All-trans retinoic acid-induced ADAM28 degrades proteoglycans in human chondrocytes

Hikichi, Yuichi; Yoshimura, Koji; Takigawa, Masaharu

doi:10.1016/j.bbrc.2009.06.052

Cited by 12 publications

(8 citation statements)

References 29 publications

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“…ADAM28 is a member of the ADAM (a disintegrin and metalloprotease domain) family. ADAM28 induced by all-trans retinoic acid can degrade both bovine and human proteoglycans in chondrocytes [25], which suggests that ADAM28 may be a new aggrecanase. Given that chondronecrosis in the deep zone of articular cartilage and growth plate cartilage is the key feature of KBD, ADAM28 may play a role in cartilage degradation of KBD patients.…”

Section: Discussionmentioning

confidence: 99%

Genome-Wide Gene Expression Analysis Suggests an Important Role of Suppressed Immunity in Pathogenesis of Kashin-Beck Disease

Wang

Guo

et al. 2012

PLoS ONE

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ObjectiveTo investigate the differences between the gene expression profiles in peripheral blood mononuclear cells (PBMC) from normal controls and patients with Kashin-Beck disease (KBD).MethodsTwenty KBD patients and 12 normal subjects were selected from a KBD-endemic area and divided into four pairs of KBD vs. control (KBD, n = 5 per pair; control, n = 3 per pair). RNAs were respectively isolated from KBD PBMCs and normal PBMCs. Gene expression profiles were analyzed by oligonucleotide microarray. The gene expression profiles in PBMCs from KBD patients and normal controls were compared and the differentially expressed genes were identified. The obtained microarray data was further confirmed by using quantitative real-time reverse transcription polymerase chain reaction (qRT-PCR).ResultsApproximately 501 genes, corresponding to 2.4% of the total probe transcripts, showed a 2-fold change in differential expression. 19.4% (97 out of 501)of the differentially expressed genes were commonly detected in all the four pairs. Among the 97 differentially expressed genes, 83 genes were up-regulated and 14 genes were down-regulated, compared with those in the normal controls. Some differentially expressed genes were found to be related to functions such as immunity, metabolism, apoptosis, cystoskeleton and cell movement, and extracellular matrix. The validity of our microarray data were supported by the results of qRT-PCR assay.ConclusionDifferences in the PBMC gene expression profile between the KBD patients and the normal controls exhibited a similar pattern among all the four pairs of microarrays examined, indicating that the suppressed immunity may play an important role in the pathogenesis of KBD.

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Section: Discussionmentioning

confidence: 99%

Genome-Wide Gene Expression Analysis Suggests an Important Role of Suppressed Immunity in Pathogenesis of Kashin-Beck Disease

Wang

Guo

et al. 2012

PLoS ONE

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“…The enzyme has been suggested to promote retinoic acid-stimulated proteoglycan degradation 93 , although the molecular mechanism for this observation has not been established. Known substrates of ADAM28 include TNF 94 and growth factors such as IGF binding protein-3 95 and connective tissue growth factor (CTGF) 96 .…”

Section: Adamtssmentioning

confidence: 99%

ADAMTS and ADAM metalloproteinases in osteoarthritis – looking beyond the ‘usual suspects’

Yang

Chanalaris

Troeberg

2017

Osteoarthritis and Cartilage

228

164

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SummaryIntroductionMatrix metalloproteinases (MMPs) and ‘aggrecanase’ a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs) are well established to play key roles in osteoarthritis (OA) through degradation of extracellular matrix (ECM) type II collagen and aggrecan, and are thus potential targets for development of OA therapies.ObjectiveThis paper aims to provide a comprehensive review of the expression and potential roles of other, lesser-known ADAMTSs and related adamalysins (or a disintegrin and metalloproteinases (ADAMs)) in cartilage, with a view to identifying potentially protective or homeostatic metalloproteinases in the joint and informing consequent selective inhibitor design.DesignA comprehensive literature search was performed using PubMed terms ‘osteoarthritis’ and ‘ADAMTS’ or ‘ADAM’.ResultsSeveral ADAMTSs and ADAMs were identified as having reportedly increased expression in OA. These include enzymes likely to play roles in cartilage matrix anabolism (e.g., the procollagen N-proteinases ADAMTS-2, ADAMTS-3 and ADAMTS-14), chondrocyte differentiation and proliferation (e.g., ADAM9, ADAM10, ADAM12), as well as enzymes contributing to cartilage catabolism (e.g., Cartilage oligomeric protein (COMP)-degrading ADAMTS-7 and ADAMTS-12).ConclusionsIn addition to the well-characterised MMPs, ADAMTS-4 and ADAMTS-5, many other ADAMTSs and ADAMs are expressed in cartilage and several show significantly altered expression in OA. Studies aimed at elucidating the pathophysiological roles of these enzymes in cartilage will contribute to our understanding of OA pathogenesis and enable design of targeted inhibitors that effectively target metalloproteinase-mediated cartilage degradation while sparing cartilage repair pathways.

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“…ADAM-28, a membrane-bound protease, enhances chondrocytes releasing proteoglycan (Hikichi et al 2009). The activity of ADAM-28 is recently linked to the malignancy of chondrosarcoma (Matsuura et al 2010) and other cancers (Mochizuki and Okada 2009).…”

Section: Discussionmentioning

confidence: 98%

A proteomic approach for identification and localization of the pericellular components of chondrocytes

Zhang

Beckett

et al. 2011

Histochem Cell Biol

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Although the pericellular matrix (PCM) plays a central role in the communication between chondrocytes and extracellular matrix, its composition is largely unknown. In this study, the PCM was investigated with a proteomic approach using chondrons, which are enzymatically isolated constructs including the chondrocyte and its surrounding PCM. Chondrons and chondrocytes alone were isolated from human articular cartilage. Proteins extracted from chondrons and chondrocytes were used for two-dimensional electrophoresis. Protein spots were quantitatively compared between chondron and chondrocyte gels. Cellular proteins, which had similar density between chondron and chondrocyte gels, did not proceed for analysis. Since chondrons only differ from chondrocytes in association of the PCM, protein spots in the chondron gels that had higher quantity than that in the chondrocyte gels were selected as candidates of the PCM components and processed for mass spectrometry. Among 15 identified peptides, several were fragments of the three type VI collagen chains (α-1, α-2, and α-3). Other identified PCM proteins included triosephosphate isomerase, transforming growth factor-β induced protein, peroxiredoxin-4, ADAM (A disintegrin and metalloproteinases) 28, and latent-transforming growth factor beta-binding protein-2. These PCM components were verified with immunohisto(cyto)chemistry for localization in the PCM region of articular cartilage. The abundance of type VI collagen in the PCM emphasizes its importance to the microenvironment of chondrocytes. Several proteins were localized in the PCM of chondrocytes for the first time and that warrants further investigation for their functions in cartilage biology.

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All-trans retinoic acid-induced ADAM28 degrades proteoglycans in human chondrocytes

Cited by 12 publications

References 29 publications

Genome-Wide Gene Expression Analysis Suggests an Important Role of Suppressed Immunity in Pathogenesis of Kashin-Beck Disease

Genome-Wide Gene Expression Analysis Suggests an Important Role of Suppressed Immunity in Pathogenesis of Kashin-Beck Disease

ADAMTS and ADAM metalloproteinases in osteoarthritis – looking beyond the ‘usual suspects’

A proteomic approach for identification and localization of the pericellular components of chondrocytes

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