Current understanding of the thrombospondin-1 interactome

Andrea Resovi, Denise Pinessi, Giovanna Chiorino, Giulia Taraboletti

Research output: Contribution to journalArticlepeer-review


The multifaceted action of thrombospondin-1 (TSP-1) depends on its ability to physically interact with different ligands, including structural components of the extracellular matrix, other matricellular proteins, cell receptors, growth factors, cytokines and proteases. Through this network, TSP-1 regulates the ligand activity, availability and structure, ultimately tuning the cell response to environmental stimuli in a context-dependent manner, contributing to physiological and pathological processes. Complete mapping of the TSP-1 interactome is needed to understand its diverse functions and to lay the basis for the rational design of TSP-1-based therapeutic approaches. So far, large-scale approaches to identify TSP-1 ligands have been rarely used, but many interactions have been identified in small-scale studies in defined biological systems. This review, based on information from protein interaction databases and the literature, illustrates current knowledge of the TSP-1 interactome map.

Original languageEnglish
Pages (from-to)83-91
Number of pages9
JournalMatrix Biology
Publication statusPublished - Jul 1 2014


  • Angiogenesis
  • Domains
  • Growth factors
  • Matricellular proteins
  • Protein-protein interaction
  • Thrombospondin-1

ASJC Scopus subject areas

  • Molecular Biology
  • Medicine(all)


Dive into the research topics of 'Current understanding of the thrombospondin-1 interactome'. Together they form a unique fingerprint.

Cite this