Molecules associated with elastic fibres

Summary
Organism
Homo sapiens (human)
Reactome
R-HSA-2129379
PubChem
R-HSA-2129379
Description
  • Proteins found associated with microfibrils include vitronectin (Dahlback et al. 1990), latent transforming growth factor beta-binding proteins (Kielty et al. 2002, Munger & Sheppard 2011), emilin (Bressan et al. 1993, Mongiat et al. 2000), members of the microfibrillar-associated proteins (MFAPs, Gibson et al.1996), and fibulins (Roark et al. 1995, Yanagisawa et al. 2002). The significance of these interactions is not well understood but may help mediate elastin-fibrillin interactions during elastic fibre assembly.

    Proteoglycans such as versican (Isogai et al. 2002), biglycan, and decorin (Reinboth et al. 2002) can interact with the microfibrils. They confer specific properties including hydration, impact absorption, molecular sieving, regulation of cellular activities, mediation of growth factor association, and release and transport within the extracellular matrix (Buczek-Thomas et al. 2002). In addition, glycosaminoglycans have been shown to interact with tropoelastin through its lysine side chains (Wu et al. 1999) regulating tropoelastin assembly (Tu and Weiss, 2008).
Click on a node on the pathway to see its details. Glycoproteins are marked with a glycoprotein icon in their name.
Displaying 1 entry
GlyCosmos Lectin UniProt ID Lectin Name Pathway Viewer
GL_002853 P04004 Vitronectin view

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Acknowledgements

Supported by JST NBDC Grant Number JPMJND2204

Partly supported by NIH Common Fund Grant #1U01GM125267-01


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Last updated: April 6, 2026