A Selective Extracellular Matrix Proteomics Approach Identifies Fibronectin Proteolysis by A Disintegrin-like and Metalloprotease Domain with Thrombospondin Type 1 Motifs (ADAMTS16) and Its Impact on Spheroid Morphogenesis

Schnellmann, Rahel; Sack, Ragna; Heß, Daniel; Annis, Douglas S.; Mosher, Deane F.; Apte, Suneel S.; Chiquet‐Ehrismann, Ruth

doi:10.1074/mcp.ra118.000676

Cited by 35 publications

(32 citation statements)

References 47 publications

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“…In relation to other ADAMTSs, ADAMTS16 inhibits Fn fibrillogenesis and cleaves Fn, releasing a 30 Da N-terminal heparin-binding Fn-fs, which in turn, upregulates MMP-3, which is also able to cleave Fn, generating new Fn-fs and inducing a positive degradative feedback loop in an epithelial cell line [207]. Additionally, ADAMTS9 is involved in Fn turnover and fibrillogenesis in ECM remodeling during mouse embryogenesis [208].…”

Section: Fn-fs Modifies Adamts Expression and Signalingmentioning

confidence: 99%

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Pérez‐García

Carrión

Gutiérrez‐Cañas

et al. 2019

Cells

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The extracellular matrix (ECM) is a complex and specialized three-dimensional macromolecular network, present in nearly all tissues, that also interacts with cell surface receptors on joint resident cells. Changes in the composition and physical properties of the ECM lead to the development of many diseases, including osteoarthritis (OA). OA is a chronic degenerative rheumatic disease characterized by a progressive loss of synovial joint function as a consequence of the degradation of articular cartilage, also associated with alterations in the synovial membrane and subchondral bone. During OA, ECM-degrading enzymes, including urokinase-type plasminogen activator (uPA), matrix metalloproteinases (MMPs), and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs), cleave ECM components, such as fibronectin (Fn), generating fibronectin fragments (Fn-fs) with catabolic properties. In turn, Fn-fs promote activation of these proteinases, establishing a degradative and inflammatory feedback loop. Thus, the aim of this review is to update the contribution of ECM-degrading proteinases to the physiopathology of OA as well as their modulation by Fn-fs.

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Section: Fn-fs Modifies Adamts Expression and Signalingmentioning

confidence: 99%

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Pérez‐García

Carrión

Gutiérrez‐Cañas

et al. 2019

Cells

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“…We have previously reported that Adamts18 is required for eye, lung and female reproductive tract and kidney development in the mouse 18 . It is highly homologous to Adamts16, which has a role in renal development and fertility 19,20 and can cleave fibronectin 21 . Here, we show that Adamts18 provides a mechanistic link between epithelial steroid hormone receptor signaling and changes in the ECM, in particular the BM, that regulate mammary epithelial stemness.…”

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confidence: 99%

The secreted protease Adamts18 links hormone action to activation of the mammary stem cell niche

et al. 2020

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Estrogens and progesterone control breast development and carcinogenesis via their cognate receptors expressed in a subset of luminal cells in the mammary epithelium. How they control the extracellular matrix, important to breast physiology and tumorigenesis, remains unclear. Here we report that both hormones induce the secreted protease Adamts18 in myoepithelial cells by controlling Wnt4 expression with consequent paracrine canonical Wnt signaling activation. Adamts18 is required for stem cell activation, has multiple binding partners in the basement membrane and interacts genetically with the basal membranespecific proteoglycan, Col18a1, pointing to the basement membrane as part of the stem cell niche. In vitro, ADAMTS18 cleaves fibronectin; in vivo, Adamts18 deletion causes increased collagen deposition during puberty, which results in impaired Hippo signaling and reduced Fgfr2 expression both of which control stem cell function. Thus, Adamts18 links luminal hormone receptor signaling to basement membrane remodeling and stem cell activation.

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“…Until about a decade ago, no substrates were reported for the ADAMTS proteases that form the central clade of the ADAMTS homology tree, i.e., ADAMTS6,7,10,12,16,17,18,and 19, and these ADAMTS proteases were considered "orphan" [6][7][8]. However, more recent work identified several substrates for these proteases, many of them are linked to fibrillin biology, such as fibrillin-1 and fibrillin-2 themselves, several latent transforming growth factor (TGF) β binding proteins (LTBPs), fibronectin, or ADAMTS-like 6 [9][10][11][12][13]. The consilience between evolutionary conservation and functionally related ECM substrates suggests that at least some of these ADAMTS proteases perform biological roles related to the formation or function of fibrillin microfibrils [14].…”

Section: The Adamts Protease Familymentioning

confidence: 99%

The ADAMTS/Fibrillin Connection: Insights into the Biological Functions of ADAMTS10 and ADAMTS17 and Their Respective Sister Proteases

et al. 2020

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Secreted a disintegrin-like and metalloprotease with thrombospondin type 1 motif (ADAMTS) proteases play crucial roles in tissue development and homeostasis. The biological and pathological functions of ADAMTS proteases are determined broadly by their respective substrates and their interactions with proteins in the pericellular and extracellular matrix. For some ADAMTS proteases, substrates have been identified and substrate cleavage has been implicated in tissue development and in disease. For other ADAMTS proteases, substrates were discovered in vitro, but the role of these proteases and the consequences of substrate cleavage in vivo remains to be established. Mutations in ADAMTS10 and ADAMTS17 cause Weill–Marchesani syndrome (WMS), a congenital syndromic disorder that affects the musculoskeletal system (short stature, pseudomuscular build, tight skin), the eyes (lens dislocation), and the heart (heart valve abnormalities). WMS can also be caused by mutations in fibrillin-1 (FBN1), which suggests that ADAMTS10 and ADAMTS17 cooperate with fibrillin-1 in a common biological pathway during tissue development and homeostasis. Here, we compare and contrast the biochemical properties of ADAMTS10 and ADAMTS17 and we summarize recent findings indicating potential biological functions in connection with fibrillin microfibrils. We also compare ADAMTS10 and ADAMTS17 with their respective sister proteases, ADAMTS6 and ADAMTS19; both were recently linked to human disorders distinct from WMS. Finally, we propose a model for the interactions and roles of these four ADAMTS proteases in the extracellular matrix.

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A Selective Extracellular Matrix Proteomics Approach Identifies Fibronectin Proteolysis by A Disintegrin-like and Metalloprotease Domain with Thrombospondin Type 1 Motifs (ADAMTS16) and Its Impact on Spheroid Morphogenesis

Cited by 35 publications

References 47 publications

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

The secreted protease Adamts18 links hormone action to activation of the mammary stem cell niche

The ADAMTS/Fibrillin Connection: Insights into the Biological Functions of ADAMTS10 and ADAMTS17 and Their Respective Sister Proteases

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