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.

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.

Specificity and T cell receptor β chain usage of a human collagen type II-reactive T cell clone derived from a healthy individual

1992 ◽  
Vol 22 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Tan Yan ◽  
Harald Burkhardt ◽  
Thomas Ritter ◽  
Barbara Bröker ◽  
Karl Heinz Mann ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Collagen Type ◽  
Cell Clone ◽  
Cell Receptor ◽  
Type Ii ◽  
Collagen Type Ii ◽  
T Cell Clone ◽  
Human Collagen ◽  
Β Chain

scholarly journals The mRNAs for the three chains of human collagen type XI are widely distributed but not necessarily co-expressed: implications for homotrimeric, heterotrimeric and heterotypic collagen molecules

1995 ◽  
Vol 311 (2) ◽  
pp. 511-516 ◽  
Author(s):  
V C H Lui ◽  
R Y C Kong ◽  
J Nicholls ◽  
A N Y Cheung ◽  
K S E Cheah
Keyword(s):  
Collagen Type ◽  
Subunit Composition ◽  
Messenger Rnas ◽  
Collagen Types ◽  
Fetal Tissues ◽  
Chain Composition ◽  
Collagen Molecules ◽  
Human Collagen ◽  
Human Fetal Tissues ◽  
Cross Type

In cartilage collagen type XI exists as heterotrimeric molecules composed of alpha 1(XI), alpha 2(XI) and alpha 3(XI) subunits. Messenger RNAs for some of the alpha chains of collagen type XI have also been found in non-chondrogenic tissues but the chain composition of the molecule in these sites is not known. Some non-chondrogenic tissues also contain heterotrimers containing collagen alpha 2(V) and alpha 1(XI) chains. We have explored the possibility that collagen type XI could exist in differing trimeric forms in non-chondrogenic tissues and aimed to predict the subunit composition of this collagen in those tissues. The distribution and relative levels of expression of collagen alpha 1(XI), alpha 2(XI) and alpha 3(XI)/alpha 1(II) mRNAs in different human fetal tissues were studied. Expression of mRNAs for all three genes of collagen type XI is not restricted to cartilage but is widespread. However, in some non-chondrogenic tissues, the mRNAs for all three alpha chains of collagen type XI were not co-expressed, but collagen alpha 1(XI) and alpha 2(XI) mRNAs were found either singly or without collagen alpha 3(XI) transcripts. Collagen type XI may therefore exist as homotrimers and/or heterotrimers composed of two collagen alpha(XI) chains in some tissues. The distribution of mRNAs for collagen alpha 2(V) and alpha 1(I) were also studied. Co-expression of collagen type XI, alpha 2(V) and alpha 1(I) mRNAs was found for many tissues. These findings have implications for the possibility of additional chain associations for collagen types XI and V in cross-type heterotrimers within heterotypic fibrils.

scholarly journals Undenatured collagen type II for the treatment of osteoarthritis: a review

2018 ◽  
Vol 4 (5) ◽  
pp. 684 ◽  
Author(s):  
Ram Prabhoo ◽  
Gauri Billa
Keyword(s):  
Collagen Type ◽  
Disease Process ◽  
Type Ii Collagen ◽  
Underlying Disease ◽  
Degree Of Hydrolysis ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Inflammatory Drugs ◽  
Immunological Factors ◽  
Undenatured Type Ii Collagen

<p class="abstract">Osteoarthritis is a prevalent musculoskeletal condition worldwide with rising rates in elderly people. Both mechanical and immunological factors are implicated in the pathogenesis of osteoarthritis resulting in destruction of the articular cartilage. Non-steroidal anti-inflammatory drugs (NSAIDs) commonly used for the treatment of osteoarthritis, are associated with several adverse events and also do not affect the underlying disease process. Clinicians and patients both seek options which are safe and effective in the treatment of osteoarthritis. Collagen derivatives represent a suitable option in such cases. Collagen is the most abundant component of the cartilage. Collage derivatives have shown to have disease modifying action in osteoarthritis. Depending on the degree of hydrolysis and molecular weight, collage derivatives are classified into undenaured collagen, gelatin and collage hydrolysate. Collagen derivatives are well tolerated without major safety concerns. Undenatured type II collagen has shown to provide significant improvement in patients with osteoarthritis. In this article we discuss, the pathophysiology of osteoarthritis with focus on immunological factors and evidence for the use of undenatured collagen type II in osteoarthritis.</p><p class="abstract"> </p>

scholarly journals Gene expression and extracellular matrix ultrastructure of a mineralizing chondrocyte cell culture system.

1991 ◽  
Vol 112 (3) ◽  
pp. 501-513 ◽  
Author(s):  
L C Gerstenfeld ◽  
W J Landis
Keyword(s):  
Extracellular Matrix ◽  
Culture System ◽  
Time Course ◽  
Collagen Synthesis ◽  
Collagen Type ◽  
Fold Increase ◽  
Proteoglycan Synthesis ◽  
Type Ii ◽  
Collagen Types ◽  
Matrix Mineralization

Conditions were defined for promoting cell growth, hypertrophy, and extracellular matrix mineralization of a culture system derived from embryonic chick vertebral chondrocytes. Ascorbic acid supplementation by itself led to the hypertrophic phenotype as assessed by respective 10- and 15-fold increases in alkaline phosphatase enzyme activity and type X synthesis. Maximal extracellular matrix mineralization was obtained, however, when cultures were grown in a nutrient-enriched medium supplemented with both ascorbic acid and 20 mM beta-glycerophosphate. Temporal studies over a 3-wk period showed a 3-4-fold increase in DNA accompanied by a nearly constant DNA to protein ratio. In this period, total collagen increased from 3 to 20% of the cell layer protein; total calcium and phosphorus contents increased 15-20-fold. Proteoglycan synthesis was maximal until day 12 but thereafter showed a fourfold decrease. In contrast, total collagen synthesis showed a greater than 10-fold increase until day 18, a result suggesting that collagen synthesis was replacing proteoglycan synthesis during cellular hypertrophy. Separate analysis of individual collagen types demonstrated a low level of type I collagen synthesis throughout the 21-d time course. Collagen types II and X synthesis increased during the first 2 wk of culture; thereafter, collagen type II synthesis decreased while collagen type X synthesis continued to rise. Type IX synthesis remained at undetectable levels throughout the time course. The levels of collagen types I, II, IX, and X mRNA and the large proteoglycan core protein mRNA paralleled their levels of synthesis, data indicating pretranslational control of synthesis. Ultrastructural examination revealed cellular and extracellular morphology similar to that for a developing hypertrophic phenotype in vivo. Chondrocytes in lacunae were surrounded by a well-formed extracellular matrix of randomly distributed collagen type II fibrils (approximately 20-nm diam) and extensive proteoglycan. Numerous vesicular structures could be detected. Cultures mineralized reproducibly and crystals were located in extracellular matrices, principally associated with collagen fibrils. There was no clear evidence of mineral association with extracellular vesicles. The mineral was composed of calcium and phosphorus on electron probe microanalysis and was identified as a very poorly crystalline hydroxyapatite on electron diffraction. In summary, these data suggest that this culture system consists of chondrocytes which undergo differentiation in vitro as assessed by their elevated levels of alkaline phosphatase and type X collagen and their ultrastructural appearance.(ABSTRACT TRUNCATED AT 400 WORDS)

Distribution of type I collagen, type II collagen and PNA binding glycoconjugates during chondrogenesis of three distinct embryonic cartilages

1992 ◽  
Vol 186 (3) ◽  
Author(s):  
Yasuyuki Sasano ◽  
Itaru Mizoguchi ◽  
Manabu Kagayama ◽  
Lillian Shum ◽  
Pablo Bringas ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Collagen Type ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Type Ii

Collagen/hyaluronan membrane as a scaffold for chondrocytes cultivation

Biologia ◽  
2009 ◽  
Vol 64 (5) ◽  
Author(s):  
Denisa Harvanová ◽  
Ján Rosocha ◽  
Dušan Bakoš ◽  
Róbert Švihla ◽  
Gabriel Vaško ◽  
...  
Keyword(s):  
Collagen Type ◽  
In Vitro Cultivation ◽  
Type Ii ◽  
Chondrocyte Viability ◽  
Suitable Material ◽  
Long Time ◽  
Human Collagen ◽  
Hematoxylin And Eosin ◽  
Safranin O

AbstractRabbit chondrocytes were cultivated in vitro using the collagen/hyaluronan membrane. The membrane did not show any adverse effects on chondrocyte viability during in vitro cultivation. The inoculated cells grew without any negative changes. According to the histochemical analyses: (i) hematoxylin and eosin; (ii) safranin O; and (iii) rabbit anti-human collagen type II staining, the rabbit chondrocytes maintained their morphology and phenotype during in vitro cultivation. The collagen/hyaluronan membrane became more stable and stiffer after long time cultivation. The proliferation of the chondrocytes stabilised the structure of the membrane. The collagen/hyaluronan membrane is suitable material for the chondrocyte growth and could provide functional tissue-engineered scaffold for cartilage repair.

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 Early detection of osteoarthritis in the rat with an antibody specific to type II collagen modified by reactive oxygen species

2021 ◽  
Vol 23 (1) ◽  
Author(s):  
Anne Gigout ◽  
Donata Harazin ◽  
Louise M. Topping ◽  
Didier Merciris ◽  
Sven Lindemann ◽  
...  
Keyword(s):  
Collagen Type ◽  
Cruciate Ligament ◽  
Type Ii Collagen ◽  
Lateral Compartment ◽  
Cartilage Degradation ◽  
Type Ii ◽  
Early Biomarker ◽  
Oxidant Production ◽  
Anterior Cruciate ◽  
Radiographic Changes

Abstract Background Osteoarthritis (OA) is a disease of the whole joint, with articular cartilage breakdown as a major characteristic. Inflammatory mediators, proteases, and oxidants produced by chondrocytes are known to be responsible for driving cartilage degradation. Nevertheless, the early pathogenic events are still unclear. To investigate this, we employed an antibody that is specific to oxidative post-translationally modified collagen type II (anti-oxPTM-CII) to detect early cartilage pathogenic changes in two rat models of OA. Methods The animals underwent surgery for destabilization of the medial meniscus (DMM) and were sacrificed after 3, 5, 7, 14, and 28 days. Alternatively, anterior cruciate ligament transection with partial meniscectomy (ACLT+pMx) was performed and animals were sacrificed after 1, 3, 5, 7, and 14 days. Joints were stained with toluidine blue and saffron du Gatinais for histological scoring, anti-oxPTM-CII, and anti-collagen type X antibodies (anti-CX). Results We observed positive oxPTM-CII staining as early as 1 or 3 days after ACLT+pMx or DMM surgeries, respectively, before overt cartilage lesions were visible. oxPTM-CII was located mostly in the deep zone of the medial tibial cartilage, in the pericellular and territorial matrix of hypertrophic chondrocytes, and co-localized with CX staining. Staining was weak or absent for the lateral compartment or the contralateral knees except at later time points. Conclusion The results demonstrate that oxidant production and chondrocyte hypertrophy occur very early in the onset of OA, possibly initiating the pathogenic events of OA. We propose to use anti-oxPTM-CII as an early biomarker for OA ahead of radiographic changes.

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