Transglutaminase activity arising from Factor XIIIA is required for stabilization and conversion of plasma fibronectin into matrix in osteoblast cultures

Cui, Cui; Wang, Shuai; Myneni, Vamsee D.; Hitomi, Kiyotaka; Kaartinen, Mari T.

doi:10.1016/j.bone.2013.11.006

Cited by 44 publications

(36 citation statements)

References 57 publications

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“…4). The conversion into DOC-insoluble FN fibrils is based on strong, non-covalent protein-protein interactions47 and other factors such as extracellular transglutaminase-catalyzed crosslinking activity48 and intermolecular disulfide bonding, catalyzed by the intrinsic protein disulfide isomerase activity of FN49. All these factors might be affected by sHA1, and thus prevent the formation of DOC-insoluble FN fibers.…”

Section: Discussionmentioning

confidence: 99%

Sulfated hyaluronan alters fibronectin matrix assembly and promotes osteogenic differentiation of human bone marrow stromal cells

Vogel

Arnoldini

Möller

et al. 2016

Sci Rep

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Extracellular matrix (ECM) composition and structural integrity is one of many factors that influence cellular differentiation. Fibronectin (FN) which is in many tissues the most abundant ECM protein forms a unique fibrillary network. FN homes several binding sites for sulfated glycosaminoglycans (sGAG), such as heparin (Hep), which was previously shown to influence FN conformation and protein binding. Synthetically sulfated hyaluronan derivatives (sHA) can serve as model molecules with a well characterized sulfation pattern to study sGAG-FN interaction. Here is shown that the low-sulfated sHA (sHA1) interacts with FN and influences fibril assembly. The interaction of FN fibrils with sHA1 and Hep, but not with non-sulfated HA was visualized by immunofluorescent co-staining. FRET analysis of FN confirmed the presence of more extended fibrils in human bone marrow stromal cells (hBMSC)-derived ECM in response to sHA1 and Hep. Although both sHA1 and Hep affected FN conformation, exclusively sHA1 increased FN protein level and led to thinner fibrils. Further, only sHA1 had a pro-osteogenic effect and enhanced the activity of tissue non-specific alkaline phosphatase. We hypothesize that the sHA1-triggered change in FN assembly influences the entire ECM network and could be the underlying mechanism for the pro-osteogenic effect of sHA1 on hBMSC.

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Section: Discussionmentioning

confidence: 99%

Sulfated hyaluronan alters fibronectin matrix assembly and promotes osteogenic differentiation of human bone marrow stromal cells

Vogel

Arnoldini

Möller

et al. 2016

Sci Rep

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“…Cui et al demonstrated in osteoblast cultures that Factor XIII catalyzed the cross-linking of fibronectin from serum (plasma fibronectin; pFn), as opposed to the EDA-splice variant of fibronectin endogenously expressed by osteoblasts (cellular Fn; cFn) [33]. Formation of a cross-linked fibronectin matrix derived from pFn was required for subsequent deposition and assembly of a collagen network.…”

Section: Transglutaminasementioning

confidence: 99%

“…Formation of a cross-linked fibronectin matrix derived from pFn was required for subsequent deposition and assembly of a collagen network. Inhibition of Factor XIII activity, but not that of TG2, decreased collagen deposition and mineralization in osteoblast cultures [33]. Hence, cross-linking of pFn by Factor XIII was predicted to be an essential phase of bone formation that precedes collagen deposition.…”

Section: Transglutaminasementioning

confidence: 99%

SPARC/osteonectin in mineralized tissue

2016

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Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM40) is one of the most abundant non-collagenous protein expressed in mineralized tissues. This review will focus on elucidating functional roles of SPARC in bone formation building upon results from non-mineralized cells and tissues, the phenotype of SPARC-null bones, and recent discoveries of human diseases with either dysregulated expression of SPARC or mutations in the gene encoding SPARC that give rise to bone pathologies. The capacity of SPARC to influence pathways involved in extracellular matrix assembly such as procollagen processing and collagen fibril formation as well as the capacity to influence osteoblast differentiation and osteoclast activity will be addressed. In addition, the potential for SPARC to regulate cross-linking of extracellular matrix proteins by members of the transglutaminase family of enzymes is explored. Elucidating defined biological functions of SPARC in terms of bone formation and turnover are critical. Further insight into specific cellular mechanisms involved in the formation and homeostasis of mineralized tissues will lead to a better understanding of disease progression.

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“…We have shown previously that FXIII-A is produced by osteoblasts and is externalized to the extracellular matrix where its function has been linked to the stabilization of plasma fibronectin matrix (Al-Jallad et al 2006Cui et al 2014;Piercy-Kotb et al 2011). Cell-associated FXIII-A resides on the extracellular side of the osteoblast plasma membrane where it appears to facilitate the formation of high-molecular weight detyrosinated Glu-tubulin, which is linked to the secretion and elaboration of collagenous extracellular matrix in these cells ).…”

Section: Introductionmentioning

confidence: 99%

“…The best known and most studied catalytic function of TG enzymes is the protein transamidation reaction that occurs between a protein-bound glutamine residue and a protein-bound lysine or primary amine, resulting in the formation of a γ-glutamyl-ε-lysyl crosslink, also referred to as an isopeptide bond. This crosslinking in certain extracellular matrix substrate proteins has been reported to stabilize both collagenous and 597964J HCXXX10.1369/0022155415597964Wang and KaartinenFactor XIII-A Is Found in Caveolae research-article2015 noncollagenous extracellular matrices (Al-Jallad et al 2006;Akagi et al 2002;Cui et al 2014;Esposito and Caputo 2005;Hohenadl et al 1995;Kaartinen et al 2002). The crosslinking is also essential for cornified cell envelope formation in terminal keratinocyte differentiation, where covalent crosslinking occurs in proteins such as involucrin, loricrin, and small proline-rich protein (Eckert et al 2005;Hitomi 2005).…”

Section: Introductionmentioning

confidence: 99%

Cellular Factor XIIIA Transglutaminase Localizes in Caveolae and Regulates Caveolin-1 Phosphorylation, Homo-oligomerization and c-Src Signaling in Osteoblasts

Wang

Kaartinen

2015

J Histochem Cytochem.

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SummaryTransglutaminases (TGs) are a family of widely distributed enzymes that catalyze protein crosslinking by forming a covalent isopeptide bond between the substrate proteins. We have shown that MC3T3-E1 osteoblasts express Factor XIII-A (FXIII-A), and that the extracellular crosslinking activity of FXIII-A is involved in regulating matrix secretion and deposition. In this study, we have investigated the localization and potential role of intracellular FXIII-A. Conventional immunofluorescence microscopy and TIRF microscopy analyses showed that FXIII-A co-localizes with caveolin-1 in specialized membrane structures, caveolae, in differentiating osteoblasts. The caveolae-disrupting agent methyl-β-cyclodextrin abolished FXIII-A staining and co-localization with caveolin-1 from the osteoblast plasma membrane. The presence of FXIII-A in caveolae was confirmed by preparing caveolae-enriched cellular fractions using sucrose density gradient ultracentrifugation followed by western blotting. Despite this association of FXIII-A with caveolae, there was no detectable transglutaminase activity in caveolae, as measured by monodansylcadaverine incorporation. TG inhibitor NC9-which can alter TG enzyme conformation-localized to caveolae and displaced FXIII-A from these structures when added to the osteoblast cultures. The decreased FXIII-A levels in caveolae after NC9 treatment increased c-Src activation, which resulted in caveolin-1 phosphorylation, homo-oligomerization and Akt phosphorylation, suggesting cellular FXIII-A has a role in regulating c-Src signaling in osteoblasts. (J Histochem Cytochem 63:829-841, 2015)

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Transglutaminase activity arising from Factor XIIIA is required for stabilization and conversion of plasma fibronectin into matrix in osteoblast cultures

Cited by 44 publications

References 57 publications

Sulfated hyaluronan alters fibronectin matrix assembly and promotes osteogenic differentiation of human bone marrow stromal cells

Sulfated hyaluronan alters fibronectin matrix assembly and promotes osteogenic differentiation of human bone marrow stromal cells

SPARC/osteonectin in mineralized tissue

Cellular Factor XIIIA Transglutaminase Localizes in Caveolae and Regulates Caveolin-1 Phosphorylation, Homo-oligomerization and c-Src Signaling in Osteoblasts

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