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Extracellular Matrix

Extracellular matrix (ECM) has both structural and regulatory roles. Biological regulation by ECM is emerging as a major research area, driven by several new directions. As a crucial modulator of cell behavior, ECM has exceptionally strong relevance and translational implications for human disease, opening novel opportunities for mechanistic understanding of disease pathogenesis as well as treatment.(1) Formation of the extracellular matrix (ECM) requires cells to secrete ECM proteins. Assembly is achieved by following a strict hierarchical assembly pattern which begins with the deposition of fibronectin filaments on the cell surface, a process known as fibrillogenesis(2). Cells continue to remodel the ECM by degradation and reassembly mechanisms, the dynamic nature of the ECM being particularly apparent during development, wound healing, and certain disease states (3). It is estimated that there are over 300 proteins comprising the mammalian ECM or “core matrisome” and this does not include the large number of ECM-associated proteins. Cells interact with the ECM through receptors such as integrins and syndecans, resulting in the transduction of multiple signals to regulate key cellular processes such as differentiation, proliferation, survival, and motility of cells(4). The ECM has also been shown to bind growth factors such as VEGF, HGF and BMPs which are thought to create growth factor gradients that regulate pattern formation during development(5). Many of the ECM-regulated cell processes operate via reorganization of the actin and microtubule cytoskeletons(6).

Here you will find a list of important antibodies, reagents, kits, and other tools you need for your research in the field of ECM, and additional resources on the topic.

Mechanisms of ECM function

Mechanisms of ECM function - antibodies-online.com

The versatile functions of the ECM depend on its diverse physical, biochemical, and biomechanical properties. Anchorage to the basement membrane is essential for various biological processes, including asymmetric cell division in stem cell biology and maintenance of tissue polarity (stage 1). Depending on contexts, the ECM may serve to block or facilitate cell migration (stages 2 and 3). In addition, by binding to growth factor signaling molecules and preventing their otherwise free diffusion, the ECM acts as a sink for these signals and helps shape a concentration gradient (stage 4). Certain ECM components, including heparan sulfate proteoglycans and the hyaluronic acid receptor CD44, can selectively bind to different growth factors and function as a signal coreceptor (stage 5) or a presenter (stage 6) and help determine the direction of cell–cell communication (Lu et al., 2011). The ECM also direct signals to the cell by using its endogenous growth factor domains (not depicted) or functional fragment derivatives after being processed by proteases such as MMPs (stage 7). Finally, cells directly sense the biomechanical properties of the ECM, including its stiffness, and change a wide variety of behaviors accordingly (stage 8).(8)

ECM Biomarkers(7)

Serum Markers of collagen synthesis:

Serum Markers of collagen degradation:

Serum Markers of inhibition of degradation:

Important ECM Proteins:

The following targets are directly related to research on ECM. Search Antibodies, Kits, Reagents and other products.

Type 1 Collagen Antibodies

Collagen is the most abundant fibrous protein within the interstitial ECM and constitutes up to 30% of the total protein mass of a multicellular animal.(12)

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
ReactivityCow, Human, Mammalian, Mouse, Rat
ClonalityPolyclonal
ApplicationELISA, IHC, IP, WB
Cat. No.ABIN5596823
Quantity50 μg
ReactivityCow, Deer, Human, Pig, Rabbit, Rat
ClonalityMonoclonal
ApplicationELISA, IF, IHC, IHC (fro), IHC (p), IHC (pfa)
Cat. No.ABIN957814
Quantity50 μL
ReactivityCow, Human, Mammalian, Mouse, Rat
ClonalityPolyclonal
ApplicationELISA, IHC, IP, WB
Cat. No.ABIN5596819
Quantity100 μg

Fibronectin Antibodies

Matrix assembly is usually initiated by ECM glycoproteins binding to cell surface receptors, such as fibronectin (FN) dimers binding to α5β1 integrin.(11)

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
ReactivityHuman
ClonalityMonoclonal
ApplicationEIA, FACS, IF, IHC (p), WB
Cat. No.ABIN1107234
Quantity0.1 mL
ReactivityHuman, Mouse, Rat
ClonalityPolyclonal
ApplicationIF (cc), IF (p)
Cat. No.ABIN671653
Quantity100 μL
ReactivityCow, Human, Monkey, Mouse, Rat
ClonalityPolyclonal
ApplicationELISA, IHC, IP, WB
Cat. No.ABIN5596762
Quantity100 μg

Laminin Antibodies

Laminin is key extracellular-matrix regulator of cell adhesion, migration, differentiation and proliferation.(10)/

MMP1 (Collagenase-1) Antibodies

Player in ECM Degradation. EMC targets are: Collagens I, II, III, VII, and X; gelatins; aggrecan; entactin; tenascin; perlecan(9)

Product
Reactivity
Clonality
Application
Cat. No.
Quantity
ReactivityHuman
ClonalityMonoclonal
ApplicationICC, FACS, IHC, ELISA, WB
Cat. No.ABIN969287
Quantity100 μL
ReactivityHuman
ClonalityPolyclonal
ApplicationWB
Cat. No.ABIN3043405
Quantity100 μg

References

(1) Hubmacher D, Apte SS. The biology of the extracellular matrix: novel insights. Curr Opin Rheumatol. 2013 Jan;25(1):65-70. doi: 10.1097/BOR.0b013e32835b137b. PMID: 23143224; PMCID: PMC3560377.

(2) Sottile J. and Hocking D. 2002. Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol. Biol. Cell. 13, 3546-3559.

(3) Daley W. et al. 2007. Extracellular matrix dynamics in development and regenerative medicine. J. Cell Sci. 121, 255-264.

(4) Hynes R. and Naba. 2011. Overview of the matrisome-an inventory of extracellular matrix constituents and functions. Cold Spring Harb Perspect Biol. doi:10.1101.

(5) Taipale J. and Keski-Oja J. 1997. Growth factors in the extracellular matrix. FASEB J. 11, 51-59.

(6) Ballestrem C. et al. 2004. Interplay between the actin cytoskeleton, focal adhesions and microtubules. Cell Motility. Ed Anne Ridley, Michelle Peckham and Peter Clark. 75-99.

(7) Begoña López, Arantxa González, Javier Díez. Circulating Biomarkers of Collagen Metabolism in Cardiac Diseases. 2010;121:1645–1654.

(8) Lu P, Weaver VM, Werb Z. The extracellular matrix: a dynamic niche in cancer progression. J Cell Biol. 2012 Feb 20;196(4):395-406. doi: 10.1083/jcb.201102147. PMID: 22351925; PMCID: PMC3283993.

(9) Lu P, Takai K, Weaver VM, Werb Z. Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb Perspect Biol. 2011 Dec 1;3(12):a005058. doi: 10.1101/cshperspect.a005058. PMID: 21917992; PMCID: PMC3225943.

(10) Hamill KJ, Kligys K, Hopkinson SB, Jones JC. Laminin deposition in the extracellular matrix: a complex picture emerges. J Cell Sci. 2009 Dec 15;122(Pt 24):4409-17. doi: 10.1242/jcs.041095. PMID: 19955338; PMCID: PMC2787456.

(11) Singh P, Carraher C, Schwarzbauer JE. Assembly of fibronectin extracellular matrix. Annu Rev Cell Dev Biol. 2010;26:397-419. doi: 10.1146/annurev-cellbio-100109-104020. PMID: 20690820; PMCID: PMC3628685.

(12) Frantz C, Stewart KM, Weaver VM. The extracellular matrix at a glance. J Cell Sci. 2010 Dec 15;123(Pt 24):4195-200. doi: 10.1242/jcs.023820. PMID: 21123617; PMCID: PMC2995612.

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