoglycans and alkaline phosphatase. By these methods, three groups of cells were identified within the groove: 1. A group of densely packed cells deep in the groove, which are the progenitor cells for the osteoblasts that form the bone bark, a cuff of bone surrounding the epiphyseal growth-plate region and the adjacent part of the metaphysis. 2. A group of more widely dispersed, relatively undifferentiated mesenchymal cells and fibroblasts, some of which are chondroblast precursors that probably contribute to appositional chondrogenesis and growth in width of the epiphyseal cartilage. 3. Fibroblasts and fibrocytes among sheets of highly oriented and organized collagen fibers which form a fibrous layer that is continuous with the outer fibrous layer of the periosteum and with the perichondrium. This layer also sends fibers into the epiphyseal cartilage and anchors the periosteum firmly to the epiphyses as bone growth proceeds.

Animals↗
PubMed1976

Changes in the hexosamine content and swelling ratio of articular cartilage as functions of depth from the surface.

The hexasamine content and swelling ratio of adult bovine articular cartilage were determined as functions of depth. Progressing from the surface downward, the hexosamine content increased rapidly to a depth equivalent to approximately 30 to 35 per cent of the total thickness of the uncalcified portion of the tissue, and thereafter decreased at a less rapid rate. The swelling ratio was relatively constant throughtout the first quarter of the tissue but diminished thereafter. At depths below 35 per cent, the curve for the decrease in swelling ratio with depth was similar in form to that for the decrease in hexosamine content. Considering the factors that determine the swelling ratio of polyelectrolyte gels, it is proposed that progressing down from the surface, the interaction between the macromolecular components of the tissue is increased to a depth equivalent to about one-third of the total thickness of the cartilage.

Animals↗
PubMed1975

Studies on the interaction between heparin and mouse bone collagenase.

Mouse bone collagenase was found to be tightly bound to a heparin-substituted gel at low ionic strength. The bond was reversible, however, and the collagenase could be elutted at high ionic strength. In addition to providing a method for purifying the enzyme with high yield, the results suggest that the strong ionic bond between heparin and collagenase may partially explain the mechanism wherein heparin enhances the activity of mouse bone collagenase.

Animals↗
PubMed1975

In vitro wear of articular cartilage.

Seeking a reliable chemical index of the wear of articular cartilage during in vitro experiments, the contents of hydroxyproline, hexosamine, and the amino acid composition of adult bovine articular cartilage were determined as functions of depth from the surface. The hydroxyproline content, expressed as per cent of dry weight of tissue, was constant throughout the thickness of the tissue except in a surface region approximately twenty-five micrometers thick; the hexosamine content in this region was less than in the interior of the tissue; the collagen content was higher and the amino acid composition was less like that of pure collagen here than in the interior, indicating that the content of noncollagenous protein in the superficial layer of cartilage was greater than that in the interior. It was also evident that adult bovine articular cartilage contains significant amounts of collagen with a low hydroxylysine content, presumably Type I as well as Type II. Since the content of hydroxyproline is constant throughout the cartilage and the collagen and proteoglycan constituents of the intact tissue are relatively insoluble, the hydroxyproline content of the lubricant and the wear debris can be used to measure the extent of wear of articular cartilage during in vitro experiments. However, approximately 10 per cent of the hydroxyproline and 50 to 60 per cent of the glycosaminoglycans of the wear debris are dissolved in the lubricating fluid. Therefore, both the lubricant (solvent) and the solid wear debris must be analyzed to determine the amount of cartilage wear.

Amino Acids↗