Simone D. Scilabra
ISMETT
Matrix metalloproteinaseLigand (biochemistry)Membrane proteinCellMolecular biologyThrombospondinReceptorChemistryExtracellular matrixTransmembrane proteinAggrecanaseOsteoarthritisADAMTSCell membraneDisintegrinADAM10ADAM15CartilageProteolysisEndocytosisExtracellularADAMTS4 ProteinLDL receptorBiochemistryMetalloproteinaseEndocytic cycleBiologyCell biology
26Publications
8H-index
467Citations
Publications 17
Newest
#1Anna Paola Carreca (ISMETT)H-Index: 7
#2Veronica M. Pravata (Dund.: University of Dundee)H-Index: 4
Last. Simone D. Scilabra (ISMETT)H-Index: 8
view all 9 authors...
Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial...
1 CitationsSource
#2Doretta Cuffaro (UniPi: University of Pisa)H-Index: 5
Last. Simone D. Scilabra (ISMETT)H-Index: 8
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For decades, disintegrin and metalloproteinase 17 (ADAM17) has been the object of deep investigation. Since its discovery as the tumor necrosis factor convertase, it has been considered a major drug target, especially in the context of inflammatory diseases and cancer. Nevertheless, the development of drugs targeting ADAM17 has been harder than expected. This has generally been due to its multifunctionality, with over 80 different transmembrane proteins other than tumor necrosis factor α (TNF) b...
7 CitationsSource
#1C.Y. Yang (University of Oxford)H-Index: 1
#2Anastasios Chanalaris (University of Oxford)H-Index: 15
Last. Stephan A. Müller (TUM: Technische Universität München)H-Index: 7
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Abstract Objective The adamalysin metalloproteinase 15 (ADAM15) has been shown to protect against development of osteoarthritis in mice. Here, we have investigated factors that control ADAM15 levels in cartilage. Design Secretomes from wild-type and Adam15−/− chondrocytes were compared by label-free quantitative mass spectrometry. mRNA was isolated from murine knee joints, either with or without surgical induction of osteoarthritis on male C57BL/6 mice, and the expression of Adam15 and other rel...
1 CitationsSource
#1Anna Paola Carreca (ISMETT)H-Index: 7
#2Veronica M. Pravata (Dund.: University of Dundee)H-Index: 4
Last. Simone D. Scilabra (ISMETT)H-Index: 8
view all 8 authors...
Matrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in extracellular matrix (ECM) turnover and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocytosed by the low-de...
5 CitationsSource
#1Chun-Yao Yang (Arthritis Research UK)
#2Linda Troeberg (Arthritis Research UK)H-Index: 28
Last. Simone D. Scilabra (ISMETT)H-Index: 8
view all 3 authors...
: Cell surface proteolysis controls numerous biological processes including cell-cell attachment and the communication between cells. The membrane-tethered families of matrix metalloproteinases (MT-MMPs) and disintegrin metalloproteinases (ADAMs) are major enzymes involved in the cleavage of molecules at the cell surface, and their activity is finely regulated by their endogenous inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). The biological function of a metalloproteinase close...
Source
#1Anna Paola Carreca (ISMETT)H-Index: 7
#2Veronica M. Pravata (Dund.: University of Dundee)H-Index: 4
Last. Simone D. Scilabra (ISMETT)H-Index: 8
view all 6 authors...
Matrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in the turnover of extracellular matrix (ECM) components and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocyt...
Source
#1Hung-En Hsia (TUM: Technische Universität München)H-Index: 4
#2Johanna Tüshaus (TUM: Technische Universität München)H-Index: 5
Last. Stefan F. Lichtenthaler (TUM: Technische Universität München)H-Index: 43
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‘A disintegrin and metalloproteases’ (ADAMs) are a family of transmembrane proteins with diverse functions in multicellular organisms. About half of the ADAMs are active metalloproteases and cleave numerous cell surface proteins, including growth factors, receptors, cytokines and cell adhesion proteins. The other ADAMs have no catalytic activity and function as adhesion proteins or receptors. Some ADAMs are ubiquitously expressed, others are expressed tissue specifically. This review highlights ...
31 CitationsSource
#1Simone D. Scilabra (TUM: Technische Universität München)H-Index: 8
#2Martina Pigoni (German Center for Neurodegenerative Diseases)H-Index: 7
Last. Stefan F. LichtenthalerH-Index: 43
view all 7 authors...
The tissue inhibitor of metalloproteinases-3 (TIMP-3) is a major regulator of extracellular matrix turnover and protein shedding by inhibiting different classes of metalloproteinases, including disintegrin metalloproteinases (ADAMs). Tissue bioavailability of TIMP-3 is regulated by the endocytic receptor low-density-lipoprotein receptor-related protein-1 (LRP-1). TIMP-3 plays protective roles in disease. Thus, different approaches have been developed aiming to increase TIMP-3 bioavailability, ye...
13 CitationsSource
#1Simone D. Scilabra (Nagoya University)H-Index: 8
#2Kazuhiro Yamamoto (University of Oxford)H-Index: 17
Last. Kenji Kadomatsu (Nagoya University)H-Index: 74
view all 10 authors...
Tissue inhibitor of metalloproteinases 3 (TIMP-3) is a key regulator of extracellular matrix turnover for its ability to inhibit matrix metalloproteinases (MMPs), adamalysin-like metalloproteinases (ADAMs) and ADAMs with thrombospondin motifs (ADAMTSs). TIMP-3 is a secreted protein whose extracellular levels are regulated by endocytosis via the low-density-lipoprotein receptor-related protein-1 (LRP-1). In this study we developed a molecule able to "trap" TIMP-3 extracellularly, thereby increasi...
14 CitationsSource