Matrix as an Interstitial Transport System
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Summary
The extracellular matrix is best known for its function as a structural scaffold for the tissue and more recently as a microenvironment to sequester growth factors and cytokines allowing for rapid and localized changes in their activity in the absence of new protein synthesis.
- Type
- article
- Published
- 2014-02-28
- Cited by
- 80
- References
- 208
- Access
- Open access
- OpenAlex
- https://openalex.org/W24577968
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:820284
Keywords
Seismic analysis, Response spectrum, Bridge (graph theory), Incremental Dynamic Analysis, Structural engineering
References
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- Regulation of MMP-1 and MMP-2 production through CD147/extracellular matrix metalloproteinase inducer interactions.
- The pericellular environment regulates cytoskeletal development and the differentiation of mesenchymal stem cells and determines their response to hydrostatic pressure.
- Essentials of Glycobiology
- Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen.
- The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1
- Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain.
- Hindered diffusion of spherical macromolecules through dilute fibrous media
- The art of cellular communication: tunneling nanotubes bridge the divide
- Syndecan‐4 contributes to endothelial tubulogenesis through interactions with two motifs inside the pro‐angiogenic N‐terminal domain of thrombospondin‐1
- Interplay of matrix metalloproteinases, tissue inhibitors of metalloproteinases and their regulators in cardiac matrix remodeling.
- Extracellular miRNAs: the mystery of their origin and function.
- The extracellular matrix metalloproteinase inducer EMMPRIN is a target of nitric oxide in myocardial ischemia/reperfusion.
Cited by
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease
- Investigation of the tumour necrosis factor-stimulated gene-6 (TSG-6) interactome : use and development of surface sensitive techniques
- Cardioprotective Signature of Short-Term Caloric Restriction
- Cardiac Physiology of Aging: Extracellular Considerations
- Extracellular Matrix Communication and Turnover in Cardiac Physiology and Pathology
- ADAMs family and relatives in cardiovascular physiology and pathology.
- Engineered heart slices for electrophysiological and contractile studies
- Myocardial matrix metalloproteinase-2: inside out and upside down
- Extracellular matrix in gene expression profiling of cancer
- Functional gastrointestinal disorders are associated with the joint hypermobility syndrome in secondary care: a case–control study
- Nucleic Acid Aptamer-Guided Cancer Therapeutics and Diagnostics: the Next Generation of Cancer Medicine
- Differential impact of mechanical unloading on structural and nonstructural components of the extracellular matrix in advanced human heart failure.
- Clinical significance of immunohistochemically detected extracellular matrix proteins and their spatial distribution in primary cancer.
- Protein pathways working in human follicular fluid: the future for tailored IVF?
- The missing link: does tunnelling nanotube-based supercellularity provide a new understanding of chronic and lifestyle diseases?
- Approximating bone ECM: Crosslinking directs individual and coupled osteoblast/osteoclast behavior.
- How Biomaterials Can Influence Various Cell Types in the Repair and Regeneration of the Heart after Myocardial Infarction
- A Disintegrin and Metalloprotease-17 Regulates Pressure Overload–Induced Myocardial Hypertrophy and Dysfunction Through Proteolytic Processing of Integrin &bgr;1
- Cell-type dependent response to photodynamic treatment in 3D collagen cell cultures.
- A Collagen Matrix Promotes Anti-Inflammatory Healing Macrophage Function Through a miR-92a Mechanism
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