Poul Henning Jensen

Cleaved intracellular plasminogen activator inhibitor 2 in human myeloleukaemia cells is a marker of apoptosis

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

The proteolytic modification of plasminogen activator inhibitor 2 (PAI-2) was studied during apoptosis in the human promyelocytic leukaemic NB4 cell line during treatment with the phosphatase inhibitors okadaic acid and calyculin A as well as the protein synthesis inhibitor cycloheximide. The apoptic type of cell death was ascertained by morphological and biochemical criteria. In cell homogenates PAI-2 was probed by [125I]urokinase plasminogen activator (uPA) and detected as a sodium dodecyl sulphate-stable M(r) 80,000 complex after reducing sodium dodecyl sulphate-polyacrylamide gel electrophoresis and autoradiography. During apoptosis a smaller (M(r) 70,000) uPA-PAI-2 complex was consistently detected. The modification was in the PAI-2 moiety, as the [125I]uPA tracer could be extracted in its intact form from the complex. Thus the cleaved PAI-2 isoform is a biochemical marker of apoptosis in the promyelocytic NB4 cell line. The modified PAI-2 isoform was also detected in homogenates made from purified human mononuclear leukaemic cells aspirated from the bone marrow of patients suffering from acute and chronic myeloid leukaemia.
Original languageEnglish
JournalBritish Journal of Cancer
Pages (from-to)834-40
Number of pages7
Publication statusPublished - 1 Nov 1994

    Research areas

  • Apoptosis, Bone Marrow, Cell Death, Ethers, Cyclic, Humans, Intracellular Fluid, Isomerism, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Leukemia, Promyelocytic, Acute, Okadaic Acid, Oxazoles, Phosphoprotein Phosphatases, Plasminogen Activator Inhibitor 2, Tumor Cells, Cultured, Tumor Markers, Biological

See relations at Aarhus University Citationformats

ID: 40647273