Preliminary evidence for a matrix metalloproteinase-2 (MMP-2)-dependent shedding of soluble CD40 ligand (sCD40L) from activated platelets.
Platelets are the major source of soluble CD40 ligand (sCD40L) in the blood. It has been demonstrated that CD40L is cleaved from the surface of activated platelets to release sCD40L. However, the enzyme involved in sCD40L shedding has not been identified yet. Using a panel of pharmacological inhibitors of serine, cysteine, aspartate, or metalloproteinases, preliminary evidence is presented for the hypothesis that matrix metalloproteinase-2 (MMP-2) might be the protease, primarily responsible for CD40L cleavage from platelet surface.
Reinboldt
Stephan
S
Institut für Pharmakologie, Universitätsklinikum Essen, Universität Duisburg-Essen, Germany.
Wenzel
Folker
F
Rauch
Bernhard H
BH
Hohlfeld
Thomas
T
Grandoch
Maria
M
Fischer
Jens W
JW
Weber
Artur-Aron
AA
D001792:Blood Platelets / Q000187:drug effects / Q000201:enzymology / Q000276:immunology / Q000378:metabolism*; D023201:CD40 Ligand / Q000097:blood* / Q000276:immunology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D020778:Matrix Metalloproteinase 2 / Q000097:blood* / Q000276:immunology; D061965:Matrix Metalloproteinase Inhibitors; D010446:Peptide Fragments / Q000494:pharmacology; D015539:Platelet Activation / Q000187:drug effects / Q000502:physiology*; D010976:Platelet Count
D004791:Enzyme Inhibitors; D061965:Matrix Metalloproteinase Inhibitors; D010446:Peptide Fragments; C082835:thrombin receptor peptide (42-47); D023201:CD40 Ligand; D020778:Matrix Metalloproteinase 2