Human extracellular matrix proteins (ECM proteins)

Human extracellular matrix (ECM) proteins constitute a complex, non-cellular network that provides essential structural and biochemical support to tissues and organs. The ECM is primarily composed of fibrous proteins such as collagens, elastins, fibronectins, and laminins, as well as various proteoglycans and glycosaminoglycans [1]. Beyond serving as a physical scaffold, these proteins act as a dynamic niche that regulates fundamental cellular processes, including survival, proliferation, and differentiation, through interactions with cell-surface receptors like integrins [2]. In many diseases, the ECM is pathologically altered; for example, excessive deposition of collagen leads to organ fibrosis, while the degradation of the basement membrane is a critical step in cancer metastasis [3]. Therapeutic interventions targeting the ECM include the use of enzymes to clear excessive matrix, small molecules to inhibit the synthesis of fibrotic proteins, and antibodies designed to block cell-matrix interactions or deliver payloads to specific matrix neo-epitopes [4]. Because ECM proteins are ubiquitous throughout the body, achieving tissue-specific targeting remains a significant challenge in drug development [5]. Sources: [1] Frantz, C., Stewart, K. M., & Weaver, V. M. (2010). The extracellular matrix at a glance. Journal of Cell Science. [2] Hynes, R. O. (2009). The extracellular matrix: not just glycans anymore. Science. [3] Lu, P., Weaver, V. M., & Werb, Z. (2012). The extracellular matrix: a dynamic niche in cancer progression. Journal of Cell Biology. [4] Jarvelainen, H., et al. (2009). Extracellular matrix molecules: potential targets in pharmacotherapy. Pharmacological Reviews. [5] Theocharis, A. D., et al. (2016). Extracellular matrix structure. Advanced Drug Delivery Reviews.

Other names

Extracellular matrixMatrisomeInterstitial matrixBasement membrane proteinsConnective tissue proteins

Enzymatic degradation of specific matrix components, inhibition of pro-fibrotic signaling to reduce matrix synthesis, and blockade of cell-surface receptors that mediate adhesion to the extracellular matrix.