scholarly journals Ultrastructural localization of collagen types II, IX, and XI in the growth plate of human rib and fetal bovine epiphyseal cartilage: type XI collagen is restricted to thin fibrils.

1995 ◽  
Vol 43 (10) ◽  
pp. 967-979 ◽  
Author(s):  
D R Keene ◽  
J T Oxford ◽  
N P Morris
Keyword(s):  
Growth Plate ◽  
Ultrastructural Localization ◽  
Collagen Fibrils ◽  
Epiphyseal Cartilage ◽  
Collagen Types ◽  
Amino Terminal ◽  
Proliferative Zone ◽  
Human Newborn ◽  
Fetal Bovine ◽  
Type Xi Collagen

The collagen fibrils of hyaline cartilage vary in diameter depending on developmental stage and location within the tissue. In general, growth plates and fetal epiphyseal cartilages contain fibrils with diameters of less than approximately 25 nm, whereas the permanent cartilage of adult tissues contains fibrils of approximately 30-200 nm. The interstitial collagen fibrils of fetal cartilage are complex, having at least three collagen types as integral components. Type XI, a member of the fibrillar collagen class, has been proposed to limit fibril diameter. To test this proposition we sought to determine if Type XI collagen was preferentially associated with fibrils of smaller diameter. We focused our study on human juvenile rib growth plate, which has thin fibrils in the hypertrophic zone, thick fibrils in the resting zone or permanent cartilage, and a mixture of thin and thick fibrils in the proliferative zone. Tissues were examined by immunoelectron microscopy with antipeptide antibodies to the carboxyl telopeptide and to the amino terminal non-triple-helical domains of alpha 1 (XI). These studies showed that (a) both epitopes of Type XI collagen were readily accessible to antibodies at the fibrillar surface, (b) Type XI collagen was associated predominantly with fibrils < 25 nm in diameter, (c) Type XI collagen was not found in thick fibrils even after disruption with chaotropic agents, and (d) collagen Types II and IX were associated with fibrils of all sizes. These studies were extended to human newborn epiphyseal cartilage and to fetal calf cartilage, with the same result.

scholarly journals Ultrastructural localization of the C-propeptide released from type II procollagen in fetal bovine growth plate cartilage.

1996 ◽  
Vol 44 (5) ◽  
pp. 433-443 ◽  
Author(s):  
E R Lee ◽  
C E Smith ◽  
R Poole
Keyword(s):  
Growth Plate ◽  
Ultrastructural Localization ◽  
Collagen Fibrils ◽  
Type Ii ◽  
Guanidinium Hydrochloride ◽  
High Affinity ◽  
Sds Page ◽  
The Matrix ◽  
Fetal Bovine ◽  
Mineralized Matrix

We used immunochemical and immunoelectron gold techniques to determine whether the C-propeptide previously identified in the matrix of endochondral cartilage (CPII) was still a part of the Type 11 procollagen molecule or had been released from it. Guanidinium hydrochloride extraction, followed by SDS-PAGE and Western blotting techniques and immunoelectron localization, revealed that predominantly only the released form (hereafter referred to as released CPII) was detected. The ultrastructural distribution of this CPII was examined with affinity-purified antibodies and with immunogold or immunoperoxidase localization techniques in the presence or absence of embedding resins. These methods yielded similar results. Although no significant amount of this CPII was retained in the matrix after guanidinium hydrochloride extraction, it was present in two recognizable sites under normal conditions, i.e., locally concentrated in a random association with collagen fibrils in the nonmineralized matrix and mainly concentrated in interfibrillar mineralizing sites in the mineralized matrix. These results suggest that the C-propeptide that has been released from Type II procollagen associates with collagen fibrils and then preferentially associates with mineralizing sites when these form in the endochondral cartilage. The significance of this preference for mineral is not known but may have something to do with its high affinity for hydroxyapatite.

Ultrastructural organization of type XI collagen in fetal bovine epiphyseal cartilage

1993 ◽  
Vol 100 (3) ◽  
pp. 231-239 ◽  
Author(s):  
B. Petit ◽  
M. C. Ronzi�re ◽  
D. J. Hartmann ◽  
D. Herbage
Keyword(s):  
Epiphyseal Cartilage ◽  
Ultrastructural Organization ◽  
Fetal Bovine ◽  
Type Xi Collagen

scholarly journals Analisis Pertumbuhan Kartilago Epifisialis Os Tibia Fetus Mencit (Mus musculus L.) Swiss Webster Setelah Induksi Ochratoxin A Selama Periode Organogenesis

2018 ◽  
Vol 4 (1) ◽  
pp. 25-31
Author(s):  
Arum Setiawan ◽  
Mammed Sagi ◽  
Widya Asmara ◽  
Istriyati Istriyati
Keyword(s):  
Key Words ◽  
Ochratoxin A ◽  
Growth Plate ◽  
Mus Musculus ◽  
Epiphyseal Cartilage ◽  
Maturation Zone ◽  
Proliferative Zone ◽  
Key Words Ochratoxin A ◽  
Pregnant Mice ◽  
Tibial Growth Plate

The aims of this study were determined the effects of Ochratoxin A (OTA) on growth of fetus tibia epiphyseal cartilage during organogenesis period. Twenty four pregnant mice were divided randomly into 4 groups of 6. Ochratoxin A was dissolved in sodium bicarbonateand administered orally on seventh to fourteenth days of gestation at dosage of 0.5, 1.0, 1.5 mg/kg bw, respectively. The remaining were used as control. The fetal tibia was taken after the 18 th day of pregnancy. The growth of tibia epiphyseal cartilages were observed histologically using Erlich’s Haematoxylin-Eosin Stain. The result of this study indicated that OTA caused decreased thickness of the rest zone, proliferative zone, maturation zone and calsification zone of the fetus tibial growth plate significantly. Key words: Ochratoxin A, tibia, cartilage, and thickness.

scholarly journals Localization of a dermatan sulfate proteoglycan (DS-PGII) in cartilage and the presence of an immunologically related species in other tissues.

1986 ◽  
Vol 34 (5) ◽  
pp. 619-625 ◽  
Author(s):  
A R Poole ◽  
C Webber ◽  
I Pidoux ◽  
H Choi ◽  
L C Rosenberg
Keyword(s):  
Articular Cartilage ◽  
Growth Plate ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Articular Surface ◽  
Collagen Fibrils ◽  
Superficial Zone ◽  
Condylar Cartilage ◽  
Proliferative Zone ◽  
Dermatan Sulfate Proteoglycan

A monoclonal antibody to a core-protein-related epitope of a small dermatan sulfate-rich proteoglycan (DS-PGII) isolated from adult bovine articular cartilage (22) was used to localize this molecule, or molecules containing this epitope, in bovine articular cartilages, in cartilage growth plate, and in other connective tissues. Using an indirect method employing peroxidase-labeled pig anti-mouse immunoglobulin G, DS-PGII was shown to be present mainly in the superficial zone of adult articular condylar cartilage of the metacarpal-phalangeal joint. In fetal articular and epiphyseal cartilages, the molecule was uniformly distributed throughout the matrix. By approximately 10 months of age it was confined mainly to the superficial and middle zones of articular cartilage and the inter-territorial and pericellular matrix of the deep zone. DS-PGII was not detected in the primary growth plate of the fetus except in the proliferative zone, where it was sometimes present in trace amounts. In contrast, it was present throughout the adjacent matrix of developing epiphyseal cartilage. In the trabeculae of the metaphysis, strong staining for DS-PGII was seen in decalcified osteoid and bone immediately adjacent to osteoblasts. Staining was also observed on collagen fibrils in skin, tendon, and ligament and in the adventitia of the aorta and of smaller arterial vessels in the skin. These observations indicate that DS-PGII and/or molecules containing this epitope are widely distributed in collagenous tissues, where the molecule is intimately associated with collagen fibrils; in adult cartilage this association is limited mainly to the narrow parallel arrays of fibrils which are found in the superficial zone at the articular surface. From its intimate association and other studies, this molecule may play an important role in determining the sizes and tensile properties of collagen fibrils; it may also be involved in the calcification of osteoid but not of cartilage.

Effects of EDTA, Hyaluronidase and Collagenase on Epiphyseal Cartilage Matrix

1968 ◽  
Vol 26 ◽  
pp. 56-57
Author(s):  
H. Clarke Anderson ◽  
Priscilla R. Coulter
Keyword(s):  
Light And Electron Microscopy ◽  
Matrix Vesicles ◽  
Cartilage Matrix ◽  
Collagen Fibrils ◽  
Epiphyseal Cartilage ◽  
Dense Matrix ◽  
Type Iv ◽  
Bovine Testicular Hyaluronidase ◽  
The Matrix ◽  
Testicular Hyaluronidase

Epiphyseal cartilage matrix contains fibrils and particles of at least 5 different types: 1. Banded collagen fibrils, present throughout the matrix, but not seen in the lacunae. 2. Non-periodic fine fibrils <100Å in diameter (Fig. 1), which are most notable in the lacunae, and may represent immature collagen. 3. Electron dense matrix granules (Fig. 1) which are often attached to fine fibrils and collagen fibrils, and probably contain protein-polysaccharide although the possibility of a mineral content has not been excluded. 4. Matrix vesicles (Fig. 2) which show a selective distribution throughout the epiphysis, and may play a role in calcification. 5. Needle-like apatite crystals (Fig. 2).Blocks of formalin-fixed epiphysis from weanling mice were digested with the following agents in 0.1M phosphate buffer: a) 5% ethylenediaminetetraacetate (EDTA) at pH 8.3, b) 0.015% bovine testicular hyaluronidase (Sigma, type IV, 750 units/mg) at pH 5.5, and c) 0.1% collagenase (Worthington, chromatograhically pure, 200 units/mg) at pH 7.4. All digestions were carried out at 37°C overnight. Following digestion tissues were examined by light and electron microscopy to determine changes in the various fibrils and particles of the matrix.

scholarly journals Distribution of slow-cycling cells in epiphyseal cartilage and requirement of β-catenin signaling for their maintenance in growth plate

2014 ◽  
Vol 32 (5) ◽  
pp. 661-668 ◽  
Author(s):  
Maria Elena Candela ◽  
Leslie Cantley ◽  
Rika Yasuaha ◽  
Masahiro Iwamoto ◽  
Maurizio Pacifici ◽  
...  
Keyword(s):  
Growth Plate ◽  
Epiphyseal Cartilage ◽  
Slow Cycling

scholarly journals Characterization of collagen types XII and XIV from fetal bovine cartilage.

1992 ◽  
Vol 267 (28) ◽  
pp. 20093-20099
Author(s):  
S.L. Watt ◽  
G.P. Lunstrum ◽  
A.M. McDonough ◽  
D.R. Keene ◽  
R.E. Burgeson ◽  
...  
Keyword(s):  
Collagen Types ◽  
Fetal Bovine ◽  
Bovine Cartilage

scholarly journals Comparison of collagen types in adult and fetal bovine corneas.

1982 ◽  
Vol 257 (5) ◽  
pp. 2627-2633
Author(s):  
S C Tseng ◽  
D Smuckler ◽  
R Stern
Keyword(s):  
Collagen Types ◽  
Fetal Bovine

An ultrastructural study of mitotic chondrocytes in the proliferative zone of the rat tibial growth plate

1993 ◽  
Vol 175 (1) ◽  
pp. 41-45 ◽  
Author(s):  
S. Shibata ◽  
O. Baba ◽  
M. Niikura ◽  
S. Suzuki ◽  
Y. Yamashita ◽  
...  
Keyword(s):  
Growth Plate ◽  
Ultrastructural Study ◽  
Proliferative Zone ◽  
Tibial Growth Plate

scholarly journals Local Changes to the Distal Femoral Growth Plate Following Injury in Mice

2017 ◽  
Vol 139 (7) ◽  
Author(s):  
Lauren M. Mangano Drenkard ◽  
Meghan E. Kupratis ◽  
Katie Li ◽  
Louis C. Gerstenfeld ◽  
Elise F. Morgan
Keyword(s):  
Growth Plate ◽  
Skeletal Development ◽  
Global Changes ◽  
Mineral Density ◽  
Injury Site ◽  
Hypertrophic Zone ◽  
Proliferative Zone ◽  
Spatial Changes ◽  
Zonal Organization ◽  
Growth Plate Injury

Injury to the growth plate is associated with growth disturbances, most notably premature cessation of growth. The goal of this study was to identify spatial changes in the structure and composition of the growth plate in response to injury to provide a foundation for developing therapies that minimize the consequences for skeletal development. We used contrast-enhanced microcomputed tomography (CECT) and histological analyses of a murine model of growth plate injury to quantify changes in the cartilaginous and osseous tissue of the growth plate. To distinguish between local and global changes, the growth plate was divided into regions of interest near to and far from the injury site. We noted increased thickness and CECT attenuation (a measure correlated with glycosaminoglycan (GAG) content) near the injury, and increased tissue mineral density (TMD) of bone bridges within the injury site, compared to outside the injury site and contralateral growth plates. Furthermore, we noted disruption of the normal zonal organization of the physis. The height of the hypertrophic zone was increased at the injury site, and the relative height of the proliferative zone was decreased across the entire injured growth plate. These results indicate that growth plate injury leads to localized disruption of cellular activity and of endochondral ossification. These local changes in tissue structure and composition may contribute to the observed retardation in femur growth. In particular, the changes in proliferative and hypertrophic zone heights seen following injury may impact growth and could be targeted when developing therapies for growth plate injury.

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