Microarray analysis of differential gene expression in temporomandibular joint condylar cartilage after experimentally induced osteoarthritis

Meng, Juan-Hong; Ma, Xiaoxuan; Ma, Dalong; Xu, Caimin

doi:10.1016/j.joca.2005.03.010

Cited by 68 publications

(54 citation statements)

References 36 publications

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“…More specifi cally, it is possible that similar molecular pathways that are activated during OA cause a different outcome in the TMJ compared with the knee. For example, in both OA of the TMJ and OA of other joints, it has been reported that there is an increase in apoptosis [Aigner et al, 2004;Meng et al, 2005]. However, in the healthy mandibular condylar cartilage, there is a percentage of cells that normally undergo apoptosis [Huang et al, 2004].…”

Section: Differences In the Progression Of Oa In The Knee And Tmj In mentioning

confidence: 99%

Mice Deficient in Biglycan and Fibromodulin as a Model for Temporomandibular Joint Osteoarthritis

Wadhwa¹,

Embree²,

Ameye³

et al. 2005

Cells Tissues Organs

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The temporomandibular joint (TMJ) within the craniofacial complex is unique. In humans, the TMJ can become diseased resulting in severe and disabling pain. There are no cures for TMJ disease at this time. Animal models of TMJ disease are scarce, but some exist, and they are described in this paper. We present in greater detail one animal model that is deficient in two extracellular matrix (ECM) proteoglycans, biglycan (BGN) and fibromodulin (FMOD). Doubly deficient BGN/FMOD mice develop premature TMJ osteoarthritis (OA). In order to explore the mechanistic basis of TMJ-OA, tissues from the condyle of mutant mice were examined for their relative capacity to differentiate and undergo apoptosis. Our data show that there is a redistribution of the critical ECM protein, type II collagen, in mutant mice compared with controls. Mutant mice also have increased apoptosis of the chondrocytes embedded in the articular cartilage. We speculate that the overall imbalance in apoptosis may be the cellular basis for the abnormal production of structural ECM proteins. The abnormal production of the ECM could, in turn, lead to premature erosion and degradation of the articular surface resulting in TMJ-OA. These data underscore the importance of the ECM in controlling the structural integrity of the TMJ.

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Section: Differences In the Progression Of Oa In The Knee And Tmj In mentioning

confidence: 99%

Mice Deficient in Biglycan and Fibromodulin as a Model for Temporomandibular Joint Osteoarthritis

Wadhwa¹,

Embree²,

Ameye³

et al. 2005

Cells Tissues Organs

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“…However, the regulatory mechanisms responsible for these alterations have not yet been clarified. It is abundantly clear that gene expression is regulated by genetic alterations such as mutations and by epigenetic mechanisms such as alterations in the DNA methylation status, covalent modifications of core nucleosomal histones and rearrangement of histones 6 7. DNA hypermethylation and histone hypoacetylation are hallmarks of gene silencing, while DNA hypomethylation and acetylated histones, specifically in histone H3 at lysines 9 and 14, promote active gene transcription 8 – 11.…”

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confidence: 99%

Epigenetic regulation of leptin affects MMP-13 expression in osteoarthritic chondrocytes: possible molecular target for osteoarthritis therapeutic intervention

Iliopoulos

Malizos

Tsezou

2007

Annals of the Rheumatic Diseases

178

114

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Objective: To investigate whether epigenetic mechanisms can regulate leptin's expression and affect its downstream targets as metalloproteinases 3,9,13 in osteoarthritic chondrocytes. Methods: DNA methylation in leptin promoter was measured by DNA bisulfite sequencing, and mRNA expression levels were measured by real-time quantitative PCR in osteoarthritic as well as in normal cartilage. Osteoarthritic articular cartilage samples were obtained from two distinct locations of the knee (n = 15); from the main defective area of maximum load (advanced osteoarthritis (OA)) and from adjacent macroscopically intact regions (minimal OA). Using small interference RNA, we tested if leptin downregulation would affect matrix metalloproteinase (MMP)-13 activity. We also evaluated the effect of the demethylating agent, 59-Aza-2-deoxycytidine (AZA) and of the histone deacetylase inhibitor trichostatin A (TSA) on leptin expression in chondrocyte cultures. Furthermore, we performed chromatin immunoprecipitation in leptin's promoter area. Results: We found a correlation between leptin expression and DNA methylation and also that leptin controls MMP-13 activity in chondrocytes. Leptin's downregulation with small interference RNA inhibited MMP-13 expression dramatically. After 5-AZA application in normal chondrocytes, leptin's methylation was decreased, while its expression was upregulated, and MMP-13 was activated. Furthermore, TSA application in normal chondrocyte cultures increased leptin's expression. Also, chromatin immunoprecipitation in leptin's promoter after TSA treatment revealed that histone H3 lysines 9 and 14 were acetylated. Conclusion: We found that epigenetic mechanisms regulate leptin's expression in chondrocytes affecting its downstream target MMP-13. Small interference RNA against leptin deactivated directly MMP-13, which was upregulated after leptin's epigenetic reactivation, raising the issue of leptin's therapeutic potential for osteoarthritis.

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“…It has been considered that, in addition to its normal physiological functions, AQP3 might play a role in the pathophysiology of various diseases. Increased expression of AQP3 mRNA and the presence of AQP3 proteins in different localizations in OA cartilage indicate that they have important roles in OA pathogenesis [24]. Expression of aquaporin in various tissues changes with age.…”

Section: Discussionmentioning

confidence: 99%

Investigation of Age-Related Changes in Expression of Aquaporin-1 and Aquaporin-3 in Rat Bone

Sapmaz¹

2016

Ann Clin Anal Med

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ÖzetAmaç: Aquaporinler su ve iyon transportu sağlayan membran kanal proteinleridir. Yaşlanma ile dokulardaki aquaporinlerin miktarı değişmektedir. Aquaporin-1 (AQP1) ve aquaporin-3 (AQP3)'ün kıkırdak dokuda yaşlanma ile azaldığı gösterilmiştir. Ancak kemik dokuda yaşlanma ile aquaporinlerin miktarında değişim gösterilmemiştir. Bu çalışmada genç ve yaşlı hayvanların kemik dokularında AQP1, AQP3 ve tip I kollajen ekspresyonlarının immünohis-tokimyasal olarak araştırılması amaçlandı. Gereç ve Yöntem: Bu çalışmada 14 adet Wistar Albino cinsi sıçan kullanıldı. Grup I (n=7) iki aylık genç sıçan-lardan, Grup II (n=7) onsekiz aylık yaşlı sıçanlardan oluşmaktaydı. Kemik dokusu (femur) histopatolojik ve immunohistokimyasal değerlendirme için alın-dı. Rutin histolojik prosedürün ardından parafine gömülen dokulardan 4-5 µm kalınlığında kesitler alındı. İmmunohistokimyasal olarak AQP1, AQP3 ve tip I kollajen boyama ayrıca Hematoksilen-eozin boyama yapıldı. Bulgular: Genç ve yaşlı sıçanlarda immünohistokimyasal olarak AQP1, AQP3 ve tip I kollajen ekspresyonu gösterildi. Yaşlanma ile AQP1, AQP3 ve tip I kollajen miktarında azalma olduğu gözlendi. Tartışma: AQP1 ve AQP3 mik tarındaki azalmanın kemik dokuda yaşa bağlı değişikliklerle ilgili olabilece ği kanaatindeyiz. Anahtar KelimelerSıçan; Kemik Dokusu; Yaşlanma; Aquaporin 1; Aquaporin 3 Özet Aim: Aquaporins are membrane channel proteins that transport water and ions. The amount of aquaporins in tissue changes with age. The amount of aquaporin-1 (AQP1) and aquaporin-3 (AQP3) is considered to decrease in cartilage tissue with age. However, no age-related change has been reported regarding the amount of aquaporins in bone tissue. In this study, our aim was to examine expressions of AQP1, AQP3, and type I collagen immunohistochemically in the bone tissues of young and old rats. Material and Method: Fourteen Wistar Albino rats were included in this study. Group I (n=7) consisted of young rats that were two months old, while Group II (n=7) consisted of old rats that were eighteen months old. Bone tissue (femur) was dissected and examined histopathologically and immunohistochemically. After routine histological procedure, sections at 4-5 µm thickness were obtained from tissues embedded in paraffin. Sections were stained immunohistochemically for AQP1, AQP3, and type I collagen as well as with hematoxylin-eosin. Results: Immunohistochemically, expressions of AQP1, AQP3, and type I collagen were demonstrated in both young and old rats. AQP1, AQP3, and type I collagen amounts were found to decrease with aging. Discussion: Our findings suggest that reduced amounts of AQP1 and AQP3 may be related to agerelated changes in bone tissue.

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Microarray analysis of differential gene expression in temporomandibular joint condylar cartilage after experimentally induced osteoarthritis

Abstract: This study provides a new gene expression profile of the progression of OA. Further study of these OA-related genes may provide new insights into understanding the molecular mechanisms underlying OA.

Cited by 68 publications

References 36 publications

Mice Deficient in Biglycan and Fibromodulin as a Model for Temporomandibular Joint Osteoarthritis

Mice Deficient in Biglycan and Fibromodulin as a Model for Temporomandibular Joint Osteoarthritis

Epigenetic regulation of leptin affects MMP-13 expression in osteoarthritic chondrocytes: possible molecular target for osteoarthritis therapeutic intervention

Investigation of Age-Related Changes in Expression of Aquaporin-1 and Aquaporin-3 in Rat Bone

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