scholarly journals QUANTITATIVE APPRECIATION BY COMPARATIVE AUTORADIOGRAPHY OF THE SYNTHESIS AND MAINTENANCE OF SOME ORGANIC CONSTITUENTS OF THE EPIPHYSEAL PLATE OF GROWING RATS, IN RELATION WITH MAGNESIUM DEFICIENCY

1958 ◽  
Vol 6 (2) ◽  
pp. 146-153 ◽  
Author(s):  
LEONARD F. BELANGER
Keyword(s):  
Magnesium Deficiency ◽  
Epiphyseal Plate ◽  
Growing Rats ◽  
Organic Constituents

Expression of Bcl-2 protein in the epiphyseal plate cartilage and trabecular bone of growing rats

1997 ◽  
Vol 108 (1) ◽  
pp. 45-55 ◽  
Author(s):  
Ying Wang ◽  
Renée Toury ◽  
Michelle Hauchecorne ◽  
N. Balmain
Keyword(s):  
Trabecular Bone ◽  
Epiphyseal Plate ◽  
Growing Rats

Effect of Magnesium Deficiency in Growing Rats on Synthesis of Liver Proteins and Serum Albumin

1970 ◽  
Vol 100 (1) ◽  
pp. 123-128 ◽  
Author(s):  
R. Schwartz ◽  
N. A. Woodcock ◽  
J. D. Blakely ◽  
F. L. Wang ◽  
E. A. Khairallah
Keyword(s):  
Serum Albumin ◽  
Magnesium Deficiency ◽  
Growing Rats

Ultrastructural localization of α-parvalbumin in the epiphyseal plate cartilage and bone of growing rats

Bone ◽  
1996 ◽  
Vol 19 (3) ◽  
pp. 245-253 ◽  
Author(s):  
R. Toury ◽  
F. Belqasmi ◽  
M. Hauchecorne ◽  
C.W. Heizmann ◽  
N. Balmain
Keyword(s):  
Ultrastructural Localization ◽  
Epiphyseal Plate ◽  
Growing Rats

Parvalbumin expression in epiphyseal plate cartilage and bone of growing rats

Bone ◽  
1995 ◽  
Vol 17 (6) ◽  
pp. 594
Author(s):  
R. Toury ◽  
F. Belqasmi ◽  
M. Hauchecorne ◽  
D. LeGuellec ◽  
C.W. Heizmann ◽  
...  
Keyword(s):  
Epiphyseal Plate ◽  
Growing Rats

Localization of the Ca2+-binding α-Parvalbumin and its mRNA in epiphyseal plate cartilage and bone of growing rats

Bone ◽  
1995 ◽  
Vol 17 (2) ◽  
pp. 121-130 ◽  
Author(s):  
R. Toury ◽  
F. Belqasmi ◽  
M. Hauchecorne ◽  
D. Leguellec ◽  
C.W. Heizmann ◽  
...  
Keyword(s):  
Epiphyseal Plate ◽  
Growing Rats

Electron Probe Morphological and Chemical Analyses of The Rat Epiphyseal Plate

1968 ◽  
Vol 26 ◽  
pp. 62-63
Author(s):  
Jon C. Hagerty ◽  
A. J. Tousimis
Keyword(s):  
Electron Microscope ◽  
Electron Probe ◽  
Epiphyseal Plate ◽  
Chemical Analyses ◽  
Specific Interest ◽  
X Ray ◽  
Growing Rats ◽  
Epiphyseal Plates ◽  
Scanning Electron

The electron probe affords a means not possible with previous techniques for simultaneous morphological and chemical analyses in situ on biological systems. This method of analysis has been applied to the study of the soluble and insoluble components of the epiphyseal plates of the tibias of young growing rats Sections of both frozen dried and chemically treated, i.e. fixed and embedded, epiphyseal plates have been studied through the use of the scanning electron microscope and X-ray microanalytical capabilities of a modified electron probe. The elements Ca, P, S, K, Na, Cl, and Mg have been of specific interest in these studies on the chemical environment of the zones of the epiphyseal plate from resting to mineralization.

c-Myc and Mxi1 immunoreactivities in the calcifying areas of the epiphyseal-plate cartilage matrix of growing rats

Bone ◽  
1999 ◽  
Vol 24 (6) ◽  
pp. 555-563 ◽  
Author(s):  
R Toury ◽  
Y Wang ◽  
M Hauchecorne ◽  
N Balmain
Keyword(s):  
Cartilage Matrix ◽  
Epiphyseal Plate ◽  
Growing Rats

scholarly journals CARTILAGE RESORPTION IN THE TIBIAL EPIPHYSEAL PLATE OF GROWING RATS

1967 ◽  
Vol 34 (1) ◽  
pp. 275-291 ◽  
Author(s):  
Robert K. Schenk ◽  
David Spiro ◽  
Joseph Wiener
Keyword(s):  
Endothelial Cells ◽  
Surface Membrane ◽  
Active Surface ◽  
Epiphyseal Plate ◽  
Electron Microscopic ◽  
Growing Rats ◽  
Ruffled Border ◽  
Tibial Epiphyseal ◽  
Cytoplasmic Processes ◽  
Epiphyseal Plates

An electron microscopic study of the tibial epiphyseal plates of growing rats reveals that the resorption of unmineralized and mineralized cartilage occurs by two different mechanisms. During resorption the unmineralized transverse cartilaginous walls between chondrocytes are invaded by capillary sprouts. At the resorption zone, numerous cytoplasmic processes derived primarily from the perivascular cells and, to a lesser extent, from the endothelial cells of the sprouts penetrate and appear to lyse the unmineralized transverse cartilaginous walls. Hydrolases released from the degenerating chondrocytes and/or capillary sprouts may also participate in this process. The second resorption mechanism involves the mineralized longitudinal cartilaginous septa. Resorption of these septa is mediated by chondroclasts whose fine structure is identical with that of osteoclasts. The active surface of the chondroclasts has a ruffled border. The surface membrane of the chondroclasts is relatively smooth on either side of the ruffled border and lies in direct apposition with the underlying mineralized cartilage. This observation suggests that the microenvironment in the zone of resorption may be maintained by the neighboring unruffled surfaces of the chondroclasts, which thus seal off and segregate the active portions of these cells.

MICROCHEMICAL ANALYSIS OF HUMAN TIBIAL GROWTH CARTILAGE IN VARIOUS FORMS OF DWARFISM

1972 ◽  
Vol 69 (4) ◽  
pp. 659-688 ◽  
Author(s):  
V. Stanescu ◽  
R. Stanescu ◽  
J. A. Szirmai
Keyword(s):  
Growth Plate ◽  
Chondroitin Sulphate ◽  
Epiphyseal Plate ◽  
Molecular Characteristics ◽  
Growth Disorders ◽  
Normal Children ◽  
Collagen Concentration ◽  
Vitamin D Resistant Rickets ◽  
Pooled Samples ◽  
Tibial Epiphyseal

ABSTRACT Microchemical determinations of glycosaminoglycans and collagen were preformed in isolated histological zones from sections of tibial epiphyseal plate biopsies obtained from children with growth disorders (pituitary dwarfism, congenital myxoedema, Turner's syndrome, Noonan's syndrome, mucopolysaccharidosis type VI, vitamin D resistant rickets and achondroplasia). Alternate sections were used for histochemical localization of glycosaminoglycans and proteins. The values were compared with those found in comparable zones of the growth plate from normal children of the same age. The chondroitin sulphate concentration (% of defatted dry wt.) in the normal epiphyseal plate increased from the resting zone towards the proliferating/hypertrophic zone; collagen exhibited a reverse trend. In some of the pathological biopsies the concentration of chondroitin sulphate was slightly decreased whereas that of collagen was slightly increased. A marked increase in the collagen concentration was found in achondroplasia. The solubility profiles of the cetylpyridinium complexes of the chondroitin sulphate fraction showed three main peaks with slight but characteristic differences in the various zones of the normal cartilage plate. Significant shifts in the proportion of these peaks were observed in several pathological biopsies, indicating possible deviations from the normal molecular characteristics of the chondroitin sulphate. Analysis of the main chondroitin sulphate fraction, obtained from pooled samples of normal tibial growth plate after fractionation on the macroscale, indicated that all three peaks contained both chondroitin-4 sulphate and chondroitin-6 sulphate and that they probably differed in their molecular weight.

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