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.

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 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.

Immunohistochemical Localization of Matrix Proteins in the Femoral Joint Cartilage of Growing Commercial Pigs

1992 ◽  
Vol 29 (6) ◽  
pp. 514-520 ◽  
Author(s):  
S. Ekman ◽  
D. Heinegård
Keyword(s):  
Subchondral Bone ◽  
Matrix Protein ◽  
Collagen Type ◽  
Immunohistochemical Localization ◽  
Matrix Composition ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Chondrocyte Maturation ◽  
Proliferative Zone ◽  
The Matrix

The immunocytochemical localization of several matrix macromolecules, including collagen type II and proteoglycans, in the distal femoral articular-epiphyseal cartilage complex of 15 commercial pigs between the age of 6 and 18 weeks was studied. Early osteochondrotic lesions, i.e., chondronecrosis in the resting region of the growth cartilage, as well as extensions of necrotic cartilage into the subchondral bone, were present in all animals, except those 6 weeks old. A battery of antibodies were used for identification of macromolecules in the matrix at different stages of the disease. Chondrocyte involvement in the process could be studied by identifying the sequence of alterations in matrix macromolecules as the lesion developed. The immunostaining for aggrecan (large aggregating proteoglycans), cartilage oligomeric matrix protein, fibronectin, collagen type II, fibromodulin, and biglycan was more prominent in the areas of chondronecrosis, extending into the subchondral bone, than in the normal resting region. This altered pattern of matrix macromolecules resembled that of the matrix of the proliferative chondrocytes and suggests that the chondrocyte maturation had stopped in the proliferative zone. The matrix in the areas of chondronecrosis in the resting region resembled that in the normal resting region. Thus the chondronecrosis appears to have preceded alterations of the matrix composition. The antibody reactivity pattern was, however, altered in the matrix of the clustered chondrocytes in areas of chondronecrosis. Staining in these regions suggested a more prominent appearance of fibronectin and collagen type II than in the normal matrix of the resting region. These changes are suggestive of attempt to repair. The chondronecrotic areas restricted to the resting region have a matrix that is different from the matrix of the abnormal cartilage extending into the subchondral bone, which resembled the matrix of the proliferative region. Hence the osteochondrotic lesion may not start in the resting region, instead the maturation of chondrocytes seems to stop in the proliferative zone, which would result in impaired bone formation.

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)

scholarly journals Type II collagen deposition in cruciate ligament precedes osteoarthritis in the guinea pig knee

2002 ◽  
Vol 10 (5) ◽  
pp. 420-428 ◽  
Author(s):  
R.D. Young ◽  
A. Vaughan-Thomas ◽  
R.J. Wardale ◽  
V.C. Duance
Keyword(s):  
Guinea Pig ◽  
Cruciate Ligament ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Collagen Deposition

scholarly journals Comparative effectiveness of two methods for inducing osteoarthritis in a novel animal model, the Diannan small-ear pig1

2020 ◽  
Author(s):  
Di Jia ◽  
Yinghong He ◽  
Guofeng Cai ◽  
Jiali Zheng ◽  
Yuye Yang ◽  
...  
Keyword(s):  
Stromal Cell ◽  
Collagen Type ◽  
The Other ◽  
Cartilage Loss ◽  
Type Ii ◽  
Collagen Type Ii ◽  
Matrix Metalloproteinase 3 ◽  
Protein Levels ◽  
Stromal Cell Derived Factor ◽  
Chemical Groups

Abstract Background: Varieties of animals were used to study osteoarthritis pathogenesis. The Diannan small-ear pig, which is native to Yunnan, China, is thought to have an articular anatomy similar to that of humans and is more likely to be a source of pathological tissues than other animals. The aim of this study was determine whether this animal can serve as a more effective osteoarthritis model.[A1] Methods: Twenty-seven adult pigs were randomly divided into three groups and underwent the Hulth procedure, papain articular injection [A2] , and conventional breeding. After 4, 8, and 12 weeks, cartilage tissues from knee joint were extracted for general and histological observation, immunofluorescence, and biochemical analysis. [A3] Synovium was taken out for stromal cell-derived factor-1 analysis. Results: Histopathological observation showed obvious cartilage loss in two experimental groups, this cartilage loss was more severe in the chemical groups. Synovial stromal cell-derived factor1 levels increased over time in all groups. mRNA and protein levels of matrix metalloproteinase-3 were much higher in the chemical groups than in the other groups, whereas levels of collagen type II[A4] and aggrecan were significantly lower in the chemical groups than in the other groups. Immunofluorescence assays of collagen type II[A5] revealed an apparent reduction in this marker in the chemical groups compared with the other groups. Conclusions: These results indicated that the Diannan small-ear pig can be used as an effective osteoarthritis model. In addition, it is much more convenient and much faster to induce osteoarthritis by intra-articular injection of papain, which is a method worthy of being promoted.

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 Correction of abnormal matrix formed by cmd/cmd chondrocytes in culture by exogenously added cartilage proteoglycan.

1986 ◽  
Vol 103 (4) ◽  
pp. 1605-1614 ◽  
Author(s):  
M Takeda ◽  
H Iwata ◽  
S Suzuki ◽  
K S Brown ◽  
K Kimata
Keyword(s):  
Hyaluronic Acid ◽  
Culture Medium ◽  
Core Protein ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Intact Cartilage ◽  
The Matrix ◽  
Mutant Cells ◽  
Hyaluronic Acid Binding

The cartilage matrix deficiency (cmd/cmd) mouse fails to synthesize the core protein of cartilage-characteristic proteoglycan (cartilage PG). Chondrocytes from the cmd/cmd cartilage cultured in vitro produced nodules with greatly reduced extracellular matrix. Immunofluorescence staining revealed that the nodules of mutant cells differed from the normal in lacking cartilage PG and in uneven and reduced deposition of type II collagen. Exogenously added cartilage PG prepared from either normal mouse cartilage or Swarm rat chondrosarcoma to the culture medium was incorporated exclusively into the extracellular matrices of the nodules, with a concurrent correction of the abnormal distribution pattern of type II collagen. The incorporation of cartilage PG into the matrix was disturbed by hyaluronic acid or decasaccharide derived therefrom, suggesting that the incorporation process involves the interaction of added proteoglycan with hyaluronic acid. Both the hyaluronic acid-binding region and the protein-enriched core molecule prepared from rat chondrosarcoma cartilage PG could also be incorporated but, unlike the intact cartilage PG, they were distributed equally in the surrounding zones where fibroblast-like cells predominate. The results indicate that the intact form of cartilage PG is required for specific incorporation into the chondrocyte nodules, and further suggest that cartilage PG plays a regulatory role in the assembly of the matrix macromolecules.

Sign in / Sign up

Export Citation Format

Share Document