Target intelligence / Profile preview

Extracellular matrix and tissue protein interfaces (ECM interfaces)

Target
ECM interfaces
Molecular classification
Other, Structural proteins, Adhesion molecules, Glycoproteins
01

Overview

The extracellular matrix (ECM) and tissue protein interfaces represent the complex network of physical and biochemical interactions between cells and their surrounding structural environment (Frantz et al., 2010, J Cell Sci). These interfaces are composed of fibrous proteins like collagens and elastins, glycoproteins such as fibronectin and laminin, and proteoglycans, which provide essential mechanical support and serve as a reservoir for growth factors (Lu et al., 2012, J Cell Biol). They regulate critical cellular processes including adhesion, migration, and differentiation through receptors like integrins and syndecans. Dysregulation of these interfaces is a hallmark of various pathologies, particularly fibrosis and cancer metastasis, where altered matrix stiffness and composition drive disease progression (Winkler et al., 2020, Nat Commun). While specific components within these interfaces, such as integrins or matrix-degrading enzymes, are major therapeutic targets, the interface itself is a broad structural and functional category rather than a single molecular entity.

Other names
ECM-cell interfacesCell-matrix interactionsTissue-protein interfacesMatrisome interactions
02

Mechanism of action

Modulation of cell-matrix adhesion via integrin inhibition, or interference with matrix synthesis and degradation pathways.

03

Biological functions

Cell adhesionStructural supportSignal transductionTissue remodelingGrowth factor sequestration
04

Disease associations

CancerFibrosisCardiovascular diseaseInflammationOsteoarthritis
05

Safety considerations

Impaired wound healingMusculoskeletal painSystemic toxicity due to ECM ubiquityIncreased bleeding risk
06

Interacting drugs

Abciximab

4 more in the full profile.

07

Biomarkers

Matrix metalloproteinases (MMPs)Collagen type III N-terminal propeptide (PIIINP)FibronectinLaminin-332

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