The transglutaminase, Factor XIIIA, is present in articular chondrocytes

Rosenthal, Ann K.; Masuda, Ikuko; Gohr, Claudia M.; Derfus, Beth A.; Le, Min

doi:10.1053/joca.2000.0423

Cited by 43 publications

(37 citation statements)

References 13 publications

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“…Chondrocytes have the capacity to release FXIIIA Nurminskaya et al, 2002;Rosenthal et al, 2001). In this study, we identified novel functional implications of upregulation of FXIIIA expression and release in both the growth plate chondrocyte hypertrophic differentiation program and in OA cartilage chondrocytes Nurminskaya and Linsenmayer, 1996).…”

Section: Discussionmentioning

confidence: 85%

Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation

Johnson

Rose

Terkeltaub

2008

Journal of Cell Science

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Two transglutaminases (TGs), factor XIIIA (FXIIIA) and TG2, undergo physiologic upregulation in growth plate hypertrophic chondrocytes, and pathological upregulation in osteoarthritic cartilage. Externalization of guanine-nucleotide-bound TG2 drives chondrocyte maturation to hypertrophy, a state linked to matrix remodeling and calcification. Here, we tested the hypothesis that FXIIIA also promotes hypertrophic differentiation. Using human articular chondrocytes, we determined that extracellular FXIIIA induced chondrocyte hypertrophy associated with rapid movement of TG2 to the cell surface. Site-directed mutagenesis revealed that FXIIIA Pro37 bordering the thrombin endoproteolytic Arg38-Gly39 site, but not intrinsic TG catalytic activity, were necessary for FXIIIA to induce chondrocyte hypertrophy. TGs have been demonstrated to interact with certain integrins and, during osteoarthritis (OA), α1β1 integrin is upregulated and associated with hypertrophic chondrocytes. FXIIIA engaged α1β1 integrin in chondrocytes. Antibody crosslinking of α1β1 integrin mobilized TG2. Conversely, an α1β1-integrin-specific blocking antibody inhibited the capacity of FXIIIA to induce TG2 mobilization to the cell surface, phosphorylation of p38 MAP kinase, and chondrocyte hypertrophy. Our results identify a unique functional network between two cartilage TG isoenzymes that accelerates chondrocyte maturation without requirement for TG-catalyzed transamidation by either TG.

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Section: Discussionmentioning

confidence: 85%

Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation

Johnson

Rose

Terkeltaub

2008

Journal of Cell Science

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“…To date, the transglutaminase family consists of 9 different TG genes (2). Tissue transglutaminase (TG2, type II) is one of the best-characterized, skeletal tissue-related TGs (3,4) and may be involved in the initiation of mineralization and play an important role in ossification (5,6). …”

Section: Introductionmentioning

confidence: 99%

Tissue transglutaminase (TG2) activity regulates osteoblast differentiation and mineralization in the SAOS-2 cell line

Yin

Chen

Liu

et al. 2012

Braz J Med Biol Res

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Tissue transglutaminase (type II, TG2) has long been postulated to directly promote skeletal matrix calcification and play an important role in ossification. However, limited information is available on the expression, function and modulating mechanism of TG2 during osteoblast differentiation and mineralization. To address these issues, we cultured the well-established human osteosarcoma cell line SAOS-2 with osteo-inductive conditioned medium and set up three time points (culture days 4, 7, and 14) to represent different stages of SAOS-2 differentiation. Osteoblast markers, mineralization, as well as TG2 expression and activity, were then assayed in each stage. Furthermore, we inhibited TG activity with cystamine and then checked SAOS-2 differentiation and mineralization in each stage. The results showed that during the progression of osteoblast differentiation SAOS-2 cells presented significantly high levels of osteocalcin (OC) mRNA, bone morphogenetic protein-2 (BMP-2) and collagen I, significantly high alkaline phosphatase (ALP) activity, and the increased formation of calcified matrix. With the same tendency, TG2 expression and activity were up-regulated. Furthermore, inhibition of TG activity resulted in a significant decrease of OC, collagen I, and BMP-2 mRNA and of ALP activity and mineralization. This study demonstrated that TG2 is involved in osteoblast differentiation and may play a role in the initiation and regulation of the mineralization processes. Moreover, the modulating effects of TG2 on osteoblasts may be related to BMP-2.

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“…Transglutaminase activates latent TGF-β to increase chondrocyte ePPi production. Two dominant forms of transglutaminase have been identified in articular cartilage-type II transglutaminase and factor XIIIA [24]. Interleukin-1-beta (as well as tumor necrosis factor-alpha, donors of nitric oxide, and the potent oxidant peroxynitrite) induces increased chondrocyte transglutaminase activity [20].…”

Section: Calcification Mechanism: Role Of Extracellular Inorganic Pyrmentioning

confidence: 99%

Calcium pyrophosphate dihydrate and basic calcium phosphate crystalinduced arthropathies: Update on pathogenesis, clinical features, and Therapy

Ea¹,

Lioté

2004

Curr Rheumatol Rep

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Calcium-containing crystals are the most common class for the osteoarthritic joint. They are responsible for acute periarthritis and destructive arthropathies, and for tissue deposits mimicking tumor-like masses. These crystals encompassed mainly calcium pyrophosphate dihydrate and basic calcium phosphate crystals, with the latter being related to hydroxyapatite, carbonate-substituted apatite, and octacalcium phosphate. Calcification deposit mechanisms will be reviewed with respect to extracellular inorganic pyrophosphate dysregulation mainly caused by modulation of specific membrane channel disorders. Genetic defects have been extensively studied and identified mutation of specific genes such as ANKH and COL. Pathogenesis of crystal-induced inflammation is related to synovial tissue and direct cartilage activation. Besides classical knee or wrist pseudogout attacks or Milwaukee shoulder arthropathies, clinicians should be aware of other specific common presentations, such as erosive calcifications, spinal cord compression by intraspinal masses, ligamentum flavum calcification, or atypical calcified tophus. Promising clinical results for preventing calcium crystal deposits and cartilage degradation are lacking. Practical imaging tools are needed to monitor reduction of calcification of fibrocartilage and articular cartilage as markers of drug efficacy.

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The transglutaminase, Factor XIIIA, is present in articular chondrocytes

Abstract: FXIIIA is present in articular chondrocytes. FXIIIA levels correlate with TGase activity in chondrocytes. The presence of two forms of TGase in articular chondrocytes suggest an important function for this enzyme family in articular cartilage.

Cited by 43 publications

References 13 publications

Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation

Factor XIIIA mobilizes transglutaminase 2 to induce chondrocyte hypertrophic differentiation

Tissue transglutaminase (TG2) activity regulates osteoblast differentiation and mineralization in the SAOS-2 cell line

Calcium pyrophosphate dihydrate and basic calcium phosphate crystalinduced arthropathies: Update on pathogenesis, clinical features, and Therapy

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