ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions

Cain, Stuart A.; Mularczyk, Ewa J.; Singh, Mukti; Massam-Wu, Teresa; Kielty, Cay M.

doi:10.1038/srep35956

Cited by 56 publications

(85 citation statements)

References 44 publications

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“…; Cain et al . ). Supplementation of cultured bovine nuchal ligament fibroblasts with medium containing recombinantly expressed ADAMTS10 accelerated deposition of microfibrils; in comparison, fibroblasts from a WMS patient deposited few microfibrils (Kutz et al .…”

Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

“…Another explanation for how ADAMTS10 stimulates microfibril deposition was revealed in our recent study (Cain et al . ). Purified recombinant ADAMTS10 and its closest homologue, ADAMTS6, both bound fibrillin‐1, heparin and syndecan‐4 ectodomain.…”

Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

“…Notably, in these epithelial cultures, ADAMTS10 was expressed at extremely low levels (Cain et al . ). It was also not detected in a proteomic analysis of zonules, despite the fact that ectopia lentis is often a feature of WMS (De Maria et al .…”

Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

“…; Hubmacher & Apte, ; Cain et al . ), and it colocalizes with microfibrils in the papillary dermis (Kutz et al . ).…”

Section: Microfibril‐associated Moleculesmentioning

confidence: 99%

“…Its close homologue ADAMTS6 (Cain et al . ) and related ADAMTSL4 (Gabriel et al . ) and ADAMTSL6 (Tsutsui et al .…”

Section: Microfibril‐associated Moleculesmentioning

confidence: 99%

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Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

2017

Int J Experimental Path

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SummaryFibrillin microfibrils are indispensable structural elements of connective tissues in multicellular organisms from early metazoans to humans. They have an extensible periodic beaded organization, and support dynamic tissues such as ciliary zonules that suspend the lens. In tissues that express elastin, including blood vessels, skin and lungs, microfibrils support elastin deposition and shape the functional architecture of elastic fibres. The vital contribution of microfibrils to tissue form and function is underscored by the heritable fibrillinopathies, especially Marfan syndrome with severe elastic, ocular and skeletal tissue defects. Research since the early 1990s has advanced our knowledge of biology of microfibrils, yet understanding of their mechanical and homeostatic contributions to tissues remains far from complete. This review is a personal reflection on key insights, and puts forward the conceptual hypothesis that microfibrils are structural ‘tensometers’ that direct cells to monitor and respond to altered tissue mechanics.

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Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

Section: How Might Hs‐rich Cell Surface Zones Influence Microfibril Dmentioning

confidence: 97%

“…; Hubmacher & Apte, ; Cain et al . ), and it colocalizes with microfibrils in the papillary dermis (Kutz et al . ).…”

Section: Microfibril‐associated Moleculesmentioning

confidence: 99%

“…Its close homologue ADAMTS6 (Cain et al . ) and related ADAMTSL4 (Gabriel et al . ) and ADAMTSL6 (Tsutsui et al .…”

Section: Microfibril‐associated Moleculesmentioning

confidence: 99%

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Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

2017

Int J Experimental Path

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ADAMTSL6β promotes fibrillin‐1 microfibril assembly, which is possibly mediated via binding through the third thrombospondin type I domain to fibrillin‐1

Orimoto

Fukuda

2020

Cell Biology International

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Fibrillin‐1 is the major component of extracellular matrix microfibrils. Microfibrils dysfunction is responsible for the onset of various connective tissue diseases, including Marfan syndrome. Although ADAMTSL (a disintegrin and metalloproteinase with thrombospondin motifs‐like) 6β is one of the fibrillin‐1 binding proteins, the detailed mechanism underlying the involvement of ADAMTSL6β in microfibril formation remains unclear. In this study, we created deletion mutants of ADAMTSL6β and examined their interactions with fibrillin‐1 assembly. Pull‐down assay of the ADAMTSL6β deletion mutants and fibrillin‐1 protein revealed that ADAMTSL6β binds to fibrillin‐1 through the third thrombospondin type I domain. Furthermore, we observed that formation of fibrillin‐1 matrix assembly was enhanced in MG63 cells, expressing full‐length ADAMTSL6β, when compared with that of wild type MG63 cells. While MG63 cells expressing Δ TSP3‐ADAMTSL6β form showed enhanced assembly formation, Δ TSP2‐ADAMTSL6β form did not enhance that, indicating the difference between Δ TSP2‐Δ TSP3 has a critical role for fibrillin‐1 assembly. As the difference of Δ TSP2‐Δ TSP3 is the third thrombospondin type I domain, we concluded that the third thrombospondin type I domain of ADAMTSL6β influence the microfibril formation. Our data are the functional presentation of the biological role of ADAMTSL6β in the process of microfibril formation.

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Reversion‐inducing cysteine‐rich protein with Kazal motifs and MT1‐MMP promote the formation of robust fibrillin fibers

Matsuzaki

Keene

Nishimoto

et al. 2020

Journal Cellular Physiology

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Fibrillins (FBNs) form mesh-like structures of microfibrils in various elastic tissues. RECK and FBN1 are co-expressed in many human tissues, suggesting a functional relationship. We found that dermal FBN1 fibers show atypical morphology in mice with reduced RECK expression (RECK-Hypo mice). Dermal FBN1 fibers in micelacking membrane-type 1-matrix metalloproteinase (MT1-MMP) show a similar atypical morphology, despite the current notion that MT1-MMP (a membranebound protease) and RECK (a membrane-bound protease inhibitor) have opposing functions. Our experiments using dermal fibroblasts indicated that RECK promotes pro-MT1-MMP activation, increases cell-associated gelatinase/collagenase activity, and decreases diffusible gelatinase/collagenase activity, while MT1-MMP stabilizes RECK in these cells. Experiments using purified proteins indicate that RECK and its binding partner ADAMTS10 keep the proteolytic activity of MT1-MMP within a certain range. These findings suggest that RECK, ADAMTS10, and MT1-MMP cooperate to support the formation of robust FBN1 fibers.

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ADAMTS-10 and -6 differentially regulate cell-cell junctions and focal adhesions

Cited by 56 publications

References 44 publications

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

Fell‐Muir Lecture: Fibrillin microfibrils: structural tensometers of elastic tissues?

ADAMTSL6β promotes fibrillin‐1 microfibril assembly, which is possibly mediated via binding through the third thrombospondin type I domain to fibrillin‐1

Reversion‐inducing cysteine‐rich protein with Kazal motifs and MT1‐MMP promote the formation of robust fibrillin fibers

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