scholarly journals Extraction and characterization of the tissue forms of collagen types II and IX from bovine vitreous

1994 ◽  
Vol 299 (2) ◽  
pp. 497-505 ◽  
Author(s):  
P N Bishop ◽  
M V Crossman ◽  
D McLeod ◽  
S Ayad
Keyword(s):  
Chondroitin Sulphate ◽  
Minor Component ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Collagen Types ◽  
The Matrix ◽  
Type V ◽  
Chain Lengths ◽  
First Time

We report for the first time that, after centrifugation of adult bovine vitreous, the hyaluronan-rich supernatant contains collagens which can be isolated in their intact forms by precipitation with 4.5 M NaCl. This precipitate constituted approx. 4% of the total vitreous collagen and comprised collagen types IX and II (in the approximate ratio of 4:1) with negligible amounts of type-V/XI collagen. Type-II collagen was present partly in a pro-alpha 1(II) form, suggesting that there is active synthesis of type-II collagen into the matrix of adult bovine vitreous. Type-IX collagen was purified (2-2.5 mg/l of vitreous) and its glycosaminoglycan chain composition was analysed. Bovine vitreous type-IX collagen always possessed a glycosaminoglycan chain of comparatively low M(r) that was predominantly 4-sulphated, with chondroitin 6-sulphate representing a more minor component. By contrast, chick vitreous has been shown to contain type-IX collagen which always possesses a high-M(r) chondroitin sulphate chain that is predominantly 6-sulphated. The functional significance of these different glycosaminoglycan chain lengths and sulphation patterns is discussed.

Independent deposition of collagen types II and IX at epithelial-mesenchymal interfaces

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 85-95 ◽  
Author(s):  
J.M. Fitch ◽  
A. Mentzer ◽  
R. Mayne ◽  
T.F. Linsenmayer
Keyword(s):  
Collagen Type ◽  
Immunohistochemical Study ◽  
Type Ii Collagen ◽  
The Other ◽  
Extracellular Matrices ◽  
Type Ii ◽  
Collagen Deposition ◽  
Collagen Types ◽  
Hind Limbs ◽  
The Matrix

Previous studies have demonstrated the presence of type II collagen (in mature chickens predominantly a ‘cartilage-specific’ collagen) in a variety of embryonic extracellular matrices that separate epithelia from mesenchyme. In an immunohistochemical study using collagen type-specific monoclonal antibodies, we asked whether type IX collagen, another ‘cartilage-specific’ collagen, is coexpressed along with type II at such interfaces. We confirmed that, in the matrix underlying a variety of cranial ectodermal derivatives and along the ventrolateral surfaces of neuroepithelia, type II collagen is codistributed with collagen types I and IV. Type IX collagen, however, was undetectable at those sites. We observed immunoreactivity for type IX collagen only within the notochordal sheath, where it first appeared at a later stage than did collagen types I and II. We also observed type II collagen (without type IX) beneath the dorsolateral ectoderm at stage 16; this correlates with the period during which limb ectoderm has been reported to induce the mesoderm to become chondrogenic. Finally, in older hind limbs we observed subepithelial type II collagen that was not associated with subsequent chondrogenesis, but appeared to parallel the formation of feathers and scales in the developing limb. These observations suggest that the deposition of collagen types II and IX into interfacial matrices is regulated independently, and that induction of mesenchymal chondrogenesis by such matrices does not involve type IX collagen. Subepithelial type IX collagen deposition, on the other hand, correlates with the assembly of a thick multilaminar fibrillar matrix, as present in the notochordal sheath and, as shown previously, in the corneal primary stroma.

scholarly journals Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites

1996 ◽  
Vol 314 (1) ◽  
pp. 327-332 ◽  
Author(s):  
Mohammad DIAB ◽  
Jiann-Jiu WU ◽  
David R. EYRE
Keyword(s):  
Minor Component ◽  
Type Ii Collagen ◽  
Cross Linking ◽  
Type Ii ◽  
Human Cartilage ◽  
The Matrix ◽  
Collagen Molecules ◽  
Cross Links ◽  
A Minor ◽  
Bovine Cartilage

Type IX collagen, a quantitatively minor collagenous component of cartilage, is known to be associated with and covalently cross-linked to type II collagen fibrils in chick and bovine cartilage. Type IX collagen molecules have also been shown to form covalent cross-links with each other in bovine cartilage. In the present study we demonstrate by structural analysis and location of cross-linking sites that, in human cartilage, type IX collagen is covalently cross-linked to type II collagen and to other molecules of type IX collagen. We also present evidence that, if the proteoglycan form of type IX collagen is present in human cartilage, it can only be a minor component of the matrix, similar to findings with bovine cartilage.

scholarly journals A new look at vitreous-humour collagen

1984 ◽  
Vol 218 (3) ◽  
pp. 835-840 ◽  
Author(s):  
S Ayad ◽  
J B Weiss
Keyword(s):  
Nasal Septum ◽  
Type Ii Collagen ◽  
Vitreous Humour ◽  
Molar Ratio ◽  
Type Ii ◽  
Collagen Types ◽  
The Difference ◽  
Type V ◽  
Phosphate Buffered Saline ◽  
And Cartilage

The collagens of bovine vitreous-humour and nasal-septum cartilage have been extracted, fractionated and compared. Both tissues show the same heterogeneity of collagen types, consisting of type II, 1 alpha, 2 alpha, 3 alpha and C-PS collagens. The type II collagen of the vitreous humour was significantly more hydroxylated both in the lysine and proline residues than was that of cartilage. C-PS1 collagen, together with higher-Mr forms were present in the vitreous humour, but the higher-Mr forms were not seen in cartilage. Both C-PS1 and C-PS2 were present in vitreous humour and cartilage, but vitreous humour contained three times more of these collagens than did cartilage. Despite the difference in amount, the molar ratio C-PS1/C-PS2 was approx. 1 in both tissues, suggesting that they are components of a larger molecule. The 1 alpha, 2 alpha, 3 alpha collagens were present in the same concentration in both tissues. These three chains co-precipitated on dialysis against phosphate-buffered saline, pH 7.2, in a manner analogous to type V collagen.

Healing of Circular Defects in the Rabbit Medial Meniscus Can Occur Spontaneously and Is not Improved by Intra-Articular Hyaluronic Acid

1996 ◽  
Vol 09 (02) ◽  
pp. 60-5 ◽  
Author(s):  
N. Hope ◽  
P. Ghosh ◽  
S. Collier
Keyword(s):  
Hyaluronic Acid ◽  
Medial Meniscus ◽  
Chondroitin Sulphate ◽  
Rabbit Model ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Keratan Sulphate ◽  
Meniscal Healing ◽  
Meniscus Healing ◽  
Made In

SummaryThe aim of this study was to determine the effects of intra-articular hyaluronic acid on meniscal healing. Circular defects, 1.0 mm in diameter, were made in the anterior third of the medial meniscus in rabbits. In one joint, 0.4 ml hyaluronic acid (Healon®) was instilled, and in the contralateral (control) joint, 0.4 ml Ringer’s saline. Four rabbits were killed after four, eight and 12 weeks and the menisci examined histologically. By eight weeks most of the lesions had healed by filling with hyaline-like cartilage. Healing was not improved by hyaluronic acid treatment. The repair tissue stained strongly with alcian blue, and the presence of type II collagen, keratan sulphate, and chondroitin sulphate was demonstrated by immunohistochemical localisation. In contrast to the circular defects, longitudinal incisions made in the medial menisci of a further six rabbits did not show any healing after 12 weeks, indicating that the shape of the lesion largely determined the potential for healing.The effect of hyaluronic acid on meniscal healing was tested in a rabbit model. With one millimeter circular lesions in the medial meniscus, healing by filling with hyalinelike cartilage was not significantly affected by the application of hyaluronic acid intra-articularly at the time of surgery, compared to saline controls, as assessed histologically four, eight and 12 weeks after the operation.

Characterization of human type II procollagen and collagen-specific antibodies and their application to the study of human type II collagen processing and ultrastructure

1997 ◽  
Vol 16 (1) ◽  
pp. 29-39 ◽  
Author(s):  
Sergio A. Jimenez ◽  
Leena Ala-Kokko ◽  
Darwin J. Prockop ◽  
Carmen F. Merryman ◽  
Nora Shepard ◽  
...  
Keyword(s):  
Type Ii Collagen ◽  
Type Ii ◽  
Specific Antibodies ◽  
Human Type

Graphite/UPE Nanocomposite: Transport, Thermal, Mechanical and Viscoelastic Properties

2019 ◽  
Vol 23 ◽  
pp. 201-212
Author(s):  
Shivkumari Panda ◽  
Dibakar Behera ◽  
Tapan Kumar Bastia
Keyword(s):  
Transport Properties ◽  
Unsaturated Polyester ◽  
Homogeneous Distribution ◽  
Thermo Gravimetric ◽  
New Class ◽  
The Matrix ◽  
Novel Method ◽  
Water Transport Properties ◽  
First Time

This chapter presents the preparation and characterization of some unique properties of nanocomposites by dispersing graphite flakes in commercial unsaturated polyester (UPE) matrix. The composite was prepared by a novel method with the use of solvent swelling technique. Three different specimens of UPE/graphite nanocomposites were fabricated with addition of 1, 2 and 3 wt% of graphite flakes. Except mechanical, viscoelastic and thermo gravimetric properties, transport properties like electrical conductivity, thermal conductivity and water transport properties were studied for the first time. Graphite flakes propose enhanced properties to the composites suggesting homogeneous distribution of the nanofiller in the matrix and strong interaction with the matrix. 2wt% nanofiller loading showed superior essential characteristics and after that the properties reduced may be due to the nucleating tendency of the nanofiller particles. The XRD pattern showed the compatibility of the graphite flakes by introducing a peak around 26.550 in the nanocomposites. SEM Properties are also in agreement with the compatibility. Nanocomposite with 2wt% graphite also showed remarkable enhancement in transport, mechanical, viscoelastic and thermo gravimetric properties. So by introduction of a small quantity of graphite endow the new class of multiphase nanocomposites with inimitable structure and tremendous application.

scholarly journals Cellular heterogeneity in cultured human chondrocytes identified by antibodies specific for alpha 2(XI) collagen chains.

1989 ◽  
Vol 109 (3) ◽  
pp. 1363-1369 ◽  
Author(s):  
B Swoboda ◽  
R Holmdahl ◽  
H Stöss ◽  
K von der Mark
Keyword(s):  
Hyaline Cartilage ◽  
Type Ii Collagen ◽  
Cross Reactivity ◽  
Cellular Heterogeneity ◽  
Human Chondrocytes ◽  
Type I ◽  
Type Ii ◽  
Human Cartilage ◽  
The Matrix ◽  
Type Xi Collagen

Collagen type XI is a component of hyaline cartilage consisting of alpha 1(XI), alpha 2(XI), and alpha 3(XI) chains; with 5-10% of the total collagen content, it is a minor but significant component next to type II collagen, but its function and precise localization in cartilaginous tissues is still unclear. Owing to the homology of the alpha 3(XI) and alpha 1(II) collagen chains, attempts to prepare specific antibodies to native type XI collagen have been unsuccessful in the past. In this study, we report on the preparation and use for immunohistochemistry of a polyclonal antibody specific for alpha 2(XI) denatured collagen chains. The antibody was prepared by immunization with the isolated alpha 2(XI) chain and reacts neither with native type XI collagen nor type I, II, V, or IX by ELISA or immunoblotting, nor with alpha 1(XI) or alpha 3(XI), but with alpha 2(XI) chains. Using this antibody, it was possible to specifically localize alpha 2(XI) in cartilage by pretreating tissue sections with 6 M urea. In double immunofluorescence staining experiments, the distribution of alpha 2(XI) as indicative for type XI collagen in fetal bovine and human cartilage was compared with that of type II collagen, using a monoclonal antibody to alpha 1(II). Type XI collagen was found throughout the matrix of hyaline cartilage. However, owing to cross-reactivity of the monoclonal anti-alpha 1(II) with alpha 3(XI), both antibodies produced the same staining pattern. Cellular heterogeneity was, however, detected in monolayer cultures of human chondrocytes.(ABSTRACT TRUNCATED AT 250 WORDS)

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