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Dipeptidyl peptidase IV (DPP IV/CD26) is a cell-surface plasminogen receptor

Mario Gonzalez-Gronow1, Steven Kaczowka, Govind Gawdi

  • 1Department of Pathology, Duke University Medical Center, Durham, North Carolina 27710, USA. Gonza002@mc.duke.edu

Frontiers in Bioscience : a Journal and Virtual Library
|November 6, 2007
PubMed

Insights

This review explores how plasminogen (Pg) binds to cell receptors, facilitating plasmin (Pm) activity crucial for tissue remodeling and cancer metastasis. It highlights lysine binding sites and sialic acid interactions, identifying DPP IV as a key receptor.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Oncology

Background:

  • Plasminogen (Pg) binding to cell receptors activates plasmin (Pm), essential for extracellular matrix degradation in processes like cell migration and tumor metastasis.
  • Pg binding is modulated by its lysine binding sites (LBS) and sialic acid residues, interacting with diverse cell-surface receptors.

Purpose of the Study:

  • To review the mechanisms of Pg binding to cell-surface receptors.
  • To discuss the role of Pg and its activator in physiological and pathological processes.
  • To identify potential Pg receptors and their role in prostate cancer.

Main Methods:

  • Literature review of studies on plasminogen binding mechanisms.
  • Analysis of structural features of plasminogen involved in receptor interaction.
  • Identification of specific cell-surface receptors, including DPP IV, ADA, and NHE-3.

Main Results:

  • Plasminogen utilizes L-lysine binding sites for broad receptor interaction and sialic acid residues for specific interactions with cationic pockets or lectin-like modules.
  • Dipeptidyl peptidase IV (DPP IV) is identified as a plasminogen receptor.
  • Potential roles of plasminogen/plasmin complexes with DPP IV, adenosine deaminase (ADA), and Na+/H+ exchanger isoform NHE-3 in prostate cancer are discussed.

Conclusions:

  • Cell-surface receptor binding is a critical regulatory step for plasminogen activation and plasmin-mediated extracellular matrix degradation.
  • The identification of DPP IV as a plasminogen receptor offers new insights into plasminogen's function in cancer.
  • Further research into the complexes of Pg/Pm with DPP IV, ADA, and NHE-3 may elucidate their role in prostate cancer progression.

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