Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The minor collagens in articular cartilage.

ABSTRACT: Articular cartilage is a connective tissue consisting of a specialized extracellular matrix (ECM) that dominates the bulk of its wet and dry weight. Type II collagen and aggrecan are the main ECM proteins in cartilage. However, little attention has been paid to less abundant molecular components, especially minor collagens, including type IV, VI, IX, X, XI, XII, XIII, and XIV, etc. Although accounting for only a small fraction of the mature matrix, these minor collagens not only play essential structural roles in the mechanical properties, organization, and shape of articular cartilage, but also fulfil specific biological functions. Genetic studies of these minor collagens have revealed that they are associated with multiple connective tissue diseases, especially degenerative joint disease. The progressive destruction of cartilage involves the degradation of matrix constituents including these minor collagens. The generation and release of fragmented molecules could generate novel biochemical markers with the capacity to monitor disease progression, facilitate drug development and add to the existing toolbox for in vitro studies, preclinical research and clinical trials.

SUBMITTER: Luo Y

PROVIDER: S-EPMC5546929 | biostudies-other | 2017 Aug

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Main and Minor Types of Collagens in the Articular Cartilage: The Role of Collagens in Repair Tissue Evaluation in Chondral Defects.

Project description:Several collagen subtypes have been identified in hyaline articular cartilage. The main and most abundant collagens are type II, IX and XI collagens. The minor and less abundant collagens are type III, IV, V, VI, X, XII, XIV, XVI, XXII, and XXVII collagens. All these collagens have been found to play a key role in healthy cartilage, regardless of whether they are more or less abundant. Additionally, an exhaustive evaluation of collagen fibrils in a repaired cartilage tissue after a chondral lesion is necessary to determine the quality of the repaired tissue and even whether or not this repaired tissue is considered hyaline cartilage. Therefore, this review aims to describe in depth all the collagen types found in the normal articular cartilage structure, and based on this, establish the parameters that allow one to consider a repaired cartilage tissue as a hyaline cartilage.

| S-EPMC8706311 | biostudies-literature

Expression of minor cartilage collagens and small leucine rich proteoglycans may be relatively reduced in osteoarthritic cartilage.

Project description:BackgroundIn osteoarthritis (OA), cartilage matrix is lost despite vigorous chondrocyte anabolism. In this study, we attempted to determine whether altered matrix synthesis is involved in this paradox in disease progression through gene expression analysis and ultrastructural analysis of collagen fibrils within the cartilage matrix.MethodsCartilage tissues were obtained from 29 end-stage OA knees and 11 control knees. First, cDNA microarray analysis was performed and the expression of 9 genes involved in collagen fibrillogenesis was compared between OA and control cartilages. Then their expression was investigated in further detail by a quantitative polymerase chain reaction (qPCR) analysis combined with laser capture microdissection. Finally, collagen fibril formation was compared between OA and control cartilage by transmission electron microscopy.ResultsThe result of the microarray analysis suggested that the expression of type IX and type XI collagens and fibrillogenesis-related small leucine-rich proteoglycans (SLRPs) may be reduced in OA cartilage relative to the type II collagen expression. The qPCR analysis confirmed these results and further indicated that the relative reduction in the minor collagen and SLRP expression may be more obvious in degenerated areas of OA cartilage. An ultrastructural analysis suggested that thicker collagen fibrils may be formed by OA chondrocytes possibly through reduction in the minor collagen and SLRP expression.ConclusionsThis may be the first study to report the possibility of altered collagen fibrillogenesis in OA cartilage. Disturbance in collagen fibril formation may be a previously unidentified mechanism underlying the loss of cartilage matrix in OA.

| S-EPMC6525975 | biostudies-literature

Isolation and Characterisation of Major and Minor Collagens from Hyaline Cartilage of Hoki (Macruronus novaezelandiae).

Project description:The composition and properties of collagen in teleost (bony fish) cartilage have never been studied. In this study, we aimed to identify and characterise all collagen species in the nasal cartilage of hoki (Macruronus novaezelandiae). Four native collagen species were extracted using two techniques, and isolated with differential salt precipitation. We were able to assign the identity of three of these collagen species on the basis of solubility, SDS-PAGE and amino acid analyses. We found that hoki cartilage contains the major collagen, type II, and the minor collagens, type IX and type XI, which are homologous to those found in mammal and chicken cartilage. Using these extraction protocols, we also isolated a full-length type IX collagen from cartilage for the first time. In addition, we detected a 90 kDa, highly glycosylated collagen that has not been identified in any other species. For each isolate, structural and biochemical characterisations were performed using circular dichroism and Fourier transform infrared spectroscopy analyses, and the thermal denaturation properties were determined. Our results showed that the properties of hoki cartilage-derived collagens are similar to those of collagens in mammalian cartilage, indicating that teleost cartilage could provide biological ingredients for the development of biomaterials to treat cartilage-related illnesses.

| S-EPMC6521242 | biostudies-literature

The expression patterns of minor fibrillar collagens during development in zebrafish.

Project description:Minor fibrillar collagens are recognized as the organizers and nucleators during collagen fibrillogenesis but likely serve additional functions. The minor fibrillar collagens include collagens type V and XI. Mutations of collagens type V and XI can cause Ehlers-Danlos, Stickler's, and Marshall's syndromes in human. We have characterized the spatiotemporal expression patterns of Col11a1, Col11a2, Col5a1 as well as Col5a3 in zebrafish embryos by in situ hybridization. Col5a1 is expressed in developing somites, neural crest, the head mesenchyme, developing cranial cartilage, pharyngeal arches and vertebrae. Col5a3 is detected in the notochord, mesenchyme cells in the eyes and lens. Both Col11a1 and Col11a2 have similar expression patterns, including notochord, otic vesicle, and developing cranial cartilages. Zebrafish may therefore serve as a valuable vertebrate model system for the study of diseases associated with collagens type V and XI mutations.

| S-EPMC2956583 | biostudies-literature

horse articular cartilage explant secretome

Project description:proteins secreted during 5 day culture of articular cartilage explants

2012-03-04 | PRD000359 | Pride

Circadian Mouse Articular Cartilage Proteomics

Project description:Mouse hip articular cartilage was collected every 4 hour for 48 hours and analysed by mass spec

2021-03-01 | PXD019431 | Pride

Minor fibrillar collagens, variable regions alternative splicing, intrinsic disorder, and tyrosine sulfation.

Project description:Minor fibrillar collagen types V and XI, are those less abundant than the fibrillar collagen types I, II and III. The alpha chains share a high degree of similarity with respect to protein sequence in all domains except the variable region. Genomic variation and, in some cases, extensive alternative splicing contribute to the unique sequence characteristics of the variable region. While unique expression patterns in tissues exist, the functions and biological relevance of the variable regions have not been elucidated. In this review, we summarize the existing knowledge about expression patterns and biological functions of the collagen types V and XI alpha chains. Analysis of biochemical similarities among the peptides encoded by each exon of the variable region suggests the potential for a shared function. The alternative splicing, conservation of biochemical characteristics in light of low sequence conservation, and evidence for intrinsic disorder, suggest modulation of binding events between the surface of collagen fibrils and surrounding extracellular molecules as a shared function.

| S-EPMC3484837 | biostudies-literature

Nutrition and degeneration of articular cartilage.

Project description:PurposeTo determine the importance of synovial fluid (SF) or subchondral bone marrow (BM) as nutrition sources in cartilage degeneration.MethodsNinety-five-month-old male rabbits were randomly divided into 5 groups according to sources of nutrition: SFBM-both; BM-only; SF-only; None-SFBM; and Free plug (unrestricted). Nutrition to 4-mm-diameter cylindrical osteochondral plugs created on the trochlea of the distal femurs was obstructed by Polyvinyl Chloride (PVC) cap. Cartilage changes were assessed after 4, 8, and 12 weeks by histology, immunohistochemistry, and real-time PCR.ResultsCartilage in the BM-only group suffered the greatest damage, followed by the None-SFBM and SF-only groups. Apoptosis was increased in the BM-only and None-SFBM groups compared with others. Cartilage was significantly thinner at all time points in the BM-only and None-SFBM groups when compared with SFBM-both and Free plug, whereas in the SF-only group, this difference occurred after 8 weeks. Compared with SFBM-both and Free plug, expression of collagen II and aggrecan mRNAs in all groups was decreased but MMP-3 increased, respectively.ConclusionOur data indicate that SF-derived nutrition is the dominant source of sustenance for adult cartilage structure and function. Cartilage damage is observed when the only nutrition source is the BM.

| S-EPMC3717153 | biostudies-literature

Temperature effects in articular cartilage biomechanics.

Project description:Articular cartilage is the soft tissue that covers contacting surfaces of bones in synovial joints. Cartilage is composed of chondrocytes and an extracellular matrix containing numerous biopolymers, cations and water. Healthy cartilage functions biomechanically to provide smooth and stable joint movement. Degenerative joint diseases such as osteoarthritis involve cartilage deterioration, resulting in painful and cumbersome joint motion. Temperature is a fundamental quantity in mechanics, yet the effects of temperature on cartilage mechanical behavior are unknown. This study addressed the questions of whether cartilage stiffness and stress relaxation change with temperature. Samples of middle-zone bovine calf patellofemoral cartilage were tested in unconfined compression first at 24°C and then again after heating to 60°C. The data reveal that when temperature increases: (1) both peak and equilibrium stiffness increase by 150 and 8%, respectively, and (2) stress relaxation is faster at higher temperature, as shown by a 60% decrease in the time constant. The increases in temperature-dependent stiffness are consistent with polymeric mechanisms of matrix viscoelasticity but not with interstitial fluid flow. The changes in the time constant are consistent with a combination of both fluid flow and matrix viscoelasticity. Furthermore, we discovered a novel phenomenon: at stress-relaxation equilibrium, compressive stress increased with temperature. These data demonstrate a rich area of cartilage mechanics that has previously been unexplored and emphasize the role of polymer dynamics in cartilage viscoelasticity. Further studies of cartilage polymer dynamics may yield additional insight into mechanisms of cartilage material behavior that could improve treatments for cartilage degeneration.

| S-EPMC2966351 | biostudies-literature

NFATc1 marks articular cartilage progenitors and negatively determines articular chondrocyte differentiation.

Project description:The origin and differentiation mechanism of articular chondrocytes remain poorly understood. Broadly, the difference in developmental mechanisms of articular and growth-plate cartilage is still less elucidated. Here, we identified that the nuclear factor of activated T-cells cytoplasmic 1 (NFATc1) is a crucial regulator of articular, but not growth-plate, chondrocyte differentiation during development. At the early stage of mouse knee development (embryonic day 13.5), NFATc1-expressing cells were mainly located in the flanking region of the joint interzone. With development, NFATc1-expressing cells generated almost all articular chondrocytes but not chondrocytes in limb growth-plate primordium. NFATc1-expressing cells displayed prominent capacities for colony formation and multipotent differentiation. Transcriptome analyses revealed a set of characteristic genes in NFATc1-enriched articular cartilage progenitors. Strikingly, the expression of NFATc1 was diminished with articular chondrocyte differentiation, and suppressing NFATc1 expression in articular cartilage progenitors was sufficient to induce spontaneous chondrogenesis while overexpressing NFATc1 suppresses chondrogenesis. Mechanistically, NFATc1 negatively regulated the transcriptional activity of the Col2a1 gene. Thus, our results reveal that NFATc1 characterizes articular, but not growth-plate, cartilage progenitors during development and negatively determines articular chondrocyte differentiation at least partly through regulating COL2A1 gene transcription.

| S-EPMC10076019 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data