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PubMed1992

Localization of type II, IX and V collagen in the inner ear.

Types II and IX collagen are traditionally considered cartilage collagens; however, within the inner ear, types II and IX collagen have a more diverse distribution. In the adult gerbil, type II collagen is the major fibrillar component. In the otic capsule it is present surrounding the osteocytes embedded and branching in the periosteal layer, in the cartilaginous rests of the enchondral layer, and in the endosteal layer bordering the membranous labyrinth. In the regions of the sensory cells, type II collagen is found in the osseous spiral lamina, the connective tissue of the spiral limbus, the subepithelial tissue of the maculae in the vestibule and the cristae in the ampullae, and in the spiral ligament. It is present in the non-cartilaginous and acellular structures of the tectorial membrane over the cochlear hair cells and the vestibular membrane lining the semicircular canals. Type IX collagen, when present, in all cases co-localizes with type II collagen but is found in more limited regions. It is found only in the cartilaginous rests of the enchondral bone, the tectorial membrane and the vestibular membrane. Type V-like collagen, a connective tissue collagen, is found to have a complementary localization to types II and IX collagen within the interstitial bone of the otic capsule, the osseous spiral lamina and the tectorial membrane, but it is absent from the vestibular membrane. This report is the first documenting the co-localization of types II and IX collagen.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1989

A histological and biochemical assessment of the cartilage matrix obtained from in vitro storage of osteochondral allografts.

Fresh osteochondral allografts were stored at 4 degrees C in tissue culture media at variable time periods (3, 7, 14 and 28 days). Sterilely dissected tibial plateaus with a standardized 1/2 cm subchondral bone "shell" were obtained from canines 1-3 hrs post mortem. X-rays were taken to determine maturity of the animals. Only mature animals (closed epiphyses) were considered for the study. Histologically, safranin 0 (metachromatic stain for glycosaminoglycans) was observed in all experimental specimens. H&E stained sections showed at all time periods of 3, 7, 14 and 28 days that the cell morphology and arrangements were similar in the superficial and deep areas of the cartilage obtained from the stored osteochondral allograft when compared to the control articular cartilage. The cells were in lacunae and arranged in clusters. Biochemically, glycosaminoglycans and collagen content showed no difference at the 95% level of confidence during the duration of the study (28 days) when compared to the 0 day control cartilage. Collagen typing, based on the assessment by HPLC of the CNBr peptides showed the major presence of type II collagen (no evidence of dedifferentiation was observed). No type I was found to be present. Some apparent variations in the proportions of minor collagen components were noted--e.g. at 14 days the cartilage appeared to contain increased amounts of type XI but little or no type IX collagen (HMW, LMW) when compared to the day 0 control. At 28 days a shift to a larger amount of type IX collagen occurs, especially in the LMW component, with a small amount of type XI collagen when compared to normal day 0 articular cartilage. Cell viability, i.e., the ability of the allograft tissue to incorporate 35SO4 in the synthesis of glycosaminoglycans, was intact up to 28 days of storage.

Animals↗
PubMed1995

Zonal variations of types II, IX and XI collagen mRNAs in rat epiphyseal cartilage chondrocytes: quantitative evaluation of in situ hybridization by image analysis of radioautography.

The spatial-temporal distribution of the mRNAs for type IX and type XI collagens were compared to that of type II collagen mRNA in the tibial epiphyseal plate cartilage of normal growing rats. The mRNAs were detected by in situ hybridization with radio-labelled specific probes and visualized by radioautography. The areas covered by the resulting silver grains were quantified by computer assisted image analysis. The areas in chondrocytes of each zone of the epiphyseal plate cartilage, which correspond to the stages of chondrocyte development and function were determined. Types II, IX and XI mRNAs were present to some extent in chondrocytes of all zones. The distributions of type II and type IX collagen mRNAs were similar with the highest concentrations in the proliferative zone, and the lowest in the resting and calcifying zones chondrocytes. In contrast, type XI collagen mRNA had a different distribution, with the lowest concentration in the resting zone chondrocytes and a significant decrease in the calcifying zone chondrocytes. These patterns correlates with the changes in chondrocyte function, and may reflect the roles of the type IX and type XI collagens. The data show that computer assisted image analysis of in situ hybridization radioautographic images is a precise, rapid tool for analysing differences in gene expression.

Animals↗
PubMed1991

Cloning of a cDNA for a new member of the class of fibril-associated collagens with interrupted triple helices.

cDNA from embryonic chick skin has been isolated and characterized which encodes a novel member of the FACIT (fibril-associated collagen with interrupted triple helices) group whose other known members are collagen types IX and XII. Nucleotide sequence analysis of the cDNA, combined with characterization of a pepsin-resistant fragment of the protein from embryonic chick skin, demonstrates that the collagen chain is more closely related to the chain of type XII collagen than to those of type IX. It is most similar to a collagen, type XIV, recently identified in bovine skin. It is possible, therefore, that the cDNA codes for a chain of chicken type XIV collagen. From the additional data on molecular structure obtained by sequencing the cDNA, the FACIT family appears to consist of at least two classes of molecules: one of which contains the three chains of type IX collagen, and a second which includes the chains of collagen types XII and XIV.

Amino Acid Sequence↗
PubMed2001

Impact of mutations of cartilage matrix genes on matrix structure, gene activity and chondrogenesis.

OBJECTIVE: Chondrocytes in the growth plate at different stages of differentiation synthesize characteristic extracellular matrix (ECM) components. Mutations in some ECM genes result in chondrodysplasia in humans and mice. We aimed to evaluate the impact of loss- and gain-of-function mutations of ECM genes on matrix structure, gene expression and formation of the growth plate. DESIGN: We review information on the impact of deficiencies in proteoglycans, and types X and II collagens on skeletal development. Additionally, we compare the impact of a glycine904 to cysteine (G904C) mutation in the triple helical coding domain of mouse Col2a1 with two previously reported Col2a1 mutations (exon7 deletion (Del1) and G85C). The G904C Col2a1 gene was introduced as a transgene into mice. Transgenic newborn mice were examined for skeletal development. The histology of the epiphyseal cartilage and the growth plate, and the ultrastructure of chondrocytes and collagen fibrillar morphology in the ECM were studied in 18.5-day transgenic and wild-type fetuses. The distribution of the mRNAs for Col2a1, Col11a1, Col9a1, Matn1, Agc and Ihh in the growth plate of 18.5-day G904C/G904C and wild type fetuses were compared by in situ hybridization. RESULTS: Heterozygous transgenic mice harbouring five copies of the G904C Col2a1 transgene developed skeletal abnormalities and dwarfism. Homozygous G904C/G904C mice died at birth, showing cleft palate, disrupted zonation of chondrocytes and reduction of the zone of hypertrophic chondrocytes. Fewer collagen fibrils were found in ECM of the cartilage. Rough endoplasmic reticulum of the chondrocytes of G904C/+ and G904C/G904C mice was distended. In G904C/G904C mutant mice, Agc gene activity was extended to the hypertrophic zone. Expression of the other genes studied was unchanged. Calcified materials that were not found normally in the maturing and only at low abundance in the hypertrophic zones of the wild type growth plate, were present in these zones in G904C/G904C mice. Despite phenotypic similarities for the G904C and Del1 mice, reduced expression of types I, II, IX, X collagens and aggrecan were reported for the latter mutation. Changes in gene activity and matrix organization in the growth plate also accompanied deficiencies in aggrecan, perlecan and collagen II. CONCLUSIONS: The data suggest that a single amino acid alteration in collagen II could lead to skeletal abnormalities through multiple secondary effects on the synthesis and assembly of ECM components. The functional impact of mutations of ECM genes reveals that chondrodysplasia is caused not just by the formation of abnormal matrix molecules, but that the alteration of one ECM component may lead to a cascade of disruption of other gene activities in chondrocytes which collectively contribute to the pathological changes in the architecture of the growth plate.

Aggrecans↗
PubMed1999

Identification of novel pro-alpha2(IX) collagen gene mutations in two families with distinctive oligo-epiphyseal forms of multiple epiphyseal dysplasia.

Multiple epiphyseal dysplasia (MED) is a genetically heterogeneous disorder with marked clinical and radiographic variability. Traditionally, the mild "Ribbing" and severe "Fairbank" types have been used to define a broad phenotypic spectrum. Mutations in the gene encoding cartilage oligomeric-matrix protein have been shown to result in several types of MED, whereas mutations in the gene encoding the alpha2 chain of type IX collagen (COL9A2) have so far been found only in two families with the Fairbank type of MED. Type IX collagen is a heterotrimer of pro-alpha chains derived from three distinct genes-COL9A1, COL9A2, and COL9A3. In this article, we describe two families with distinctive oligo-epiphyseal forms of MED, which are heterozygous for different mutations in the COL9A2 exon 3/intron 3 splice-donor site. Both of these mutations result in the skipping of exon 3 from COL9A2 mRNA, but the position of the mutation in the splice-donor site determines the stability of the mRNA produced from the mutant COL9A2 allele.

Adolescent↗
PubMed1991

An analysis by rotary shadowing of the structure of the mammalian vitreous humor and zonular apparatus.

An electron microscopic analysis of human and bovine vitreous humor after rotary shadowing showed the presence of both collagen fibrils and an extensive loose network of hyaluronan molecules. No interaction between the collagen fibrils and the hyaluronan molecules was observed under the conditions used for rotary shadowing. Periodic "struts" were present on the surface of the collagen fibrils. These struts showed an organization the same as that previously observed for type IX collagen on the surface of collagen fibrils from chicken cartilage and vitreous. However, the knob of the noncollagenous NC4 domain of cartilage type IX collagen was not observed at the ends of the struts in a manner identical to that of chicken vitreous humor. Zonular fibrils were dissected out from bovine eyes and shown by rotary shadowing to contain a beaded fibril which is similar in morphology to the "elastin-associated" microfibrils of many connective tissues. Experiments in which the zonular fibrils were stretched and fixed prior to rotary shadowing showed that the distance between each bead is variable and can be accounted for by the bowing out of overlapping filaments which connect each bead.

Aged↗
PubMed1998

Use of rotary shadowing electron microscopy to investigate the collagen fibrils in the extracellular matrix of cuttle-fish (Sepia officinalis) and chicken cartilage.

Collagen fibrils isolated from sternal cartilage of chick embryo and chondrocranium of cuttle-fish (Sepia officinalis) were examined with the electron microscope after rotary showing. The aim was to determine whether collagen fibrils from S. officinalis cartilage contained collagen molecules similar to the type IX collagen of vertebrate cartilage. Cartilage from both sources presented a highly variable appearance and only occasionally did preparations contain fibrils having the structure described by Vaughan et al. (1988) for vertebrate cartilage. Subsequent electron microscope investigation of collagen samples during the various stages of fibril preparation showed that the method did not yield reproducible results, and that is altered the morphology of the isolated structures. It was not, therefore, possible to confirm the hypothesis that collagen molecules with a morphology similar to that type IX vertebrate collagen are a component of the extracellular matrix of cephalopod cartilage.

Animals↗
PubMed1995

Areas of asbestoid (amianthoid) fibers in human thyroid cartilage characterized by immunolocalization of collagen types I, II, IX, XI and X.

The distribution of type I, II, IX, XI and X collagens in and close to areas of asbestoid (amianthoid) fibers in thyroid cartilages of various ages was investigated in this study. Asbestoid fibers were first detected in thyroid cartilage from a 3-year-old male child. Areas of asbestoid fibers functionally appear to serve as guide rails for vascularization of thyroid cartilage. Alcian blue staining in the presence of 0.3 M MgCl2 revealed a loss of glycosaminoglycans in areas of asbestoid fibers. In addition, the fibers reacted positively with antibodies against collagen types II, IX and XI, but showed no staining with antibodies to collagen types I and X. Territorial matrix of adjacent chondrocytes showed the same staining pattern. In addition to staining for type II, IX and XI collagens, asbestoid fibers showed strong immunostaining for type I collagen after puberty but not for type X collagen. However, groups of chondrocytes within areas of asbestoid fibers reacted strongly with antibodies to type X collagen, suggesting that this collagen plays an important role in matrix of highly differentiated chondrocytes. The finding that these type X collagen-positive chondrocytes also revealed immunostaining for type I collagen confirms previous studies showing that hypertrophic chondrocytes can further differentiate into cells that are characterized by the synthesis of type X and I collagens.

Adolescent↗
PubMed2005

Adherence of Pasteurella multocida to fibronectin.

For many pathogens, adherence and/or invasion involve association with host extracellular matrix molecules, such as fibronectin (Fn). Pasteurella multocida was found to bind significantly to Fn and collagen type IX but not to laminin and collagen types IV and X. The binding of P. multocida to Fn was dose-dependent and was inhibited by heparin (Hep). Removal of polysaccharide capsule enhanced the binding capacity of the bacterium to Fn and inhibition by Hep. Protease treatment of bacteria decreased binding, implicating surface protein(s) as adhesive components. Investigation of the binding domain(s) of P. multocida on the Fn molecule revealed preferential binding to the N-terminal Hep-binding domain of Fn but not to the carboxyl-terminal Hep-binding domain. Furthermore, Fn, and anti-Fn antibodies inhibited P. multocida adherence to Madin-Darby bovine kidney cells, suggesting the involvement of Fn in the bacterium adherence to host cells. Ligand blotting, batch affinity purification and MALDI-TOF mass spectrometry implicated several proteins as putative adhesins of P. multocida in the Fn-mediated adherence. Taken together, the data suggest that P. multocida-Fn interaction may play a role in the bacterium adherence to host cells, and this may be mediated by bacterial surface proteins with preferential affinity for the Hep-1 binding domain of Fn.

Animals↗
PubMed1990

Fibril-associated collagens.

Many collagen fibrils have been shown to be heterotypic, i.e. composed of more than one collagen type. Fibrils containing type I collagen as the major constituent do also contain, at least in some tissues, type III and type V collagens. Fibrils containing type II collagen have been shown to also contain type XI collagen. The type I, II, III, V and XI collagen molecules are very similar and are clearly derived from a single ancestral gene. However their processings are not identical. While collagen types I and II have a N-propeptide which is cleaved for their insertion in the fibrils, collagen types V and XI keep a N-terminal extension which must include, based on the cDNA derived structures, a short triple helix and a globular domain. They are thought to contribute to the control of fibril lateral growth and diameter. Other collagens are associated with fibrils without having the long triple uninterrupted triple helix characteristic of collagen types I, II, III, V and XI. Type IX collagen has been shown to be covalently cross-linked to type II collagen and to lay at or near the surface of fibrils, with a triple helical arm projecting in the extrafibrillar space a globular N-terminal domain. Type XII collagen is found in type I collagen containing matrices and contains a triple helical domain homologous to the type IX COL1 domain. This suggests a similar function.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1991

Use of the metal replica technique in the electron microscopy of collagen.

The authors present a survey of visualization of the individual types of collagen by the metal replica technique, special attention was paid to the visualization of type IX collagen, which, together with type XI, is a minor component of cartilage collagen. The molecule of this collagen type contains three collagen and four non-collagen domains and during the isolation involving pepsin digestion it is cleaved into MHW and LMW fragments. The HMW fragment can be further cleaved into shorter and longer arm. Results of statistical evaluation of 199 measured molecular fragments showed the following length: whole molecule 194 +/- 23 nm, HMW 136 +/- 16 nm, the longer arm of the HMW 87 +/- +/- 12 nm and the LMW of shorter arm of the HMW 43 +/- 9 nm.

Collagen↗
PubMed1989

Bovine cartilage types VI and IX collagens. Characterization of their forms in vivo.

1. Collagens were extracted from bovine cartilage by 4 M-guanidinium chloride in the presence of proteinase inhibitors and identified by immunoblotting with specific anti-collagen sera. 2. The collagens retained their native conformations (shown by the resistance of their triple-helical domains to pepsin digestion), and the molecular masses of their component alpha-chains indicated that the chains were intact. 3. Type VI collagen was extracted as a large-molecular-mass disulphide-bonded aggregate composed of components of molecular mass 140 kDa and 200-240 kDa, and was therefore similar to type VI collagen identified in noncartilaginous tissues. Immunoblotting established the 200-240 kDa components as intact forms of the alpha 3(VI) chain. 4. Type IX collagen consisted of three clearly separable components of molecular mass 84 kDa, 72 kDa and 66 kDa, which were assigned to the alpha 1(IX)-, alpha 3(IX)- and alpha 2(IX)-chains respectively, and a large proportion of this collagen had no covalently bound glycosaminoglycan attached to the alpha 2(IX)-chain. 5. Differences between the type IX collagen extracted from bovine cartilage and that identified in biosynthetic studies on chick cartilage are discussed.

Animals↗
PubMed2001

Multiple epiphyseal dysplasia: radiographic abnormalities correlated with genotype.

Multiple epiphyseal dysplasia (MED) is an osteochondrodysplasia characterized clinically by mild short stature and early-onset degenerative joint disease and radiographically by epiphyseal hypoplasia/dysplasia. MED is genetically heterogeneous, with autosomal dominant cases resulting from mutations in at least three genes: the cartilage oligomeric matrix protein (COMP) gene (EDM1) and the COL9A2 (EDM2) and COL9A3 (EDM3) genes of type IX procollagen. We present here a comparison of the radiographic phenotypes of MED patients with type IX collagen gene mutations and those with COMP gene mutations. We reviewed radiographs from two patients with MED produced by COMP mutations, two families with COL9A2 mutations, and one family with a mutation in COL9A3. The data demonstrated that the patients with type IX collagen defects had more severe joint involvement at the knees and relative hip sparing, while the patients with COMP mutations had significant involvement at the capital femoral epiphyses and irregular acetabuli. This pattern of joint involvement was consistent regardless of overall degree of severity of the phenotype.

Adolescent↗
PubMed2003

Experimental induction of anterior disk displacement of the rabbit craniomandibular joint: an immuno-electron microscopic study of collagen and proteoglycan occurrence in the condylar cartilage.

BACKGROUND: Results from our previous studies suggest that surgical induction of anterior disk displacement (ADD) in the rabbit craniomandibular joint (CMJ) leads to histopathological alterations consistent with osteoarthritis. In addition, molecular changes in collagens and glycosaminoglycans (GAGs) were observed using immunohistochemistry. The purpose of the present study was to further characterize those molecular changes in collagens and GAGs using immuno-electron microscopy. METHODS: The right joint of 15 rabbits was exposed surgically and all discal attachments were cut except for the posterior attachment (the bilaminar zone). The disc was then repositioned anteriorly and sutured to the zygomatic arch. The left joint was used as a sham-operated control. Ten additional joints were used as non-operated controls. Mandibular condyles were removed 2 weeks following surgery and processed for light and immuno-electron microscopy using colloidal gold-labeled antibodies against collagen type I, II, VI and IX and against keratan sulfate, chondroitin-4 and -6-sulfate, and link protein. RESULTS: Light microscopic results showed osteoarthritic changes. Immuno-electron microscopy of osteoarthritic cartilage demonstrated a decline in type II collagen, the abnormal presence of type I collagen and loss of type VI and IX collagens. Quantitative colloidal gold immuno-electron microscopy confirmed the depletion of keratan sulfate, chondroitin-4 and -6-sulfate, and link protein in osteoarthritic cartilage. CONCLUSION: Anterior disk displacement leads to molecular alterations in both the collagen and the proteoglycans of rabbit condylar cartilage characteristic of osteoarthritis in other synovial joints. These alterations are consistent with loss of the shock absorber function of the cartilage and injury of the underlying bone.

Animals↗
PubMed2007

Unique matrix structure in the rough endoplasmic reticulum cisternae of pseudoachondroplasia chondrocytes.

Mutations in cartilage oligomeric matrix protein (COMP) cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (MED/EDM1). Because COMP exists as a homopentamer, only one mutant COMP subunit may result in an abnormal complex that is accumulated in expanded rough endoplasmic reticulum (rER) cisternae, a hallmark of PSACH. Type IX collagen and matrilin-3 (MATN3), also accumulate in the rER cisternae of PSACH chondrocytes, but it is unknown how mutant COMP interacts with these proteins. The studies herein focus on defining the organization of these intracellularly retained proteins using fluorescence deconvolution microscopy. A unique matrix organization was identified in which type II procollagen formed a central core surrounded by a protein network of mutant COMP, type IX collagen, and MATN3. This pattern of matrix organization was found in multiple cisternae from single chondrocytes and in chondrocytes with different COMP mutations, indicating a common pattern of interaction. This suggests that stalling of mutant COMP and an interaction between mutant COMP and type II procollagen are initiating events in the assembly of matrix in the rER, possibly explaining why the material is not readily cleared from the rER. Altogether, these data suggest that mutant COMP initiates and perhaps catalyzes premature intracellular matrix assembly.

Achondroplasia↗
PubMed2004

Cell-type specific trafficking of expressed mutant COMP in a cell culture model for PSACH.

Pseudoachondroplasia (PSACH) is an autosomal dominant disease that mainly affects cartilage, resulting in skeletal dysplasias and early onset osteoarthritis. PSACH is caused by mutations in the cartilage oligomeric matrix protein (COMP) gene. PSACH chondrocytes accumulate unique COMP-containing lamellar structures in an expanded rough endoplasmic reticulum (rER). Although COMP is also present in tendon extracellular matrix (ECM), it does not accumulate in PSACH tendon cells, suggesting the disease involves a chondrocyte-specific trafficking problem. To investigate putative cell-specific trafficking differences, we generated a cell culture model utilizing expression of the common DeltaD469 COMP mutation. In rat chondrosarcoma (RCS) cells, we find delayed secretion and ER accumulation of DeltaD469 COMP, paralleling the altered trafficking defect in PSACH chondrocytes. Non-chondrocytic COS-1 cells, in contrast, efficiently trafficked and secreted both mutant and wild-type COMP. In chondrocytic cells, expression of DeltaD469 COMP led to ER accumulation of type IX collagen, but did not affect aggrecan trafficking. Endogenous rat COMP accumulated in the ER along with expressed DeltaD469 COMP in a stably expressing RCS clone, consistent with the dominant negative effect of PSACH. When these stably expressing cells were cultured to promote ECM deposition, the small amount of secreted mutant COMP disrupted assembly of the normal fibrillar meshwork and caused irregular aggregates of COMP and type IX collagen to form. Thus, in a new model that reflects the cellular pathology of PSACH, we establish trafficking differences for mutant COMP in chondrocytic and non-chondrocytic cells and demonstrate that mutant COMP interferes with assembly of a normal ECM.

Achondroplasia↗
PubMed1994

The genes encoding alpha 2(IX) collagen (COL9A2) map to human chromosome 1p32.3-p33 and mouse chromosome 4.

We have determined the chromosomal locations of the human and murine genes coding for alpha 2(IX) collagen, a polypeptide subunit of the heterotrimeric type IX collagen molecule. COL9A2 was mapped to human chromosome 1p32.3-p33 using fluorescence in situ hybridization. A single-strand conformational polymorphism within the murine Col9a2 gene was used to map this locus to mouse chromosome 4. We also present new sequence data, which completes the coding information for the human alpha 2(IX) chain and revises the sequence for the chicken alpha 2(IX) chain. This permits comparison of the carboxyl-terminal (NC1) domains of the alpha 1(IX), alpha 2(IX), and alpha 3(IX) chains across several species.

Amino Acid Sequence↗