From plasminogen to plasmin: role of plasminogen receptors in human cancer

Int J Mol Sci. 2014 Nov 17;15(11):21229-52. doi: 10.3390/ijms151121229.

Abstract

Cell surface-associated proteolysis mediated by plasmin (PLA) is an essential feature of wound healing, angiogenesis and cell invasion, processes that are dysregulated in cancer development, progression and systemic spread. The generation of PLA, initiated by the binding of its precursor plasminogen (PLG) to the cell surface, is regulated by an array of activators, inhibitors and receptors. In this review, we will highlight the importance of the best-characterized components of the PLG/PLA cascade in the pathogenesis of cancer focusing on the role of the cell surface-PLG receptors (PLG-R). PLG-R overexpression has been associated with poor prognosis of cancer patients and resistance to chemotherapy. We will also discuss recent findings on the molecular mechanisms regulating cell surface expression and distribution of PLG-R.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / genetics
  • Actins / metabolism
  • Animals
  • Annexin A2 / genetics
  • Annexin A2 / metabolism
  • Biomarkers, Tumor / genetics
  • Biomarkers, Tumor / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Fibrinolysin / metabolism*
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Keratin-8 / genetics
  • Keratin-8 / metabolism
  • Neoplasms / genetics
  • Neoplasms / metabolism*
  • Neoplasms / pathology
  • Phosphopyruvate Hydratase / genetics
  • Phosphopyruvate Hydratase / metabolism
  • Plasminogen / metabolism*
  • Protein Transport
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / metabolism

Substances

  • Actins
  • Annexin A2
  • Biomarkers, Tumor
  • DNA-Binding Proteins
  • Keratin-8
  • Receptors, Cell Surface
  • Tumor Suppressor Proteins
  • Plasminogen
  • Fibrinolysin
  • ENO1 protein, human
  • Phosphopyruvate Hydratase