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Article ; Online: A personal journey with matrix metalloproteinases.

Nagase, Hideaki

2016 Volume 397, Issue 9, Page(s) 805–813

Abstract: I was given the honor of delivering the 2015 Lifetime Membership Award lecture at the International Proteolysis Society's annual meeting held in Penang, Malaysia in October 2015. It gave me an opportunity to look back on how I started my research on ... ...

Abstract	I was given the honor of delivering the 2015 Lifetime Membership Award lecture at the International Proteolysis Society's annual meeting held in Penang, Malaysia in October 2015. It gave me an opportunity to look back on how I started my research on matrix metalloproteinases (MMPs) and how I continued to work on these proteinases for the next 42 years. This is a series of sketches from the personal journey that I took with MMPs, starting from the purification of metalloproteinases, cloning, structural studies, then to a more recent encounter, endocytic regulation of matrix-degrading metalloproteinases.
MeSH term(s)	Biochemistry/history ; Cartilage/enzymology ; Cloning, Molecular ; DNA, Complementary/genetics ; History, 20th Century ; History, 21st Century ; Humans ; Matrix Metalloproteinase Inhibitors/pharmacology ; Matrix Metalloproteinases/chemistry ; Matrix Metalloproteinases/genetics ; Matrix Metalloproteinases/metabolism
Chemical Substances	DNA, Complementary ; Matrix Metalloproteinase Inhibitors ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2016-09-01
Publishing country	Germany
Document type	Historical Article ; Journal Article
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2016-0169
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Article ; Online: Measurement of Protease Activities Using Fluorogenic Substrates.

Santamaria, Salvatore / Nagase, Hideaki

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1731, Page(s) 107–122

Abstract: Matrix metalloproteinases and the related metalloproteases are implicated in cancer progression. They are endopeptidases that require several defined amino acid residues in both N-terminal and C-terminal sides of the scissile bond. Fluorogenic Förster ... ...

Abstract	Matrix metalloproteinases and the related metalloproteases are implicated in cancer progression. They are endopeptidases that require several defined amino acid residues in both N-terminal and C-terminal sides of the scissile bond. Fluorogenic Förster resonance energy transfer (FRET) substrates that harbor a fluorophore and a quencher on opposite sides of the scissile bond are conveniently used to measure their activities. In this chapter, we describe the principle of FRET substrates and how to use them to measure activities and kinetic parameters of endopeptidases.
MeSH term(s)	ADAMTS4 Protein/analysis ; ADAMTS4 Protein/genetics ; ADAMTS4 Protein/metabolism ; Amino Acid Sequence ; Enzyme Assays/instrumentation ; Enzyme Assays/methods ; Fluorescence Resonance Energy Transfer/instrumentation ; Fluorescence Resonance Energy Transfer/methods ; Fluorescent Dyes/chemistry ; Fluorescent Dyes/metabolism ; Kinetics ; Mutation ; Proteolysis ; Recombinant Proteins/analysis ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Substrate Specificity
Chemical Substances	Fluorescent Dyes ; Recombinant Proteins ; ADAMTS4 Protein (EC 3.4.24.82) ; ADAMTS4 protein, human (EC 3.4.24.82)
Language	English
Publishing date	2018-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7595-2_11
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Article ; Online: ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary α

Kadurin, Ivan / Dahimene, Shehrazade / Page, Karen M / Ellaway, Joseph I J / Chaggar, Kanchan / Troeberg, Linda / Nagase, Hideaki / Dolphin, Annette C

Function (Oxford, England)

2022 Volume 3, Issue 3, Page(s) zqac013

Abstract: The auxiliary ... ...

Abstract	The auxiliary α
MeSH term(s)	Humans ; Tissue Inhibitor of Metalloproteinase-3/metabolism ; Calcium Channels, N-Type/genetics ; Proteolysis ; Calcium, Dietary/metabolism ; Neuralgia ; Peptide Hydrolases/metabolism ; ADAM17 Protein/genetics
Chemical Substances	Tissue Inhibitor of Metalloproteinase-3 ; Calcium Channels, N-Type ; Calcium, Dietary ; Peptide Hydrolases (EC 3.4.-) ; ADAM17 protein, human (EC 3.4.24.86) ; ADAM17 Protein (EC 3.4.24.86)
Language	English
Publishing date	2022-03-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2633-8823
ISSN (online)	2633-8823
DOI	10.1093/function/zqac013
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Article ; Online: LRP1 Controls TNF Release via the TIMP-3/ADAM17 Axis in Endotoxin-Activated Macrophages.

Schubert, Kristin / Collins, Laura E / Green, Patricia / Nagase, Hideaki / Troeberg, Linda

Journal of immunology (Baltimore, Md. : 1950)

2019 Volume 202, Issue 5, Page(s) 1501–1509

Abstract: The metalloproteinase ADAM17 plays a pivotal role in initiating inflammation by releasing TNF from its precursor. Prolonged TNF release causes many chronic inflammatory diseases, indicating that tight regulation of ADAM17 activity is essential for ... ...

Abstract	The metalloproteinase ADAM17 plays a pivotal role in initiating inflammation by releasing TNF from its precursor. Prolonged TNF release causes many chronic inflammatory diseases, indicating that tight regulation of ADAM17 activity is essential for resolution of inflammation. In this study, we report that the endogenous ADAM17 inhibitor TIMP-3 inhibits ADAM17 activity only when it is bound to the cell surface and that cell surface levels of TIMP-3 in endotoxin-activated human macrophages are dynamically controlled by the endocytic receptor LRP1. Pharmacological blockade of LRP1 inhibited endocytic clearance of TIMP-3, leading to an increase in cell surface levels of the inhibitor that blocked TNF release. Following LPS stimulation, TIMP-3 levels on the surface of macrophages increased 4-fold within 4 h and continued to accumulate at 6 h, before a return to baseline levels at 8 h. This dynamic regulation of cell surface TIMP-3 levels was independent of changes in TIMP-3 mRNA levels, but correlated with shedding of LRP1. These results shed light on the basic mechanisms that maintain a regulated inflammatory response and ensure its timely resolution.
MeSH term(s)	ADAM17 Protein/antagonists & inhibitors ; ADAM17 Protein/immunology ; Cells, Cultured ; Endotoxins/pharmacology ; Humans ; Lipopolysaccharides/pharmacology ; Low Density Lipoprotein Receptor-Related Protein-1/antagonists & inhibitors ; Low Density Lipoprotein Receptor-Related Protein-1/immunology ; Macrophages/drug effects ; Macrophages/immunology ; Tissue Inhibitor of Metalloproteinase-3/antagonists & inhibitors ; Tissue Inhibitor of Metalloproteinase-3/immunology ; Tumor Necrosis Factors/antagonists & inhibitors ; Tumor Necrosis Factors/immunology
Chemical Substances	Endotoxins ; LRP1 protein, human ; Lipopolysaccharides ; Low Density Lipoprotein Receptor-Related Protein-1 ; TIMP3 protein, human ; Tissue Inhibitor of Metalloproteinase-3 ; Tumor Necrosis Factors ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86)
Language	English
Publishing date	2019-01-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.1800834
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Article ; Online: TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.

Carreca, Anna P / Pravatà, Veronica M / Markham, Matthew / Bonelli, Simone / Murphy, Gillian / Nagase, Hideaki / Troeberg, Linda / Scilabra, Simone D

Scientific reports

2020 Volume 10, Issue 1, Page(s) 12067

Abstract: 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 ... ...

Abstract	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-density lipoprotein receptor-related protein-1 (LRP-1). Different binding affinities of these proteins for the endocytic receptor correlate with different turnover rates which, together with differences in their mRNA expression, determines their nett extracellular levels. In this study, we used surface plasmon resonance to evaluate the affinity between LRP-1 and a number of MMPs, ADAMs, ADAMTSs, TIMPs and metalloproteinase/TIMP complexes. This identified MMP-1 as a new LRP-1 ligand. Among the proteins analyzed, TIMP-3 bound to LRP-1 with highest affinity (K
MeSH term(s)	Endocytosis ; Humans ; Kinetics ; Low Density Lipoprotein Receptor-Related Protein-1/metabolism ; Matrix Metalloproteinase 1/metabolism ; Matrix Metalloproteinases/metabolism ; Multiprotein Complexes/metabolism ; Protein Binding ; Tissue Inhibitor of Metalloproteinase-3/antagonists & inhibitors ; Tissue Inhibitor of Metalloproteinase-3/genetics ; Tissue Inhibitor of Metalloproteinase-3/metabolism
Chemical Substances	LRP1 protein, human ; Low Density Lipoprotein Receptor-Related Protein-1 ; Multiprotein Complexes ; TIMP3 protein, human ; Tissue Inhibitor of Metalloproteinase-3 ; Matrix Metalloproteinases (EC 3.4.24.-) ; Matrix Metalloproteinase 1 (EC 3.4.24.7)
Language	English
Publishing date	2020-07-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-69008-9
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Article: Proteases involved in cartilage matrix degradation in osteoarthritis.

Troeberg, Linda / Nagase, Hideaki

Biochimica et biophysica acta

2011 Volume 1824, Issue 1, Page(s) 133–145

Abstract: Osteoarthritis is a common joint disease for which there are currently no disease-modifying drugs available. Degradation of the cartilage extracellular matrix is a central feature of the disease and is widely thought to be mediated by proteinases that ... ...

Abstract	Osteoarthritis is a common joint disease for which there are currently no disease-modifying drugs available. Degradation of the cartilage extracellular matrix is a central feature of the disease and is widely thought to be mediated by proteinases that degrade structural components of the matrix, primarily aggrecan and collagen. Studies on transgenic mice have confirmed the central role of Adamalysin with Thrombospondin Motifs 5 (ADAMTS-5) in aggrecan degradation, and the collagenolytic matrix metalloproteinase MMP-13 in collagen degradation. This review discusses recent advances in current understanding of the mechanisms regulating expression of these key enzymes, as well as reviewing the roles of other proteinases in cartilage destruction. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome.
MeSH term(s)	ADAM Proteins/genetics ; ADAM Proteins/metabolism ; Animals ; Cartilage/metabolism ; Cartilage/pathology ; Collagenases/genetics ; Collagenases/metabolism ; Extracellular Matrix/metabolism ; Extracellular Matrix/pathology ; Gene Expression Regulation, Enzymologic/physiology ; Humans ; Matrix Metalloproteinases/genetics ; Matrix Metalloproteinases/metabolism ; Mice ; Models, Biological ; Osteoarthritis/enzymology ; Osteoarthritis/genetics ; Osteoarthritis/metabolism ; Osteoarthritis/pathology ; Peptide Hydrolases/genetics ; Peptide Hydrolases/metabolism ; Peptide Hydrolases/physiology ; Proteolysis
Chemical Substances	Peptide Hydrolases (EC 3.4.-) ; ADAM Proteins (EC 3.4.24.-) ; Collagenases (EC 3.4.24.-) ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2011-07-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2011.06.020
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Article ; Online: Purification of MMPs and TIMPs.

Shimokawa, Ken-Ichi / Nagase, Hideaki

Methods in molecular biology (Clifton, N.J.)

2010 Volume 622, Page(s) 123–155

Abstract: A number of matrix metalloproteinases (MMPs) and their endogenous inhibitors called tissue inhibitors of metalloproteinases (TIMPs) from natural sources have been identified. This chapter describes the purification methods of MMPs-1, -2, -3, -7, -8, -9, - ...

Abstract	A number of matrix metalloproteinases (MMPs) and their endogenous inhibitors called tissue inhibitors of metalloproteinases (TIMPs) from natural sources have been identified. This chapter describes the purification methods of MMPs-1, -2, -3, -7, -8, -9, -10, -12, and -13 and TIMPs-1 and -2. The sources of the proteins and assay methods to detect their activities are also described.
MeSH term(s)	Animals ; Enzyme Activation ; Enzyme Precursors/isolation & purification ; Humans ; Metalloproteases/isolation & purification ; Metalloproteases/metabolism ; Molecular Biology/methods ; Rats ; Tissue Inhibitor of Metalloproteinases/isolation & purification ; Tissue Inhibitor of Metalloproteinases/metabolism
Chemical Substances	Enzyme Precursors ; Tissue Inhibitor of Metalloproteinases ; Metalloproteases (EC 3.4.-)
Language	English
Publishing date	2010
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-60327-299-5_8
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Article ; Online: Metalloproteinases in health and disease: challenges and the future prospects.

Nagase, Hideaki / Karamanos, Nikos

The FEBS journal

2010 Volume 278, Issue 1, Page(s) 1

MeSH term(s)	Disease ; Health ; Humans ; Metalloproteases/metabolism ; Research/trends
Chemical Substances	Metalloproteases (EC 3.4.-)
Language	English
Publishing date	2010-08-27
Publishing country	England
Document type	Introductory Journal Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2010.07917.x
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Article ; Online: Localizing matrix metalloproteinase activities in the pericellular environment.

Murphy, Gillian / Nagase, Hideaki

The FEBS journal

2010 Volume 278, Issue 1, Page(s) 2–15

Abstract: Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface- ... ...

Abstract	Matrix metalloproteinases (MMPs) are a group of structurally related proteolytic enzymes containing a zinc ion in the active site. They are secreted from cells or bound to the plasma membrane and hydrolyze extracellular matrix (ECM) and cell surface-bound molecules. They therefore play key roles in morphogenesis, wound healing, tissue repair and remodeling in diseases such as cancer and arthritis. Although the cell anchored membrane-type MMPs (MT-MMPs) function pericellularly, the secreted MMPs have been considered to act within the ECM, away from the cells from which they are synthesized. However, recent studies have shown that secreted MMPs bind to specific cell surface receptors, membrane-anchored proteins or cell-associated ECM molecules and function pericellularly at focussed locations. This minireview describes examples of cell surface and pericellular partners of MMPs, as well as how they alter enzyme function and cellular behaviour.
MeSH term(s)	Cell Membrane/enzymology ; Extracellular Matrix/enzymology ; Humans ; Matrix Metalloproteinases/metabolism
Chemical Substances	Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2010-11-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/j.1742-4658.2010.07918.x
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Article: The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity.

Brew, Keith / Nagase, Hideaki

Biochimica et biophysica acta

2010 Volume 1803, Issue 1, Page(s) 55–71

Abstract: Tissue inhibitors of metalloproteinases (TIMPs) are widely distributed in the animal kingdom and the human genome contains four paralogous genes encoding TIMPs 1 to 4. TIMPs were originally characterized as inhibitors of matrix metalloproteinases (MMPs), ...

Abstract	Tissue inhibitors of metalloproteinases (TIMPs) are widely distributed in the animal kingdom and the human genome contains four paralogous genes encoding TIMPs 1 to 4. TIMPs were originally characterized as inhibitors of matrix metalloproteinases (MMPs), but their range of activities has now been found to be broader as it includes the inhibition of several of the disintegrin-metalloproteinases, ADAMs and ADAMTSs. TIMPs are therefore key regulators of the metalloproteinases that degrade the extracellular matrix and shed cell surface molecules. Structural studies of TIMP-MMP complexes have elucidated the inhibition mechanism of TIMPs and the multiple sites through which they interact with target enzymes, allowing the generation of TIMP variants that selectively inhibit different groups of metalloproteinases. Engineering such variants is complicated by the fact that TIMPs can undergo changes in molecular dynamics induced by their interactions with proteases. TIMPs also have biological activities that are independent of metalloproteinases; these include effects on cell growth and differentiation, cell migration, anti-angiogenesis, anti- and pro-apoptosis, and synaptic plasticity. Receptors responsible for some of these activities have been identified and their signaling pathways have been investigated. A series of studies using mice with specific TIMP gene deletions has illuminated the importance of these molecules in biology and pathology.
MeSH term(s)	Amino Acid Sequence ; Animals ; Disease ; Evolution, Molecular ; Humans ; Molecular Sequence Data ; Multigene Family ; Protein Engineering ; Tissue Inhibitor of Metalloproteinases/chemistry ; Tissue Inhibitor of Metalloproteinases/deficiency ; Tissue Inhibitor of Metalloproteinases/genetics ; Tissue Inhibitor of Metalloproteinases/metabolism
Chemical Substances	Tissue Inhibitor of Metalloproteinases
Language	English
Publishing date	2010-01-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2010.01.003
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