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Journal articles on the topic 'Human Cartilage Matrix Protein (hCMP)'

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Published: 6 September 2023

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1

Kao, Yu-Hsien, Kun-Lieh Wu, Yuan-Kun Tu, Shwu Jen Chang, Chin Chang Yang, Chi-Yen Shen, Chih-Hsin Hung, and Shyh-Ming Kuo. "DEVELOPING AND ASSESSING AN IMMUNOCHROMATOGRAPHIC STRIP FOR DETECTING OSTEOARTHRITIS BASED ON URINE CARTILAGE OLIGOMERIC MATRIX PROTEINS." Biomedical Engineering: Applications, Basis and Communications 26, no. 06 (December 2014): 1450072. http://dx.doi.org/10.4015/s1016237214500720.

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An immunochromatographic strip was developed using a gold nanoparticle-conjugated monoclonal antibody to detect cartilage oligomeric matrix protein (COMP) in human urine. The monoclonal antibody anti-hCOMP produced from the hybridoma cell clone, hCOMP, is specific to osteoarthritis (OA), and polycolonal antibodies against COMP proteins were conjugated using a gold nanoparticle (approximately 40 nm) to enable detection. The preliminary test results of the proposed biomarker-prepared strip showed a positive correlation with those obtained using Western-blot assay to urinal COMP and exhibited a reliable detection range from 50 to 400 ng. The visual detection limit of the prepared test strip was 50 ng. The test results of OA patients showed consistent diagnostic agreement compared with clinical X-ray radiography. Thus, based on the detection of COMP from urine, the proposed immunoassay method is suitable for screening and noninvasively diagnosing OA.

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Adorable, L., and J. Litang. "Blood serum human cartilage oligomeric matrix protein (hCOMP) concentration in closed kinematic chain exercises and physiological cyclic loading using enzyme-linked immunosorbent assay (ELISA)." Annals of Physical and Rehabilitation Medicine 61 (July 2018): e458-e459. http://dx.doi.org/10.1016/j.rehab.2018.05.1069.

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3

Mundlos, S., and B. Zabel. "Developmental expression of human cartilage matrix protein." Developmental Dynamics 199, no. 3 (March 1994): 241–52. http://dx.doi.org/10.1002/aja.1001990308.

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4

DiCesare, Paul E., Matthias Mörgelin, Cathy S. Carlson, Subhalakshmi Pasumarti, and Mats Paulsson. "Cartilage oligomeric matrix protein: Isolation and characterization from human articular cartilage." Journal of Orthopaedic Research 13, no. 3 (May 1995): 422–28. http://dx.doi.org/10.1002/jor.1100130316.

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5

Loeser, R., C. S. Carlson, H. Tulli, W. G. Jerome, L. Miller, and R. Wallin. "Articular-cartilage matrix γ-carboxyglutamic acid-containing protein. Characterization and immunolocalization." Biochemical Journal 282, no. 1 (February 15, 1992): 1–6. http://dx.doi.org/10.1042/bj2820001.

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Matrix gamma-carboxyglutamic acid (Gla)-containing protein (MGP) was found to be present in articular cartilage by Western-blot analysis of guanidinium chloride extracts of human and bovine cartilage and was further localized by immunohistochemical studies on human and monkey specimens. In newborn articular cartilage MGP was present diffusely throughout the matrix, whereas in growth-plate cartilage it was seen mainly in late hypertrophic and calcifying-zone chondrocytes. In adult articular cartilage MGP was present primarily in chondrocytes and the pericellular matrix. Immunoelectron microscopy studies revealed an association between MGP and vesicular structures with an appearance consistent with matrix vesicles. MGP may be an important regulator of cartilage calcification because of its localization in cartilage and the known affinity of Gla-containing proteins for Ca2+ and hydroxyapatite.

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Di Cesare, Paul E., Cathy S. Carlson, Elliot S. Stollerman, Frank S. Chen, Michael Leslie, and Roberto Perris. "Expression of cartilage oligomeric matrix protein by human synovium." FEBS Letters 412, no. 1 (July 21, 1997): 249–52. http://dx.doi.org/10.1016/s0014-5793(97)00789-8.

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7

Newton, Gail, Stanislawa Weremowicz, Cynthia C. Morton, Neal G. Copeland, Debra J. Gilbert, Nancy A. Jenkins, and Jack Lawler. "Characterization of Human and Mouse Cartilage Oligomeric Matrix Protein." Genomics 24, no. 3 (December 1994): 435–39. http://dx.doi.org/10.1006/geno.1994.1649.

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Kwak, Yoon Hae, Jae Young Roh, Ki Seok Lee, Hui Wan Park, and Hyun Woo Kim. "Altered Synthesis of Cartilage-Specific Proteoglycans by Mutant Human Cartilage Oligomeric Matrix Protein." Clinics in Orthopedic Surgery 1, no. 4 (2009): 181. http://dx.doi.org/10.4055/cios.2009.1.4.181.

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Posey, Karen L., Sherri Davies, Elise S. Bales, Richard Haynes, Linda J. Sandell, and Jacqueline T. Hecht. "In vivo human Cartilage Oligomeric Matrix Protein (COMP) promoter activity." Matrix Biology 24, no. 8 (December 2005): 539–49. http://dx.doi.org/10.1016/j.matbio.2005.07.007.

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10

Nguyen, Q., G. Murphy, C. E. Hughes, J. S. Mort, and P. J. Roughley. "Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein." Biochemical Journal 295, no. 2 (October 15, 1993): 595–98. http://dx.doi.org/10.1042/bj2950595.

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The actions of human recombinant stromelysins-1 and -2, collagenase, gelatinases A and B and matrilysin on neonatal human proteoglycan aggregates were examined. With the exception of gelatinase B, aggrecan was degraded extensively by most metalloproteinases studied, whereas link protein showed only limited proteolysis. Sequencing studies of modified link protein components revealed that stromelysins-1 and -2, gelatinases A and B and collagenase cleaved specifically between His16 and Ile17, and matrilysin, stromelysin-2 and gelatinase A cleaved between Leu25 and Leu26. Cleavage at the former bond generated a link protein component with the same N-terminus as that isolated from newborn human cartilage. Based on previously determined in situ cleavage sites it is evident that matrix metalloproteinases are not solely responsible for the accumulation of link protein degradation products in adult human cartilage, indicating that additional proteolytic agents are involved in the normal catabolism of human cartilage matrix.

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11

Haleem-Smith, Hana, Raul Calderon, Yingjie Song, Rocky S. Tuan, and Faye H. Chen. "Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells." Journal of Cellular Biochemistry 113, no. 4 (February 23, 2012): 1245–52. http://dx.doi.org/10.1002/jcb.23455.

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12

Sun, GW, H. Kobayashi, M. Suzuki, N. Kanayama, and T. Terao. "Production of cartilage link protein by human granulosa-lutein cells." Journal of Endocrinology 175, no. 2 (November 1, 2002): 505–15. http://dx.doi.org/10.1677/joe.0.1750505.

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Link protein (LP), an extracellular matrix protein in cartilage, stabilizes aggregates of hyaluronic acid (HA) and proteoglycans, including aggrecan and inter-alpha-trypsin inhibitor (ITI). We have shown previously that cartilage LP is present in the maturing rat and mouse ovary. In the present study, we have employed immunohistochemistry to examine the anatomical distribution of cartilage LP in the human ovary. The expression of cartilage LP was selectively detected in the cells within the granulosa compartment of the preovulatory dominant follicle. The HA-positive granulosa-lutein cells were found to be a cartilage LP-positive subpopulation. We subsequently studied the in vitro expression of cartilage LP in cultured human granulosa-lutein cells obtained at oocyte retrieval for in vitro fertilization. Analysis of cultured cells by enzyme-linked immunoaffinity assay, Western blotting and immunofluorescence microscopy revealed that gonadotropin stimulates cartilage LP production. Time-course studies indicated that the cartilage LP production was induced as early as with gonadotropin stimulation for 2 h, and the effect was sustained up to 8 h. Western blot analysis further revealed the presence of the macroaggregates composed of HA, ITI and cartilage LP in the gonadotropin-stimulated granulosa-lutein cell extracts. Collectively, the present results raise the possibility that cartilage LP forms extracellular structures that may have a regulatory function in the developing follicle in the human ovary.

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Barter, Matt J., Wang Hui, Rachel L. Lakey, John B. Catterall, Tim E. Cawston, and David A. Young. "Lipophilic statins prevent matrix metalloproteinase-mediated cartilage collagen breakdown by inhibiting protein geranylgeranylation." Annals of the Rheumatic Diseases 69, no. 12 (August 6, 2010): 2189–98. http://dx.doi.org/10.1136/ard.2010.129197.

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ObjectiveTo investigate if statins prevent cartilage degradation and the production of collagenases and gelatinases in bovine nasal and human articular cartilage after proinflammatory cytokine stimulation.MethodsIn a cartilage degradation model, the effects of several statins were assessed by measuring proteoglycan degradation and collagen degradation, while collagenolytic and gelatinolytic activity in culture supernatants were determined by collagen bioassay and gelatin zymography. The production of matrix metalloproteinases (MMPs) in cartilage and chondrocytes were analysed by real-time reverse transcriptase PCR and immunoassay. Cytokine-induced signalling pathway activation was studied by immunoblotting.ResultsSimvastatin and mevastatin significantly inhibited interleukin 1 (IL-1)+oncostatin M (OSM)-induced collagen degradation; this was accompanied with a marked decrease in collagenase and gelatinase activity from bovine nasal cartilage. The cholesterol pathway intermediate mevalonic acid reversed the simvastatin-mediated protection of cartilage degradation, and the expression and production of collagenase (MMP-1 and MMP-13) and gelatinase (MMP-2 and MMP-9). Statins also significantly decreased MMP-1 and MMP-13 expression in human articular cartilage and chondrocytes stimulated with IL-1+OSM, and blocked the activation of critical proinflammatory signalling pathways required for MMP expression. The loss of the isoprenoid intermediate geranylgeranyl pyrophosphate due to statin treatment accounted for the inhibition of MMP expression and signalling pathway activation.ConclusionsThis study shows, for the first time, that lipophilic statins are able to block cartilage collagen breakdown induced by proinflammatory cytokines, by downregulating key cartilage-degrading enzymes. This demonstrates a possible therapeutic role for statins in acting as anti-inflammatory agents and in protecting cartilage from damage in joint diseases.

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Di Cesare, Paul E., Carrie Fang, Michael P. Leslie, Craig J. Della Valle, Julie M. Gold, Hermina Tulli, Roberto Perris, and Cathy S. Carlson. "Localization and Expression of Cartilage Oligomeric Matrix Protein by Human Rheumatoid and Osteoarthritic Synovium and Cartilage." Journal of Bone and Joint Surgery-American Volume 81, no. 10 (October 1999): 94. http://dx.doi.org/10.2106/00004623-199910000-00035.

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15

Cesare, Paul E. Di, Carrie Fang, Michael P. Leslie, Craig J. Della Valle, Julie M. Gold, Hermina Tulli, Roberto Perris, and Cathy S. Carlson. "Localization and expression of cartilage oligomeric matrix protein by human rheumatoid and osteoarthritic synovium and cartilage." Journal of Orthopaedic Research 17, no. 3 (May 1999): 437–45. http://dx.doi.org/10.1002/jor.1100170321.

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16

Posey, Karen L., Alka C. Veerisetty, Pieman Liu, Huiqiu R. Wang, Brian J. Poindexter, Roger Bick, Joseph L. Alcorn, and Jacqueline T. Hecht. "An Inducible Cartilage Oligomeric Matrix Protein Mouse Model Recapitulates Human Pseudoachondroplasia Phenotype." American Journal of Pathology 175, no. 4 (October 2009): 1555–63. http://dx.doi.org/10.2353/ajpath.2009.090184.

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17

Jenkins, R. N., S. L. Osborne-Lawrence, A. K. Sinclair, R. L. Eddy, M. G. Byers, T. B. Shows, and A. D. Duby. "Structure and chromosomal location of the human gene encoding cartilage matrix protein." Journal of Biological Chemistry 265, no. 32 (November 1990): 19624–31. http://dx.doi.org/10.1016/s0021-9258(17)45417-2.

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18

Deere, Michelle, Catherine Rhoades Hall, Kerry B. Gunning, Veronique LeFebvre, Amy L. Ridall, and Jacqueline T. Hecht. "Analysis of the promoter region of human cartilage oligomeric matrix protein (COMP)." Matrix Biology 19, no. 8 (January 2001): 783–92. http://dx.doi.org/10.1016/s0945-053x(00)00127-x.

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19

Chubinskaya, Susan, Charis Merrihew, Gabriella Cs-Szabo, Juergen Mollenhauer, John McCartney, David C. Rueger, and Klaus E. Kuettner. "Human Articular Chondrocytes Express Osteogenic Protein-1." Journal of Histochemistry & Cytochemistry 48, no. 2 (February 2000): 239–50. http://dx.doi.org/10.1177/002215540004800209.

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This study demonstrates for the first time that human articular chondrocytes express osteogenic protein-1 (OP-1). OP-1 was originally purified from bone matrix and was shown to induce cartilage and bone formation. Both OP-1 protein and message were present in human normal and osteoarthritic (OA) cartilages. OP-1 mRNA was upregulated in OA cartilage compared with normal adult tissues. However, the level of mature OP-1 protein in the same OA tissues was downregulated, whereas the pro-OP-1 remained high. Moreover, these two forms of OP-1 were localized in an inverted manner. Mature OP-1 was primarily detected in the superficial layer, whereas the pro-form was mostly in the deep layer of cartilage. The presence of pro- and mature OP-1 in extracts of normal and OA cartilages was confirmed by Western blotting. These findings imply that articular chondrocytes continue to express and synthesize OP-1 throughout adulthood. The observed patterns of the distribution of pro- and mature OP-1 also suggest differences in the processing of this molecule by normal and OA chondrocytes and by the cells in the superficial and deep layers. Distinct distribution of OP-1 and its potential activation in deep zones and regions of cloning in OA cartilages may provide clues to the potential involvement of endogenous OP-1 in repair mechanisms.

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20

Clements, Kristen M., Jo K. Flannelly, Jonathan Tart, Sarah M. V. Brockbank, John Wardale, Jim Freeth, Andrew E. Parker, and Peter Newham. "Matrix metalloproteinase 17 is necessary for cartilage aggrecan degradation in an inflammatory environment." Annals of the Rheumatic Diseases 70, no. 4 (January 7, 2011): 683–89. http://dx.doi.org/10.1136/ard.2010.130757.

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ObjectiveAggrecan is a critical component of cartilage extracellular matrix. Several members of the ‘a disintegrin and metalloproteinase with thrombospondin motifs’ (ADAMTS) family have been characterised as aggrecanases by their ability to generate fragments containing the NITEGE neoepitope from aggrecan. Increased NITEGE fragments in synovial fluid and articular cartilage are a hallmark of osteoarthritis (OA) and it is hypothesised that the enhanced rate of aggrecan degradation is critical for cartilage destruction in OA. Recently, matrix metalloproteinase 17 (MMP17, also known as MT4-MMP) has been implicated in the activation of one of the key aggrecanases: ADAMTS4. In the present work, the hypothesis that MMP17 mediates the interleukin 1β (IL-1β) induced release of NITEGE neoepitope from human and murine articular cartilage is investigated.MethodsMMP17 was quantified at the protein and RNA level and NITEGE neoepitope generation by immunohistochemistry. Human postmortem articular cartilage explants were treated with recombinant MMP17, or IL-1β in the presence or absence of an MMP17 inhibitor. Glycosaminoglycan (GAG) loss into the media was quantified using the 1,9-dimethylmethylene blue (DMMB) assay. Intra-articular injection (IAI) of IL-1β or meniscotibial ligament transaction was carried out in MMP17 null mice.ResultsThe data reveal an association between increased MMP17 protein and NITEGE staining in areas of OA cartilage damage. Ex vivo treatment of normal human cartilage with recombinant MMP17 protein increased NITEGE generation in the cartilage and GAG loss into the media. In addition, IL-1β mediated cartilage GAG loss, and increased NITEGE neoepitope expression, were attenuated with an MMP17 inhibitor.IAI of IL-1β into C57BL6/Jax mice resulted in increased MMP17 expression in articular cartilage and increased GAG content in the synovial fluid. MMP17 null mice were protected against this increase. However, aggrecan loss driven by mechanical stress following medial meniscotibial ligament transection was not dependent on MMP17.ConclusionThese data further implicate MMP17 in the control of articular cartilage extracellular matrix aggrecan integrity in an inflammatory environment.

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Di Cesare, Paul E., Cathy S. Carlson, Elliot S. Stolerman, Nik Hauser, Hermina Tulli, and Mats Paulsson. "Increased degradation and alteered tissue distribution of cartilage oligomeric matrix protein in human rheumatoid and osteoarthritic cartilage." Journal of Orthopaedic Research 14, no. 6 (November 1996): 946–55. http://dx.doi.org/10.1002/jor.1100140615.

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22

Camper, Lisbet, Dick Heinegård, and Evy Lundgren-Åkerlund. "Integrin α2β1 Is a Receptor for the Cartilage Matrix Protein Chondroadherin." Journal of Cell Biology 138, no. 5 (September 8, 1997): 1159–67. http://dx.doi.org/10.1083/jcb.138.5.1159.

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Chondroadherin (the 36-kD protein) is a leucine-rich, cartilage matrix protein known to mediate adhesion of isolated chondrocytes. In the present study we investigated cell surface proteins involved in the interaction of cells with chondroadherin in cell adhesion and by affinity purification. Adhesion of bovine articular chondrocytes to chondroadherin-coated dishes was dependent on Mg2+ or Mn2+ but not Ca2+. Adhesion was partially inhibited by an antibody recognizing β1 integrin subunit. Chondroadherin-binding proteins from chondrocyte lysates were affinity purified on chondroadherin-Sepharose. The β1 integrin antibody immunoprecipitated two proteins with molecular mass ∼110 and 140 kD (nonreduced) from the EDTA-eluted material. These results indicate that a β1 integrin on chondrocytes interacts with chondroadherin. To identify the α integrin subunit(s) involved in interaction of cells with the protein, we affinity purified chondroadherin-binding membrane proteins from human fibroblasts. Immunoprecipitation of the EDTA-eluted material from the affinity column identified α2β1 as a chondroadherin-binding integrin. These results are in agreement with cell adhesion experiments where antibodies against the integrin subunit α2 partially inhibited adhesion of human fibroblast and human chondrocytes to chondroadherin. Since α2β1 also is a receptor for collagen type II, we tested the ability of different antibodies against the α2 subunit to inhibit adhesion of T47D cells to collagen type II and chondroadherin. The results suggested that adhesion to collagen type II and chondroadherin involves similar or nearby sites on the α2β1 integrin. Although α2β1 is a receptor for both collagen type II and chondroadherin, only adhesion of cells to collagen type II was found to mediate spreading.

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Damerau, Alexandra, Moritz Pfeiffenberger, Marie-Christin Weber, Gerd-Rüdiger Burmester, Frank Buttgereit, Timo Gaber, and Annemarie Lang. "A Human Osteochondral Tissue Model Mimicking Cytokine-Induced Key Features of Arthritis In Vitro." International Journal of Molecular Sciences 22, no. 1 (December 24, 2020): 128. http://dx.doi.org/10.3390/ijms22010128.

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Adequate tissue engineered models are required to further understand the (patho)physiological mechanism involved in the destructive processes of cartilage and subchondral bone during rheumatoid arthritis (RA). Therefore, we developed a human in vitro 3D osteochondral tissue model (OTM), mimicking cytokine-induced cellular and matrix-related changes leading to cartilage degradation and bone destruction in order to ultimately provide a preclinical drug screening tool. To this end, the OTM was engineered by co-cultivation of mesenchymal stromal cell (MSC)-derived bone and cartilage components in a 3D environment. It was comprehensively characterized on cell, protein, and mRNA level. Stimulating the OTM with pro-inflammatory cytokines, relevant in RA (tumor necrosis factor α, interleukin-6, macrophage migration inhibitory factor), caused cell- and matrix-related changes, resulting in a significantly induced gene expression of lactate dehydrogenase A, interleukin-8 and tumor necrosis factor α in both, cartilage and bone, while the matrix metalloproteases 1 and 3 were only induced in cartilage. Finally, application of target-specific drugs prevented the induction of inflammation and matrix-degradation. Thus, we here provide evidence that our human in vitro 3D OTM mimics cytokine-induced cell- and matrix-related changes—key features of RA—and may serve as a preclinical tool for the evaluation of both new targets and potential drugs in a more translational setup.

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Dang, Quan Tran, Thao Duy Huynh, Francesco Inchingolo, Gianna Dipalma, Alessio Danilo Inchingolo, Stefania Cantore, Gregorio Paduanelli, et al. "Human Chondrocytes from Human Adipose Tissue-Derived Mesenchymal Stem Cells Seeded on a Dermal-Derived Collagen Matrix Sheet: Our Preliminary Results for a Ready to Go Biotechnological Cartilage Graft in Clinical Practice." Stem Cells International 2021 (February 23, 2021): 1–12. http://dx.doi.org/10.1155/2021/6664697.

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Background. The articular cartilage is unique in that it contains only a single type of cell and shows poor ability for spontaneous healing. Cartilage tissue engineering which uses mesenchymal stem cells (MSCs) and adipose tissue-derived mesenchymal stem cells (AT-MSCs) is considered an attractive treatment for cartilage lesions and osteoarthritis. The establishment of cartilage regenerative medicine is an important clinical issue, but the search for cell sources able to restore cartilage integrity proves to be challenging. The aim of this study was to create cartilage grafts from the combination of AT-MSCs and collagen substrates. Methods. Mesenchymal stem cells were obtained from human donors’ adipose tissue, and collagen scaffold, obtained from human skin and cleaned from blood vessels, adipose tissues, and debris, which only preserve dermis and epidermis, were seeded and cultured on collagen substrates and differentiated to chondrocytes. The obtained chondrocyte extracellular matrix of cartilage was then evaluated for the expression of chondrocyte-/cartilage-specific markers, the Cartilage Oligomeric Matrix Protein (COMP), collagen X, alpha-1 polypeptide (COL10A1), and the Collagen II, Human Tagged ORF Clone (COL2A1) by using the reverse transcription polymerase chain reaction (RT-PCR). Results. Our findings have shown that the dermal collagen may exert important effects on the quality of in vitro expanded chondrocytes, leading in this way that the influence of collagen skin matrix helps to produce highly active and functional chondrocytes for long-term cartilage tissue regeneration. Conclusion. This research opens up the possibility of generating cartilage grafts with the precise purpose of improving the existing limitation in current clinical procedures.

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Chawla, Shikha, Majoska H. M. Berkelaar, Boris Dasen, Christine Halleux, Sabine Guth-Gundel, Ina Kramer, Sourabh Ghosh, Ivan Martin, Andrea Barbero, and Paola Occhetta. "Blockage of bone morphogenetic protein signalling counteracts hypertrophy in a human osteoarthritic micro-cartilage model." Journal of Cell Science 133, no. 23 (December 1, 2020): jcs249094. http://dx.doi.org/10.1242/jcs.249094.

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ABSTRACTBone morphogenetic protein (BMP) signalling plays a significant role during embryonic cartilage development and has been associated with osteoarthritis (OA) pathogenesis, being in both cases involved in triggering hypertrophy. Inspired by recent findings that BMP inhibition counteracts hypertrophic differentiation of human mesenchymal progenitors, we hypothesized that selective inhibition of BMP signalling would mitigate hypertrophic features in OA cartilage. First, a 3D in vitro OA micro-cartilage model was established using minimally expanded OA chondrocytes that was reproducibly able to capture OA-like hypertrophic features. BMP signalling was then restricted by means of two BMP receptor type I inhibitors, resulting in reduction of OA hypertrophic traits while maintaining synthesis of cartilage extracellular matrix. Our findings open potential pharmacological strategies for counteracting cartilage hypertrophy in OA and support the broader perspective that key signalling pathways known from developmental processes can guide the understanding, and possibly the mitigation, of adult pathological features.

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26

Chubinskaya, Susan, Klaus Huch, Monika Schulze, Lori Otten, Margaret B. Aydelotte, and Ada A. Cole. "Gene Expression by Human Articular Chondrocytes Cultured in Alginate Beads." Journal of Histochemistry & Cytochemistry 49, no. 10 (October 2001): 1211–19. http://dx.doi.org/10.1177/002215540104901003.

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Culture of articular chondrocytes in alginate beads offers several advantages over culture in monolayer; cells retain their phenotype for 8 months or longer. Earlier studies of chondrocytes cultured in alginate concentrated on collagen and proteoglycan synthesis. However, gene expression by in situ hybridization (ISH) has not been investigated. The purposes of the present study on human chondrocytes were (a) to modify the ISH procedure for the alginate beads to examine the mRNA expression of α1 (II) procollagen, aggrecan, and two matrix metalloproteinases (MMP-3 and MMP-8) thought to be involved in cartilage matrix degradation, and (b) to compare expression in cultured chondrocytes with that in chondrocytes of intact human cartilage. The modifications made for ISH include the presence of CaCl2 and BaCl2 in the fixation and washing steps and exclusion of cetyl pyridinium chloride. By ISH we show that aggrecan, MMP-3, and MMP-8 are continuously expressed during 8 months of culture. The α1 (II) procollagen gene is expressed only during the first 2 months of culture and after 3 months its expression is undetectable, which is consistent with its absence in adult articular cartilage. By Western blotting, Type II collagen protein had been synthesized and deposited in both the cell-associated and further-removed matrix compartments at 7 and 14 days of culture. These data indicate that chondrocytes cultured in alginate beads could be preserved for immunohistochemistry and ISH and that culture of human chondrocytes in alginate beads may serve as a good model for studying cartilage-specific phenotype as well as factors that influence cartilage matrix turnover.

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Tsushima, Hidetoshi, Ken Okazaki, Mitsumasa Hayashida, Takahiro Ushijima, and Yukihide Iwamoto. "CCAAT/enhancer binding protein β regulates expression of matrix metalloproteinase-3 in arthritis." Annals of the Rheumatic Diseases 71, no. 1 (September 13, 2011): 99–107. http://dx.doi.org/10.1136/annrheumdis-2011-200061.

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ObjectivesTo investigate whether CCAAT/enhancer binding protein β (C/EBPβ) mediates the expression of matrix metalloproteinase-3 (MMP-3) and aggrecanases in arthritis.MethodsLocalisation of C/EBPβ and MMP-3 in synovium and cartilage from patients with rheumatoid arthritis and osteoarthritis was determined by immunohistochemistry. Cell lines SW982, C28/I2 and human fibroblast-like synoviocytes stimulated by interleukin 1β (IL-1β) were subjected to western blotting and quantitative PCR. Overexpression of C/EBPβ by adenovirus was performed in cells and organ culture of normal cartilage. Knockdown of C/EBPβ by small interference RNA was performed in cells. Activity of the human MMP-3 and aggrecanase-2 ADAMTS-5 (a disintegrin and metalloproteinase with thrombospondin motifs) promoters was analysed by a luciferase assay. To determine whether C/EBPβ directly binds to the MMP-3 or ADAMTS-5 promoter,a chromatin immunoprecipitation assay was performed.ResultsImmunohistochemistry showed that C/EBPβ and MMP-3 were co-localised in arthritic synovium and cartilage. Western blots revealed increased C/EBPβ expression in cells treated with IL-1β. Expression of MMP-3, MMP-13 and ADAMTS-5 mRNA was significantly increased by the overexpression of C/EBPβ. C/EBPβ stimulated MMP-3 expression and induced matrix degradation in cartilage explants. C/EBPβ knockdown reduced MMP-3 and ADAMTS-5 expression. C/EBPβ stimulated the 2011 bp MMP-3 promoter and the 1768 bp ADAMTS-5 promoter in a dose-dependent manner. Deletion and mutation analysis of the MMP-3 promoter showed that the C/EBPβ core responsive element was located between −108 bp and −100 bp. The chromatin immunoprecipitation assay showed that C/EBPβ was directly bound to MMP-3 and ADAMTS-5 promoters.ConclusionsThese data demonstrate that C/EBPβ is involved in expression of MMP-3 and ADAMTS-5 in arthritic synovium and cartilage.

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Huang, Yijiang, Daniel Seitz, Fabian König, Peter E. Müller, Volkmar Jansson, and Roland M. Klar. "Induction of Articular Chondrogenesis by Chitosan/Hyaluronic-Acid-Based Biomimetic Matrices Using Human Adipose-Derived Stem Cells." International Journal of Molecular Sciences 20, no. 18 (September 11, 2019): 4487. http://dx.doi.org/10.3390/ijms20184487.

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Cartilage repair using tissue engineering is the most advanced clinical application in regenerative medicine, yet available solutions remain unsuccessful in reconstructing native cartilage in its proprietary form and function. Previous investigations have suggested that the combination of specific bioactive elements combined with a natural polymer could generate carrier matrices that enhance activities of seeded stem cells and possibly induce the desired matrix formation. The present study sought to clarify this by assessing whether a chitosan-hyaluronic-acid-based biomimetic matrix in conjunction with adipose-derived stem cells could support articular hyaline cartilage formation in relation to a standard chitosan-based construct. By assessing cellular development, matrix formation, and key gene/protein expressions during in vitro cultivation utilizing quantitative gene and immunofluorescent assays, results showed that chitosan with hyaluronic acid provides a suitable environment that supports stem cell differentiation towards cartilage matrix producing chondrocytes. However, on the molecular gene expression level, it has become apparent that, without combinations of morphogens, in the chondrogenic medium, hyaluronic acid with chitosan has a very limited capacity to stimulate and maintain stem cells in an articular chondrogenic state, suggesting that cocktails of various growth factors are one of the key features to regenerate articular cartilage, clinically.

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BOLTON, Mark C., Jayesh DUDHIA, and Michael T. BAYLISS. "Age-related changes in the synthesis of link protein and aggrecan in human articular cartilage: implications for aggregate stability." Biochemical Journal 337, no. 1 (December 17, 1998): 77–82. http://dx.doi.org/10.1042/bj3370077.

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The rates of incorporation of radiolabelled leucine into aggrecan and link protein have been measured in human articular cartilage of different ages. Aggrecan and link protein were purified in the A1 fraction of CsCl gradients as a result of their ability to form high-buoyant-density proteoglycan aggregates with hyaluronic acid. Separation of the aggrecan from the link protein was achieved by Mono Q anion-exchange chromatography. The rates of synthesis of both aggrecan and link protein decreased with age. The age-related decrease in synthesis of aggrecan was paralleled by a decrease in the rate of sulphate incorporation into glycosaminoglycan chains. The synthesis of link protein decreased with age to a greater extent than that of aggrecan such that the ratio of the rates of link protein to aggrecan synthesis decreased from 1 in immature cartilage to 0.2 in mature cartilage. The age-related decrease in link protein synthesis is controlled at least in part by transcriptional or post-trancriptional mechanisms, as shown by the accompanying age-related decrease in link-protein mRNA. The absence of any age-related decrease in aggrecan mRNA suggests that the decrease in synthesis of aggrecan core protein is controlled by a translational mechanism. Measurement of the total tissue content of aggrecan and link protein by radioimmunoassay revealed an age-related increase in the accumulation of these matrix proteins, even though their de novo synthesis was decreasing. This illustrates the importance that the regulation of extracellular post-translational modification also has in controlling the overall turnover of the cartilage matrix.

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Struglics, André, and Maria Hansson. "MMP proteolysis of the human extracellular matrix protein aggrecan is mainly a process of normal turnover." Biochemical Journal 446, no. 2 (August 14, 2012): 213–23. http://dx.doi.org/10.1042/bj20120274.

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Although it has been shown that aggrecanases are involved in aggrecan degradation, the role of MMP (matrix metalloproteinase) aggrecanolysis is less well studied. To investigate MMP proteolysis of human aggrecan, in the present study we used neoepitope antibodies against MMP cleavage sites and Western blot analysis to identify MMP-generated fragments in normal and OA (osteoarthritis/osteoarthritic) cartilage, and in normal, knee injury and OA and SF (synovial fluid) samples. MMP-3 in vitro digestion showed that aggrecan contains six MMP cleavage sites, in the IGD (interglobular domain), the KS (keratan sulfate) region, the border between the KS region and CS (chondroitin sulfate) region 1, the CS1 region, and the border between the CS2 and the G3 domain, and kinetic studies showed a specific order of digestion where the cleavage between CS2 and the G3 domain was the most preferred. In vivo studies showed that OA cartilage contained (per dry weight) 3.4-fold more MMP-generated FFGV fragments compared with normal cartilage, and although aggrecanase-generated SF-ARGS concentrations were increased 14-fold in OA and knee-injured patients compared with levels in knee-healthy reference subjects, the SF-FFGV concentrations did not notably change. The results of the present study suggest that MMPs are mainly involved in normal aggrecan turnover and might have a less-active role in aggrecan degradation during knee injury and OA.

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Dodge, George R., David Hawkins, Eric Boesler, Lynn Sakai, and Sergio A. Jimenez. "Production of cartilage oligomeric matrix protein (COMP) by cultured human dermal and synovial fibroblasts." Osteoarthritis and Cartilage 6, no. 6 (November 1998): 435–40. http://dx.doi.org/10.1053/joca.1998.0147.

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Hecht, Jacqueline T., Michelle Deere, Elizabeth Putnam, William Cole, Barbara Vertel, Hui Chen, and Jack Lawler. "Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudochondroplasia musculoskeletal tissues." Matrix Biology 17, no. 4 (August 1998): 269–78. http://dx.doi.org/10.1016/s0945-053x(98)90080-4.

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Riessen, Reimer, Michael Fenchel, Hui Chen, Dorothea I. Axel, Karl R. Karsch, and Jack Lawler. "Cartilage Oligomeric Matrix Protein (Thrombospondin-5) Is Expressed by Human Vascular Smooth Muscle Cells." Arteriosclerosis, Thrombosis, and Vascular Biology 21, no. 1 (January 2001): 47–54. http://dx.doi.org/10.1161/01.atv.21.1.47.

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34

Hultman, Karin, Andreas Edsfeldt, Harry Björkbacka, Pontus Dunér, Lena Sundius, Mihaela Nitulescu, Ana Persson, et al. "Cartilage Oligomeric Matrix Protein Associates With a Vulnerable Plaque Phenotype in Human Atherosclerotic Plaques." Stroke 50, no. 11 (November 2019): 3289–92. http://dx.doi.org/10.1161/strokeaha.119.026457.

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35

Recklies, Anneliese D., Linon Baillargeon, and Chantal White. "Regulation of cartilage oligomeric matrix protein synthesis in human synovial cells and articular chondrocytes." Arthritis & Rheumatism 41, no. 6 (June 1998): 997–1006. http://dx.doi.org/10.1002/1529-0131(199806)41:6<997::aid-art6>3.0.co;2-g.

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36

Merritt, Thomas M., Joseph L. Alcorn, Richard Haynes, and Jacqueline T. Hecht. "Expression of mutant cartilage oligomeric matrix protein in human chondrocytes induces the pseudoachondroplasia phenotype." Journal of Orthopaedic Research 24, no. 4 (2006): 700–707. http://dx.doi.org/10.1002/jor.20100.

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37

Petrigna, Luca, Bruno Trovato, Federico Roggio, Alessandro Castorina, and Giuseppe Musumeci. "Molecular Assessment of Healthy Pathological Articular Cartilages in Physically Active People: A Scoping Review." International Journal of Molecular Sciences 24, no. 4 (February 11, 2023): 3662. http://dx.doi.org/10.3390/ijms24043662.

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Physiological aging triggers a cascade of negative effects on the human body and the human joint is only one of the several compartments affected by this irreversible and natural process. Osteoarthritis and cartilage degeneration can cause pain and disability; therefore, identifying the molecular processes underlying these phenomena and the biomarkers produced during physical activity is of critical importance. In the present review, the main goal was to identify and discuss the articular cartilage biomarkers analyzed in studies in which physical or sports activities were adopted and eventually to propose a standard operating procedure for the assessment. Articles collected from Pubmed, Web of Science, and Scopus were scrutinized to detect reliable cartilage biomarkers. The principal articular cartilage biomarkers detected in these studies were cartilage oligomeric matrix protein, matrix metalloproteinases, interleukins, and carboxy-terminal telopeptide. The articular cartilage biomarkers identified in this scoping review may aid in a better comprehension of where research on the topic is heading and offer a viable instrument for streamlining investigations on cartilage biomarker discovery.

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Stanescu, Victor, Thuc Pham Do, Françoise Chaminade, Pierre Maroteaux, and Ritta Stanescu. "Non-collagenous protein screening in the human chondrodysplasias: Link proteins, cartilage oligomeric matrix protein (COMP), and fibromodulin." American Journal of Medical Genetics 51, no. 1 (May 15, 1994): 22–28. http://dx.doi.org/10.1002/ajmg.1320510106.

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39

Froelich, C. J., X. Zhang, J. Turbov, D. Hudig, U. Winkler, and W. L. Hanna. "Human granzyme B degrades aggrecan proteoglycan in matrix synthesized by chondrocytes." Journal of Immunology 151, no. 12 (December 15, 1993): 7161–71. http://dx.doi.org/10.4049/jimmunol.151.12.7161.

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Abstract Cartilage degradation, a hallmark of rheumatoid arthritis, is attributed to serine and metalloproteases secreted by neutrophils, synovial lining cells, macrophages, and chondrocytes. A large proportion of synovial fluid lymphocytes contains the granule-associated serine proteases granzymes A and B. We report that lysates of IL-2-stimulated lymphocytes contain an enzymatic activity (ECMase; cartilage extracellular matrix 35S release assay; extracellular matrix degrading activity) that solubilizes matrix synthesized by chondrocyte monolayers. ECMase activity is inactivated by the serine protease inhibitor diisopropylfluorophosphate, is stored in dense granules and cleaves aggrecan proteoglycans but not free glycosaminoglycans, hyaluronic acid, or type II collagen. ECMase is mediated by a cationic protein with biochemical properties identical to granzyme B, inasmuch as it preferentially hydrolyzes the substrate Boc-Ala-Ala-Asp-SBzl, immunochemically cross-reacts with an antibody that binds to a conserved amino-terminal region of lymphoid-myeloid serine proteases, and has amino-terminal sequence identity with human Q31 granzyme B. Using an agarose gel electrophoresis technique to assess cleavage of the rat sarcoma aggrecan, the catalytic efficiency of granzyme B for the digestion of aggrecan (catalytic efficiency = 1.7 x 10(7) M-1 s-1) was 425-fold faster than the catalytic efficiency reported for human stromelysin-1 at pH 7.5 (catalytic efficiency 4000 M-1 s-1) and 3200-fold faster than granzyme A. Based on these observations, we propose that granzyme B, secreted from cytotoxic lymphocytes within the rheumatoid joint, may contribute to cartilage loss by degrading resident aggrecan.

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SZTROLOVICS, Robert, Anneliese D. RECKLIES, Peter J. ROUGHLEY, and John S. MORT. "Hyaluronate degradation as an alternative mechanism for proteoglycan release from cartilage during interleukin-1β-stimulated catabolism." Biochemical Journal 362, no. 2 (February 22, 2002): 473–79. http://dx.doi.org/10.1042/bj3620473.

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Data presented previously suggest that release of components of the cartilage matrix, in response to catabolic agents, cannot be accounted for by proteolytic mechanisms alone. In the present study, the release of glycosaminoglycan-containing components from bovine nasal cartilage cultured in the presence of interleukin-1β, and from bovine nasal, fetal bovine epiphyseal and adult human articular cartilage cultured in the presence of retinoic acid, was accompanied by the loss of link protein and hyaluronate into the culture medium. Chromatographic analysis of the released hyaluronate showed it to be markedly reduced in size relative to that extracted from the corresponding tissue. It is proposed that, under stimulation by catabolic agents, two independent, but concurrent, mechanisms act to promote the release of aggrecan from the cartilage matrix. First, proteolytic cleavage of the aggrecan core protein results in the production of glycosaminoglycan-containing fragments that are free to diffuse from the tissue. Secondly, cleavage of hyaluronate renders portions of the proteoglycan aggregate small enough so that complexes of aggrecan (or fragments containing its G1 domain) and link protein are released from the tissue. It is likely that both mechanisms contribute to cartilage metabolism in normal physiology and pathology.

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Firner, Sara, Frank Zaucke, Joern Michael, Jens Dargel, Karl-Heinz Schiwy-Bochat, Juliane Heilig, Markus Alexander Rothschild, Peer Eysel, Gert-Peter Brüggemann, and Anja Niehoff. "Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage." Journal of Histochemistry & Cytochemistry 65, no. 10 (August 28, 2017): 593–606. http://dx.doi.org/10.1369/0022155417729154.

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Perifibrillar adapter proteins, interconnecting collagen fibrils, and linking the collagen network with the aggrecan matrix seem to play a crucial role in the pathogenesis of osteoarthritis (OA). Therefore, we examined immunohistochemically the extracellular distribution of collagen II and the main perifibrillar adapter proteins—collagen IX, decorin, cartilage oligomeric matrix protein (COMP), and matrilin-3—in human samples of healthy (n=4) and OA (n=42) knee joint cartilage. Histopathology assessment was performed using an OA score. Staining patterns were evaluated in relation to the disease stage. The perifibrillar adapter proteins were uniformly distributed in the upper zones of healthy cartilage. In moderate OA (n=8; score 14.3 ± 4.7), all proteins analyzed were locally absent in the fibrillated area or the superficial and upper mid zone. In advanced OA (n=20; score 18.9 ± 5.3), they were uniformly distributed in these zones and accumulated pericellularly. Perifibrillar adapter proteins are important for the stabilization of the collagen network in the upper zones of healthy cartilage. Their degradation might be a critical event in early OA. In advanced OA, there are indications for an increased synthesis in an attempt to regenerate the lost tissue and to protect the remaining cartilage from further destruction.

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Archer, C. W., J. McDowell, M. T. Bayliss, M. D. Stephens, and G. Bentley. "Phenotypic modulation in sub-populations of human articular chondrocytes in vitro." Journal of Cell Science 97, no. 2 (October 1, 1990): 361–71. http://dx.doi.org/10.1242/jcs.97.2.361.

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Human articular cartilage has been separated into surface (approx. 15% of tissue depth) and deep zones (remaining tissue) and the constituent chondrocytes released by enzymic digestion. Subsequent culture either as a low density monolayer or as a suspension over agarose revealed distinct morphological and synthetic behaviour in the two populations. Whilst in monolayer these morphological differences disappeared with time in culture, over agarose they remained. Surface zone cells formed two types of cell cluster; one that was highly cellular with little extracellular matrix, and the other less frequent, which formed copious amounts of fibrillar matrix. Both types of cluster were surrounded by a layer of flattened chondrocytes. In contrast, deep cells formed a single cluster type that lacked a surrounding cell layer, but formed large amounts of sparse cartilage-like matrix and comprised morphologically typical chondrocytes. In monolayer, both populations gradually ceased to synthesise cartilage matrix components with the exception of link protein. In suspension, whilst the chondrogenic phenotype per se was preserved, there was, nevertheless, a loss in qualitative synthetic heterogeneity, which exists between surface and deep cells, that was not accompanied by changes in the differential rate of 35S incorporation into proteoglycan. Under these conditions, surface cells that normally do not synthesise keratan sulphate initiated de novo synthesis of this glycosaminoglycan. Consequently, it appears that the observed modulation in synthetic ability of the cell sub-populations is independent of the cluster morphology, which, once established, remains constant throughout the culture period.

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Böhm, B., R. Deutzmann, and H. Burkhardt. "Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions." Biochemical Journal 274, no. 1 (February 15, 1991): 269–73. http://dx.doi.org/10.1042/bj2740269.

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An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor (‘SLPI’). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.

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Amanatullah, Derek F., Jeffrey Lu, Jacqueline Hecht, Karen Posey, Jasper Yik, Paul E. Di Cesare, and Dominik R. Haudenschild. "Identification of a 3Kbp Mechanoresponsive Promoter Region in the Human Cartilage Oligomeric Matrix Protein Gene." Tissue Engineering Part A 18, no. 17-18 (September 2012): 1882–89. http://dx.doi.org/10.1089/ten.tea.2011.0497.

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Denton, Nathan, Katherine E. Pinnick, and Fredrik Karpe. "Cartilage oligomeric matrix protein is differentially expressed in human subcutaneous adipose tissue and regulates adipogenesis." Molecular Metabolism 16 (October 2018): 172–79. http://dx.doi.org/10.1016/j.molmet.2018.07.005.

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46

Vilı́m, Vladimı́r, Zdeněk Vobůrka, Richard Vytášek, Ladislav Šenolt, Ilja Tchetverikov, Virginia B. Kraus, and Karel Pavelka. "Monoclonal antibodies to human cartilage oligomeric matrix protein: epitope mapping and characterization of sandwich ELISA." Clinica Chimica Acta 328, no. 1-2 (February 2003): 59–69. http://dx.doi.org/10.1016/s0009-8981(02)00375-3.

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Melching, L. I., and P. J. Roughley. "A matrix protein of Mr 55 000 that accumulates in human articular cartilage with age." Biochimica et Biophysica Acta (BBA) - General Subjects 1036, no. 3 (December 1990): 213–20. http://dx.doi.org/10.1016/0304-4165(90)90037-w.

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48

Xu, Chuanying, Zhonghui Zhang, Mingyuan Wu, Shunying Zhu, Jin Gao, Jing Zhang, Yunsheng Yuan, Kejian Zhang, Yan Yu, and Wei Han. "Recombinant human midkine stimulates proliferation and decreases dedifferentiation of auricular chondrocytes in vitro." Experimental Biology and Medicine 236, no. 11 (November 2011): 1254–62. http://dx.doi.org/10.1258/ebm.2011.011022.

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Autologous chondrocyte implantation (ACI) is widely used for the repair of cartilage defects. However, due to the lack of chondrocyte growth factor and dedifferentiation of the cultured primary chondrocytes, cell source has limited the clinical potential of ACI. Auricular cartilage is an attractive potential source of cells for cartilage tissue engineering. Here we demonstrated that recombinant human midkine (rhMK) significantly promoted proliferation of rat primary auricular chondrocytes cultured and passaged in monolayer, which was mediated by the activation of mitogen-activated protein kinase and phosphoinositide 3-kinase pathways. Furthermore, rhMK attenuated the dedifferentiation of cultured chondrocytes by maintaining the expression of chondrocyte-specific matrix proteins during culture expansion and passage. Importantly, rhMK-expanded chondrocytes reserved their full chondrogenic potential and redifferentiated into elastic chondrocytes after being cultured in high density. The results suggest that rhMK may be used for the preparation of chondrocytes in cartilage tissue engineering.

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BOTTOMLEY, Kevin M., Neera BORKAKOTI, David BRADSHAW, Paul A. BROWN, Michael J. BROADHURST, John M. BUDD, Lucy ELLIOTT, et al. "Inhibition of bovine nasal cartilage degradation by selective matrix metalloproteinase inhibitors." Biochemical Journal 323, no. 2 (April 15, 1997): 483–88. http://dx.doi.org/10.1042/bj3230483.

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N-terminal analysis of aggrecan fragments lost from bovine nasal cartilage cultured in the presence of recombinant human interleukin 1α revealed a predominant ARGSVIL sequence with an additional ADLEX sequence. Production of the ARGSVIL-containing fragments has been attributed to the action of a putative proteinase, aggrecanase. The minor sequence (ADLEX) corresponds to a new reported cleavage product; comparison of this sequence with the available partial sequence of bovine aggrecan indicates that this is the product of a cleavage occurring towards the C-terminus of the protein. Matrix metalloproteinase (MMP) inhibitors inhibited aggrecan loss from bovine nasal explants incubated in the presence of recombinant human interleukin 1α. A strong correlation between inhibition of aggrecan metabolism and inhibition of stromelysin 1 (MMP 3) (r = 0.93) suggests a role for stromelysin or a stromelysin-like enzyme in cartilage aggrecan metabolism. However, the compounds were approx. 1/1000 as potent in inhibiting aggrecan loss from the cartilage explants as they were in inhibiting stromelysin. There was little or no correlation between inhibition of aggrecan metabolism and inhibition of gelatinase B (MMP 9) or inhibition of collagenase 1 (MMP 1). Studies with collagenase inhibitors with a range of potencies showed a correlation between inhibition of collagenase activity and inhibition of collagen degradation in the cartilage explant assay. This indicates that in interleukin 1α-driven bovine nasal cartilage destruction, stromelysin (or a closely related enzyme) is involved in aggrecan metabolism, whereas collagenase is principally responsible for collagen degradation.

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Mundlos, S., B. Schwahn, T. Reichert, and B. Zabel. "Distribution of osteonectin mRNA and protein during human embryonic and fetal development." Journal of Histochemistry & Cytochemistry 40, no. 2 (February 1992): 283–91. http://dx.doi.org/10.1177/40.2.1552170.

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We investigated the temporal and spatial distribution of osteonectin during human embryonic and fetal development, using in situ hybridization and immunohistochemistry. Osteonectin gene expression was generally found in cells exhibiting high rates of matrix production/proliferation. In mineralized tissue, a strong signal was obtained in osteoblasts, odontoblasts, and chondrocytes of the upper hypertrophic and proliferative zones. Chondrocytes of the mineralized zone showed no expression throughout the different stages of development. Strong osteonectin expression was found in odontoblasts of developing teeth. In addition, osteonectin mRNA and protein were detected in several non-mineralized tissues: steroid-producing cells of the adrenal gland and the gonads, kidney (glomeruli), lung (bronchi), skin, megacaryocytes, and large vessels. Histochemistry confirmed the results and detected extracellular osteonectin in bone and in the zone of mineralized cartilage only. The localization of osteonectin in bone, cartilage, and teeth is consistent with a role in the initiation of mineralization. However, the organ-specific distribution in non-mineralized tissues suggests an important multifunction role of this protein during human development.

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