Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Collagen Type II”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 199 records · Page 11Linked to original sources
PubMed1989

Resistance to collagen-induced arthritis in DBA/1 mice by intraperitoneal administration of soluble type II collagen involves both CD4+ and CD8+ T lymphocytes.

In this paper we report that intraperitoneal administration of type II collagen in a soluble form protects DBA/1 mice against collagen-induced arthritis (CIA) on subsequent arthritogenic challenge with soluble type II collagen in adjuvant. The degree of arthritis suppression, which is expressed in terms of reduced incidence of arthritis, delayed onset and reduced anti-collagen antibody titres, depends on the dose and timing of the pre-immunization collagen injection. In order to elucidate the rôles of CD4+ and CD8+ T lymphocytes subsets in arthritis resistance we administered monoclonal antibodies (mAb) to these antigenic determinants around the time of immunization with soluble type II collagen. Anti-CD4 mAb caused abrogation of arthritis resistance while anti-CD8 mAb was less effective. However, administration of anti-CD8 mAb two weeks after pre-immunization with soluble collagen was very effective in reversing arthritis resistance. From these findings we conclude that CD4+ and CD8+ T cells are involved in resistance to arthritis though the relative importance of each subset changes during the course of the process leading to resistance to CIA.

Animals↗
PubMed1992

Genetic control of the immune response to collagen by the major histocompatibility complex in the rat: I. Humoral responses to bovine and chick type II collagen.

A number of congenic and recombinant rat strains with different RT1 haplotypes on a PVG/c background were immunised with native bovine or chick type II collagen. Only strains with the "u" haplotype were good responders to bovine type II collagen whilst all strains responded to chick type II collagen. However, the "u" haplotype was again associated with the production of the highest amounts of antibody. All the strains responded to a non-collagenous antigen, keyhole limpet haemocyanin, showing that this effect was not a general one relating to all antigens. When antibodies were produced to the immunising collagen, binding of antibodies to native rat type II collagen was also seen. This association, of high amounts of antibody with the "u" haplotype, was inherited in a dominant fashion when F1 and F2 hybrids between low responder (RT1a) and high responder (RT1u) were examined. The recombinant r1 (class I av1, class II c) and r8 (class I av1 and class II u) strains showed that "u" haplotype at class II rather than at class I was associated with the strong response to type II collagen. The absence of arthritis in the "u" haplotype rats, suggests that the "u" haplotype alone is insufficient for arthritis induction after immunisation with type II collagen. It suggests that background genes outside the RT1 complex influence arthritis production as Wistar rats with the RT1u haplotype (but different minor genes outside RT1 complex) give an arthritis incidence of 50% under identical immunisation protocols.

Animals↗
PubMed1989

Diastrophic dysplasia: evidence against a defect of type II collagen.

A description of an abnormal segment-long-spacing crystallite (SLS) pattern has been reported for type II collagen from patients with diastrophic dysplasia (Stanescu et al., 1982 a), a disorder that is characterized by large collagen fibrils in the cartilage matrix. The abnormal SLS consisted of an altered electron density between bands 42 and 45, which was interpreted as an abnormality in the type II collagen molecule. It was suggested that the type II collagen is abnormal in diastrophic dysplasia. We have examined SLS of type II collagen from two patients with diastrophic dysplasia and found the SLS patterns to be identical with that of control type II SLS in almost all micrographs. In a few micrographs of diastrophic SLS, crystallites exhibiting the pattern reported by Stanescu et al. were seen. However, the abnormally patterned crystallites always consisted of dimers that were overlapped at the COOH ends in such a way that an electron dense band of one crystallite was positioned between bands 42 and 45 of the second crystallite, apparently creating the abnormal pattern. The abnormal SLS pattern seen in these cases of diastrophic dysplasia appears to be the result of overlapping crystallites and may not be the result of an intrinsic abnormality of type II collagen. We have constructed histograms of the collagen fibril diameters in diastrophic cartilage. While they are larger than normal collagen fibrils, this by itself does not indicate an abnormality of type II collagen. We have shown that large fibrils such as these can be obtained from normal type II collagen when the structure of the cartilage is disrupted by extraction with guanidine.(ABSTRACT TRUNCATED AT 250 WORDS)

Bone Diseases, Developmental↗
PubMed1989

Type II collagen distribution in the ear of the developing chick embryo.

The localization of type II collagen was immunohistochemically studied in the developing chick ear using monoclonal antibodies. Type II collagen appeared under the basal lamina of the otocyst from developmental stages 14 to 16. In the otic capsule, endolymphatic duct, and semicircular canal membrane, type II collagen appeared in stage 23 or 24. From stages 28 to 29, type II collagen appeared in the primitive columella, endolymphatic sac, and fibrocartilaginous plate. Type II collagen was first observed in the crista ampullaris, basilar membrane, macula sacculi, and utriculi in stages 30 and 31. Type II collagen was not detected in the endolymphatic sac beyond developmental stage 37 and the amount of type II collagen in the otic capsule and columella decreased after stage 40. The wide distribution of type II collagen in the inner ear throughout the development of the chick embryo suggests that this collagen may act as a basic structural component of the ear.

Animals↗
PubMed1976

[Differences in distribution of type I and type II collagens in the superficial and intermediary zones of articular cartilage].

Undecalcified frozen sections, 40 mu thick, were cut from the knee articular cartilage of young adult Baboons (Papio papio). The sections were freeze dried and the superficial and the intermediate zones were separated by microdissection under a binocular dissecting microscope. The material of each zone was cleaved with CNBr and the major peptides were analyzed by discelectrophoresis in SDS polyacrylamide. Peptides alpha, CB 3,5 and alpha, (II) CB 10 were used as characteristic markers for type I and type II collagen respectively. The method could detect as little as 5-10% of type I collagen of total collagen in mixtures. The thin superficial zone contains type I and type II collagen. The intermediate zone contains only type II collagen. The possible biological significance of this different anatomical distribution of the two types of collagen is discussed. This special distribution could explain the contradictory data from the literature concerning the presence of type I collagen in the articular cartilage.

Animals↗
PubMed2003

Mapping Hsp47 binding site(s) using CNBr peptides derived from type I and type II collagen.

As a crucial molecular chaperone in collagen biosynthesis, Hsp47 interacts with the nascent form as well as the mature triple-helical form of procollagen. The location(s) of Hsp47 binding sites on the collagen molecule are, as yet, unknown. We have examined the substrate specificity of Hsp47 in vitro using well-characterized CNBr peptide fragments of type I and type II collagen along with radiolabeled, recombinant Hsp47. Interaction of these peptides with Hsp47 bound to collagen-coated microtiter wells showed several binding sites for Hsp47 along the length of the alpha1 and alpha2 chains of type I collagen and the alpha1 chain of type II collagen, with the N-terminal regions showing the strongest affinities. The latter observation was also supported by the results of a ligand-blot assay. Except for two peptides in the alpha2(I) chain, peptides that showed substantial binding to Hsp47 did so in their triple-helical and not random-coil form. Unlike earlier studies that used peptide models for collagen, the results obtained here on fragments of type I and type II collagen identify, for the first time, binding of Hsp47 to specific regions of the collagen molecule. They also point to additional structural requirements for Hsp47 binding besides the known preference for third-position Arg residues and the triple-helical conformation.

Binding, Competitive↗
PubMed1989

Structural analyses of the polymorphic area in type II collagen gene.

The structure of type II collagen gene is extremely well conserved but contains a cluster of high frequency polymorphisms in a 2.2 kb area. Here we report the nucleotide sequence of this DNA area, essential for the PCR-facilitated RFLP-analyses of this gene. In the structural analyses we found four differences in the deduced human amino acid sequence when compared to the published bovine amino acid sequence. The donor and acceptor signals and branch point signals required for the splicing events were in agreement with mammalian consensus sequences. The frequency of inverted repeats which could provoke the DNA strand to loop formation and consequently to deletion mutations did not differ from that found in other sequenced genes coding for fibrillar collagens. mutations did not differ from that found in other sequenced genes coding for fibrillar collagens.

Collagen↗
PubMed2004

Bone morphogenetic protein (BMP)-2 enhances the expression of type II collagen and aggrecan in chondrocytes embedded in alginate beads.

OBJECTIVE: For autologous chondrocyte transplantation (ACT) chondrocytes are expanded in vitro. During expansion these cells may dedifferentiate. This change in phenotype is characterized by a raised expression of type I collagen and a decrease in type II collagen expression. Since high expression of type II collagen is of central importance for the properties of hyaline cartilage, we investigated if the growth factor bone morphogenetic protein-2 (BMP-2) may modulate the chondrogenic phenotype in monolayer cell cultures and in three-dimensional culture systems. DESIGN: Chondrocytes from articular knee cartilage of 11 individuals (average age: 39.8 years) with no history of joint disease were isolated and seeded either in monolayer cultures or embedded in alginate beads in presence or absence of human recombinant BMP-2 (hr-BMP-2). Then, cells were harvested and analysis of the chondrogenic phenotype was performed using quantitative RT-PCR, immunocytochemistry and ELISA. RESULTS: Addition of BMP-2 to chondrocytes expanded in two-dimensional (2D) cultures during the first subculture (P1) had no effect on mRNA amounts encoding type II collagen and interleukin-1beta (IL-1beta). In contrast, seeding chondrocytes in three-dimensional (3D) alginate cultures raised type II collagen expression significantly and addition of BMP-2 enhanced this effect. CONCLUSIONS: We conclude that chondrocytes during expansion for ACT may benefit from BMP-2 activation only when seeded in an appropriate 3D culture system.

Adult↗
PubMed1988

Induction of an anti-human type II collagen response by monoclonal anti-idiotypic antibody.

Several distinct epitopes on human type II collagen were defined by using mAb. The presence of species-specific and species-nonspecific (common) epitopes was thus clarified. Anti-idiotypic mAb (Ab2) was developed against one of the antibodies (Ab1) reactive with species-specific epitopes. Thus Ab2 was demonstrated to recognize an idiotope expressed on the Ag-binding site (paratope) of Ab1, since the binding of Ab1 to human type II collagen was blocked by Ab2, and the binding of Ab2 to Ab1 was inhibited by soluble human type II collagen, but not by murine and bovine type II collagens. DBA/1 mice immunized with Ab2 coupled to keyhole limpet hemocyanin produced an antibody (Ab3) specifically reactive with human type II collagen. It was also demonstrated that Ab3 expressed an idiotype similar to that of Ab1. These findings indicate that anti-idiotypic antibody directed against mAb to human type II collagen mimics a species-specific epitope on human type II collagen. The anti-idiotypic antibody bearing internal image of type II collagen will open the way to isolation of the arthritogenic epitope on type II collagen.

Animals↗
PubMed1989

Type II collagen distribution in the ear of the guinea pig fetus.

By using monoclonal antibodies to type II collagen and immunohistochemical techniques, we studied the distribution of type II collagen in the developing guinea pig ear. Type II collagen appearance and disappearance corresponded to cartilage development and resorption. Type II collagen was identified in Meckel's and Reichert's cartilages, the cartilage plate of the auricle and external acoustic meatus, the ossicles, eustachian tube cartilage, and the otic capsule. Type II collagen also appeared with the development of structures in noncartilaginous parts including the tympanic membrane, tympanic annulus, basilar membrane, spiral limbus, spiral ligament, and osseous spiral lamina, Rosenthal's canal, the maculae of the utricle and saccule, and the semicircular canal membrane, crista ampullaris, and endolymphatic duct. Type II collagen is distributed widely in the ear after the early stages of development. Thus, type II collagen should be considered an important structural component of the ear.

Animals↗
PubMed2005

[Relationship between HLA-DR4/1 subtypes and T cell responses to type II collagen or anti-C II 263-272 antibodies].

OBJECTIVE: To investigate the relationship between HLA-DR4/1 subtypes and T cell responses to type II collagen or anti-CII 263-272 antibodies. METHODS: Peripheral blood mononuclear cells and sera were obtained from 70 rheumatoid arthritis (RA) patients. T cell proliferative responses to CII 263-272 were evaluated by [(3)H] thymidine incorporation assay. Antibodies specific to CII 263-272 were determined by ELISA. HLA-DR4/1 subtypes were analyzed by PCR-SSP. RESULTS: In HLA-DR4/1 positive group, T cell proliferative responses to CII 263-272 were observed in 55.6% RA patients and anti-CII 263-272 antibodies were present in 66.7% RA patients. In HLA-DR4/1 negative group, T cell proliferative responses to CII 263-272 were observed in 30.3% RA patients and anti-C II 263-272 antibodies were present in 34.8% RA patients. The number of positive antibodies to CII 263-272 or T cell proliferative responses to CII 263-272 in HLA-DR4/1 positive group were higher than in negative group. CONCLUSION: There is a relationship between HLA-DR4/1 subtypes and T cell responses to CII 263-272 or anti-CII 263-272 antibodies.

Adult↗
PubMed1984

Isolation of cDNA and genomic DNA clones encoding type II collagen.

A cDNA library constructed from total chick embryo RNA was screened with an enriched fraction of type II collagen mRNA. Two overlapping cDNA clones were characterized and shown to encode the COOH propeptide of type II collagen. In addition, a type II collagen clone was isolated from a Charon 4A library of chick genomic fragments. Definitive identification of the clones was based on DNA sequence analysis. The 3' end of the type II collagen gene appears to be similar to that of other interstitial collagen genes. Northern hybridization data indicates that there is a marked decrease in type II collagen mRNA levels in chondrocytes treated with the dedifferentiating agent 5-bromodeoxyuridine. The major type II collagen mRNA species is 5300 bases long, similar to that of other interstitial collagen RNAs.

Amino Acid Sequence↗
PubMed1997

An HLA-DR1 transgene confers susceptibility to collagen-induced arthritis elicited with human type II collagen.

Rheumatoid arthritis (RA) is an autoimmune disease that is strongly associated with the expression of several HLA-DR haplotypes, including DR1 (DRB1*0101). Although the antigen that initiates RA remains elusive, it has been shown that many patients have autoimmunity directed to type II collagen (CII). To test the hypothesis that HLA-DR1 is capable of mediating an immune response to CII, we have generated transgenic mice expressing chimeric (human/mouse) HLA-DR1. When the DR1 transgenic mice were immunized with human CII (hCII), they developed a severe autoimmune arthritis, evidenced by severe swelling and erythema of the limbs and marked inflammation and erosion of articular joints. The development of the autoimmune arthritis was accompanied by strong DR1-restricted T and B cell responses to hCII. The T cell response was focused on a dominant determinant contained within CII(259-273) from which an eight amino acid core was defined. The B cell response was characterized by high titers of antibody specific for hCII, and a high degree of cross-reactivity with murine type II collagen. These data demonstrate that HLA-DR1 is capable of presenting peptides derived from hCII, and suggest that this DR1 transgenic model will be useful in the development of DR1-specific therapies for RA.

Adjuvants, Immunologic↗
PubMed1997

In patients with rheumatoid arthritis IgG binding to denatured collagen type II is in part mediated by IgG-fibronectin complexes.

The presence of autoantibodies to native and denatured collagen type II has been reported in some patients with rheumatoid arthritis (RA). This study examined the molecular nature of IgG binding to native and denatured collagen type II. The binding of IgG to native and denatured collagen was detected with an ELISA. Serum proteins were separated by size with gel filtration. Gel-filtered fractions were further characterized by binding to staphylococcal protein A. Among plasmas or serums from 60 patients with RA, 12 patients had IgG binding to native collagen type II and 12 had IgG binding to denatured collagen type II. Decomplementing normal serums by heating to 56 degrees C for 30 min markedly increased IgG binding to denatured collagen type II, but not to native collagen. This binding was shown to result from a complex formed between IgG and fibronectin. Nine unheated RA serums were separated by gel filtration. The IgG binding to native collagen was limited to monomeric IgG, but in these serums 65.6 +/- 22.0% of the IgG binding to denatured collagen type II was in the excluded protein fractions. The binding of IgG to denatured collagen type II in the excluded fractions was inhibited by fibronectin and did not bind to staphylococcal protein A. In patients with RA, the IgG binding to native collagen type II represents true autoantibodies. In contrast, in these patients the majority of IgG binding to denatured collagen type II is caused by macromolecular complexes formed between fibronectin and IgG or between fibronectin and IgG-containing immune complexes.

Arthritis, Rheumatoid↗
PubMed1994

Type II collagen distribution during cranial development in Xenopus laevis.

Epithelially expressed type II collagen is thought to play a prominent role in the embryonic patterning and differentiation of the vertebrate skull, primarily on the basis of data derived from amniotes. We describe the spatiotemporal distribution of type II collagen in the embryonic head of the African clawed frog, Xenopus laevis, using whole-mount and serial-section immunohistochemical analysis. We studied embryos spanning Nieuwkoop and Faber (1967) stages 21-39, a period including cranial neural crest cell migration and ending immediately before the onset of neurocranial chondrogenesis. Xenopus displays a transient expression of type II collagen beginning at least as early as stage 21; staining is most intense and widespread at stages 33/34 and 35/36 and subsequently diminishes. Collagen-positive areas include the ventrolateral surface of the brain, sensory vesicles, notochord, oropharynx, and integument. This expression pattern is similar, but not identical, to that reported for the mouse and two bird species (Japanese quail, domestic fowl); thus epithelially expressed type II collagen appears to be a phylogenetically widespread feature of vertebrate cranial development. Consistent with the proposed role of type II collagen in mediating neurocranial differentiation, most collagen-positive areas lie adjacent to subsequent sites of chondrogenesis in the neurocranium but not the visceral skeleton. However, much of the collagen is expressed after the migration of cranial neural crest, including presumptive chondrogenic crest, seemingly too late to pattern the neurocranium by entrapment of these migrating cells.

Animals↗
PubMed1994

Effects of certain antiarthritic agents on the synthesis of type II collagen and glycosaminoglycans in rat chondrosarcoma cultures.

Cartilage destruction is a characteristic feature of osteoarthritis. Treatment with certain nonsteroidal anti-inflammatory drugs could exacerbate cartilage destruction by impairing the synthesis of cartilage matrix proteins, type II collagen and proteoglycan. In order to monitor the changes occurring in cartilage collagen synthesis, we developed a type II collagen specific ELISA. The effects of antiarthritic agents on type II collagen and glycosaminoglycan synthesis were examined in rat chondrosarcoma cultures. Drugs were added to the monolayer cultures and 4 days later the total type II collagen, as determined by the type II collagen ELISA, and glycosaminoglycan content, as measured by dimethyl-methylene blue dye binding assay, was measured. All drugs except tiaprofenic acid decreased type II collagen synthesis by at least 40% at 100 micrograms/ml. Tiaprofenic acid at 1 microgram/ml increased type II collagen content by 54% of the controls. Glycosaminoglycan synthesis was decreased by acetylsalicylic acid, diclofenac and tiaprofenac acid, at 50 micrograms/ml or above. Indomethacin, naproxen and dexamethasone had no effect. Interestingly, tenidap stimulated the glycosaminoglycan synthesis by 32% at 100 micrograms/ml. We show that the combination of chondrosarcoma cultures, type II collagen specific ELISA and dimethylmethylene blue dye binding assay serves as a useful model for screening the effects of agents capable of modulating type II collagen and glycosaminoglycan synthesis.

Analysis of Variance↗
PubMed1994

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

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.

Animals↗
PubMed1975

Specificity of the antibody response in inbred mice to bovine type I and type II collagen.

Mouse antibodies to soluble bovine skin (type I) collagen react with determinants which are located in the rigid triple-helical portion of the antigen and become destroyed upon unfolding the molecule. Helical antigenic determinants are dependent on the genuine chain assembly, e.g. alpha[1(I)]2alpha2. Artefactual triplehelical structures of the composition [alpha1(I)]3 or [alpha2]3 or a genetically distinct type II collagen from cartilage showed no or only weak cross-reactivity. Pepsin treatment of type I collagen known to remove short, non-helical sequences at both ends of the molecule had virtually no effect on antigenicity and immunogenic activity. A radioimmunoassay failed to detect antibodies in three congenic resistant mouse strains immunized with denatured type I collagen. These strains had been previously classified as high or low responders to native type I collagen. Agglutination titres vs denatured collagen culd already be demonstrated in nonimmune sera. The agglutinating activity was labile against heating at 56 degrees and could not be increased by immunization. Two out of five inbred strains showed a high response against pepsin-dissolved bovine type II collagen with the chain composition [alpha1(II)]3. Lack of correlation in the responder state to both collagen types indicated control by different immune response genes. Antibodies to type II collagen also reacted against triple-helical antigenic determinants and showed neglible cross-reaction with type I collagen.

Animals↗