Matrix metalloproteinases: what do they not do? New substrates and biological roles identified by murine models and proteomics.
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TLDR
A shift in the MMP functional paradigm is highlighted, together with the difficulties associated with current methods of studying proteases this highlights the need for new high content degradomics approaches to uncover and annotate MMP activities in vivo and identify novel interactions within the protease web.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2010-01-01 and is currently open access. It has received 526 citations till now. The article focuses on the topics: Proteases & Protease.read more
Citations
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Extracellular matrix structure.
TL;DR: The complex ECM structure is emphasized as to provide a better understanding of its dynamic structural and functional multipotency and the implication of the various families of ECM macromolecules in health and disease is presented.
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Biological role of matrix metalloproteinases: a critical balance
TL;DR: Advancing the understanding of the MMP contribution to tissue homeostasis will lead to identify causal relationships between their dysregulation and the development of disease pathologies, thus guiding us to successful MMP-directed therapies.
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New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression.
TL;DR: The current status of gelatinase inhibitors as anticancer agents and their failure in the clinic is discussed in light of these new data on the gelatinases' roles as cell surface transducers - data that may lead to the design and development of novel, gelatinase-targeting inhibitors.
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Pathophysiology of the brain extracellular matrix: a new target for remyelination
TL;DR: The pathophysiological roles of the brain's ECM, particularly those of CSPGs, after neural insults are highlighted and how the ECM can be targeted to promote remyelination is discussed.
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Targeting Matrix Metalloproteinases in Cancer: Bringing New Life to Old Ideas
TL;DR: The role of MMPs in cancer, clinical trials for MMP inhibitors, and novel approaches to targeting MMP's in cancer are highlighted.
References
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New functions for the matrix metalloproteinases in cancer progression
Mikala Egeblad,Zena Werb +1 more
TL;DR: It is shown that the MMPs have functions other than promotion of invasion, have substrates other than components of the extracellular matrix, and that they function before invasion in the development of cancer.
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Involvement of chemokine receptors in breast cancer metastasis.
Anja Müller,Bernhard Homey,Hortensia Soto,Nianfeng Ge,Daniel Catron,Matthew E. Buchanan,Terri McClanahan,Erin Murphy,Wei Yuan,Stephan N. Wagner,Jose Luis Barrera,Alejandro Mohar,Emma Verastegui,Albert Zlotnik +13 more
TL;DR: It is reported that the chemokine receptors CXCR4 and CCR7 are highly expressed in human breast cancer cells, malignant breast tumours and metastases and their respective ligands CXCL12/SDF-1α and CCL21/6Ckine exhibit peak levels of expression in organs representing the first destinations of breast cancer metastasis.
Journal ArticleDOI
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
TL;DR: An approach for the accurate quantification and concurrent sequence identification of the individual proteins within complex mixtures based on isotope-coded affinity tags and tandem mass spectrometry is described.
Journal ArticleDOI
Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging Reagents
Philip L. Ross,Yulin N. Huang,Jason Marchese,Brian L. Williamson,Kenneth C. Parker,Stephen J. Hattan,Nikita Khainovski,Sasi Pillai,Subhakar Dey,Scott Daniels,Subhasish Purkayastha,Peter Juhasz,Stephen A. Martin,Michael Bartlet-Jones,Feng He,Allan Jacobson,Darryl J. Pappin,Darryl J. Pappin +17 more
TL;DR: It is found that inactivation of Upf1p and Xrn1p causes common as well as unique effects on protein expression, and the use of 4-fold multiplexing to enable relative protein measurements simultaneously with determination of absolute levels of a target protein using synthetic isobaric peptide standards.
Journal ArticleDOI
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Roy A. Black,Charles Rauch,Carl J. Kozlosky,Jacques J. Peschon,Jennifer L. Slack,Martin F. Wolfson,Beverly J. Castner,Kim L. Stocking,Pranitha Reddy,Subhashini Srinivasan,Nicole Nelson,Norman Boiani,Kenneth A. Schooley,Mary Gerhart,Raymond Davis,Jeffrey N. Fitzner,Richard S. Johnson,Raymond J. Paxton,Carl J. March,Douglas P. Cerretti +19 more
TL;DR: The results should facilitate the development of therapeutically useful inhibitors of TNF-α release, and they indicate that an important function of adamalysins may be to shed cell-surface proteins.