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Comment
. 2010 Feb 18;115(7):1315-6.
doi: 10.1182/blood-2009-11-254045.

A new plasminogen receptor

Dudley K Strickland  1
Affiliations
Comment

A new plasminogen receptor

Dudley K Strickland. Blood. .

Abstract

Efficient activation of the fibrinolytic pathway occurs when plasminogen and its activators are sequestered on the cell surface. Identification of receptors responsible for localizing plasminogen to the cell surface has been elusive. Using a proteomics approach, Andronicos and colleagues have identified a novel 17-kDa transmembrane receptor, termed Plg-R(KT), that binds plasminogen with high affinity and promotes its activation.(1).

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Conflict of interest statement

Conflict-of-interest disclosure: The author declares no competing financial interests. ■

Figures

None
Pg-RKT on the monocyte/macrophage cell surface binds plasminogen (Pg) via interactions involving lysine binding sites on the Pg kringle domains with the C-terminal lysine residue on Pg-RKT. The close proximity to uPA bound to the urokinase receptor (uPAR) greatly facilitates conversion of Pg to plasmin (Pm). Cell-associated Pm is involved in degradation of the extracellular matrix (ECM), cell migration, and in degrading fibrin.
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References

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