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.

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 113 Effects of aquatic conditioning in young horses. I. Markers of inflammation and cartilage metabolism

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 86-87
Author(s):  
Brittany L Silvers ◽  
Jessica L Leatherwood ◽  
Brian D Nielsen ◽  
Carolyn E Arnold ◽  
Brandon Dominguez ◽  
...  
Keyword(s):  
Treadmill Exercise ◽  
Random Effect ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Treatment Groups ◽  
Cartilage Metabolism ◽  
Markers Of Inflammation ◽  
Young Horses ◽  
And Cartilage

Abstract Aquatic treadmills improve range of motion and increase muscular strength in mature horses; however, effects of buoyancy on inflammation and cartilage metabolism in young horses are not well investigated. Therefore, thirty Quarter Horse yearlings of similar breeding were stratified by age, BW, and sex and randomly assigned to one of three treatment groups during a 140-d trial to evaluate the influence of aquatic vs. dry exercise on joint inflammation and cartilage metabolism in young horses transitioning to an advanced workload. Treatment groups included non-exercise control (CON; n = 10), dry treadmill exercise (DRY; n = 10), or aquatic treadmill exercise (H2O; n = 10; water at 60% wither height). Animals were housed in individual stalls and allowed turnout for a minimum of 10 h/d. During Phase I, DRY and H2O walked on treadmills 30 min/d, 5 d/wk from d 0 to d 112. Phase II represented transition to an advanced workload 5d/wk for 28 d (Table 1). Every 28 d following exercise, synovial fluid samples were collected and analyzed for prostaglandin E2 (PGE2), collagenase cleavage neopeptide (C2C), collagenase of type I and type II collagen (C1,2C), and carboxypeptide of type II collagen (CPII) using commercial ELISA kits. All data were analyzed using PROC MIXED of SAS, including random effect of horse within treatment, and repeated effect of day. Baseline treatment differences were accounted for using a covariate structure. There were no treatment ′ day interactions of synovial inflammation or markers of cartilage metabolism; however, there was an effect of day for each selected marker (P < 0.03). Changes in biomarkers of cartilage turnover in horses exercised at the walk, whether dry or aquatic, could not be distinguished from horses with access to turnout alone. This indicates that there are no negative effects of buoyancy on cartilage metabolism in yearlings transitioned from aquatic exercise to 28-d advanced workload.

scholarly journals Association of external nose deformity in individuals with nasal septal deviation

2019 ◽  
Vol 5 (5) ◽  
pp. 1372
Author(s):  
Ravi Kishore Hubballi ◽  
Shruthi Manohar Koujalagi
Keyword(s):  
Nasal Septum ◽  
Type I ◽  
Type Ii ◽  
Medical Sciences ◽  
Deviated Nasal Septum ◽  
Type Iv ◽  
External Nose ◽  
Facial Midline ◽  
Nose Deformity ◽  
Type V

<p class="abstract"><strong>Background:</strong> Deviated nasal septum presents a challenge as often functional problems as well as aesthetic deformities must be addressed. Deviated nasal septum can be a result of varying pathologies and etiologies. Classifying the nasal deviation enables the surgeon to choose the appropriate operative intervention. This study is intended to know the association of external nose deformity in patients with deviated nasal septum.</p><p class="abstract"><strong>Methods:</strong> 100 patients were attending to the Department of ENT, Vijayanagara Institute of Medical Sciences, Ballari with deviated nasal septum, septal dislocation, septal spur and external nose deformity. Deviated nasal septum was classified as per the classification proposed by Mladina. External nose deformity was classified into 5 types proposed by Yong Jo Jang’s classification depending on the orientation of 2 horizontal units (bony pyramid and cartilaginous subunits) with respect to facial midline.  </p><p class="abstract"><strong>Results:</strong> Out of 100 patients with deviated nasal septum, external nose deformity was present in 61% of the patients. Significant association was present between the deviated nasal septum and external nose deformity (p=0.01).</p><p><strong>Conclusions:</strong> Type II (33%) deviated nasal septum was most common followed by Type VII (31%). Among the external nose deformity, Type I was most common followed by Type V. Type II deviated nasal septum was associated most commonly with Type V external nose deformity, Type VII deviated nasal septum with Type I external nose deformity and Type IV deviated nasal septum with Type I/II external nose deformity in equal frequency.</p>

Antibodies to Collagen Types I–VI in Dupuytren’s Contracture

1986 ◽  
Vol 11 (1) ◽  
pp. 58-60
Author(s):  
R. S. PEREIRA ◽  
C. M. BLACK ◽  
S. M. TURNER ◽  
J. D. SPENCER
Keyword(s):  
Patient Group ◽  
Blood Donor ◽  
Collagen Type ◽  
Type Ii Collagen ◽  
Dupuytren’S Contracture ◽  
Type Ii ◽  
Collagen Types ◽  
Igg Antibody ◽  
Dupuytren's Contracture ◽  
Human Collagen

Sera from 16 patients with Dupuytren’s contracture were tested for IgG and IgM antibodies to native and denatured human collagen types I, II, III, IV, V and VI. IgG antibody to at least one collagen type was found in 11/16 (69%) of these patients, compared with 27/96 (28%) normal adult blood donor controls. The prevalence of antibody to denatured type II collagen was raised, and although there was no overall increase in HLA-DR4 compared with a control population, this antibody was associated with HLA-DR4 in this patient group.

scholarly journals Osthole Inhibits Proliferation and Induces Catabolism in Rat Chondrocytes and Cartilage Tissue

2015 ◽  
Vol 36 (6) ◽  
pp. 2480-2493 ◽  
Author(s):  
Guoqing Du ◽  
Yi Song ◽  
Lei Wei ◽  
Linghui Li ◽  
Xuezong Wang ◽  
...  
Keyword(s):  
Type Ii Collagen ◽  
Cartilage Explants ◽  
Cartilage Tissue ◽  
Blue Staining ◽  
Marker Genes ◽  
Dependent Manner ◽  
Type Ii ◽  
Expression Levels ◽  
Safranine O ◽  
And Cartilage

Background/Aims: Cartilage destruction is thought to be the major mediator of osteoarthritis. Recent studies suggest that inhibition of subchrondral bone loss by anti-osteoporosis (OP) drug can protect cartilige erosion. Osthole, as a promising agent for treating osteoporosis, may show potential in treating osteoarthritis. The purpose of this study was to investigate whether Osthole affects the proliferation and catabolism of rat chondrocytes, and the degeneration of cartilage explants. Methods: Rat chondrocytes were treated with Osthole (0 μM, 6.25 μM, 12.5 μM, and 25 μM) with or without IL1-β (10ng/ml) for 24 hours. The expression levels of type II collagen and MMP13 were detected by western Blot. Marker genes for chondrocytes (A-can and Sox9), matrix metalloproteinases (MMPs), aggrecanases (ADAMTS5) and genes implicated in extracellular matrix catabolism were evaluated by qPCR. Cell proliferation was assessed by measuring proliferating cell nuclear antigen (PCNA) expression and fluorescence activated cell sorter. Wnt7b/β-catenin signaling was also investigated. Cartilage explants from two-week old SD rats were cultured with IL-1β, Osthole and Osthole plus IL-1β for four days and glycosaminoglycan (GAG) synthesis was assessed with toluidine blue staining and Safranine O/Fast Green FCF staining, collagen type II expression was detected by immunofuorescence. Results: Osthole reduced expression of chondrocyte markers and increased expression of MMP13, ADAMTS5 and MMP9 in a dose-dependent manner. Catabolic gene expression levels were further improved by Osthole plus IL-1β. Osthole inhibited chondrocyte proliferation. GAG synthesis and type II collagen were decreased in both the IL-1β groups and the Osthole groups, and significantly reduced by Osthole plus IL-1β. Conclusions: Our data suggested that Osthole increases the catabolism of rat chondrocytes and cartilage explants, this effect might be mediated through inhibiting Wnt7b/β-catenin pathway.

scholarly journals Analysis of collagen types synthesized by rabbit ear cartilage chondrocytes in vivo and in vitro

1984 ◽  
Vol 221 (1) ◽  
pp. 189-196 ◽  
Author(s):  
K Madsen ◽  
K von der Mark ◽  
M van Menxel ◽  
U Friberg
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Type Ii Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Types ◽  
Rabbit Ear ◽  
Ear Cartilage

This study compares the collagen types present in rabbit ear cartilage with those synthesized by dissociated chondrocytes in cell culture. The cartilage was first extracted with 4M-guanidinium chloride to remove proteoglycans. This step also extracted type I collagen. After pepsin solubilization of the residue, three additional, genetically distinct collagen types could be separated by fractional salt precipitation. On SDS (sodium dodecyl sulphate)/polyacrylamide-gel electrophoresis they were identified as type II collagen, (1 alpha, 2 alpha, 3 alpha) collagen and M-collagen fragments, a collagen pattern identical with that found in hyaline cartilage. Types I, II, (1 alpha, 2 alpha, 3 alpha) and M-collagen fragments represent 20, 75, 3.5, and 1% respectively of the total collagen. In frozen sections of ear cartilage, type II collagen was located by immunofluorescence staining in the extracellular matrix, whereas type I collagen was closely associated with the chondrocytes. Within 24h after release from elastic cartilage by enzymic digestion, auricular chondrocytes began to synthesize type III collagen, in addition to the above-mentioned collagens. This was shown after labelling of freshly dissociated chondrocytes with [3H]proline 1 day after plating, fractionation of the pepsin-treated collagens from medium and cell layer by NaCl precipitation, and analysis of the fractions by CM(carboxymethyl)-cellulose chromatography and SDS/polyacrylamide-gel electrophoresis. The 0.8 M-NaCl precipitate of cell-layer extracts consisted predominantly of type II collagen. The 0.8 M-NaCl precipitate obtained from the medium contained type I, II, and III collagen. In the supernatant of the 0.8 M-NaCl precipitation remained, both in the cell extract and medium, predominantly 1 alpha-, 2 alpha-, and 3 alpha-chains and M-collagen fragments. These results indicate that auricular chondrocytes are similar to chondrocytes from hyaline cartilage in that they produce, with the exception of type I collagen, the same collagen types in vivo, but change their cellular phenotype more rapidly after transfer to monolayer culture, as indicated by the prompt onset of type III collagen synthesis.

scholarly journals Differential localization of mRNAs of collagen types I and II in chick fibroblasts, chondrocytes, and corneal cells by in situ hybridization using cDNA probes.

1986 ◽  
Vol 102 (6) ◽  
pp. 2302-2309 ◽  
Author(s):  
M Hayashi ◽  
Y Ninomiya ◽  
J Parsons ◽  
K Hayashi ◽  
B R Olsen ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Types ◽  
Paraffin Sections ◽  
Extracellular Matrix Components

We have employed a highly specific in situ hybridization protocol that allows differential detection of mRNAs of collagen types I and II in paraffin sections from chick embryo tissues. All probes were cDNA restriction fragments encoding portions of the C-propeptide region of the pro alpha-chain, and some of the fragments also encoded the 3'-untranslated region of mRNAs of either type I or type II collagen. Smears of tendon fibroblasts and those of sternal chondrocytes from 17-d-old chick embryos as well as paraffin sections of 10-d-old whole embryos and of the cornea of 6.5-d-old embryos were hybridized with 3H-labeled probes for either type I or type II collagen mRNA. Autoradiographs revealed that the labeling was prominent in tendon fibroblasts with the type I collagen probe and in sternal chondrocytes with the type II collagen probe; that in the cartilage of sclera and limbs from 10-d-old embryos, the type I probe showed strong labeling of fibroblast sheets surrounding the cartilage and of a few chondrocytes in the cartilage, whereas the type II probe labeled chondrocytes intensely and only a few fibroblasts; and that in the cornea of 6.5-d-old embryos, the type I probe labeled the epithelial cells and fibroblasts in the stroma heavily, and the endothelial cells slightly, whereas the type II probe labeled almost exclusively the epithelial cells except for a slight labeling in the endothelial cells. These data indicate that embryonic tissues express these two collagen genes separately and/or simultaneously and offer new approaches to the study of the cellular regulation of extracellular matrix components.

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