Expression and activation of caspase-3/CPP32 in CD34+ cord blood cells is linked to apoptosis after growth factor withdrawal

Experimental Hematology

Volumn 28, Issue 8, 2000, Pages 907-915

  Wang, Li Sheng ^a   Liu, Hong Jun ^a   Xia, Zhen Biao ^a   Broxmeyer, Hal E ^a,b   Lu, Li ^a,b  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b WALTHER CANCER INSTITUTE   (United States)

Author keywords

Apoptosis; Caspase 3 CPP32; CD34+ cells; Cord blood

Indexed keywords

CASPASE 3; CASPASE INHIBITOR; CD34 ANTIGEN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; GROWTH FACTOR; INTERLEUKIN 3; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RECOMBINANT ERYTHROPOIETIN; STEEL FACTOR;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; DRUG WITHDRAWAL; ENZYME ACTIVATION; ENZYME ACTIVITY; FLOW CYTOMETRY; HEMATOPOIETIC STEM CELL; HUMAN; HUMAN CELL; INCUBATION TIME; LEUKEMIA CELL; NICK END LABELING; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; UMBILICAL CORD BLOOD; WESTERN BLOTTING;

ANTIGENS, CD34; APOPTOSIS; BLOTTING, WESTERN; CASPASE 3; CASPASES; CELLS, CULTURED; CYTOKINES; ENZYME ACTIVATION; FETAL BLOOD; FLOW CYTOMETRY; GENE EXPRESSION; HEMATOPOIETIC STEM CELLS; HUMANS; POLY(ADP-RIBOSE) POLYMERASES; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER;

MAMMALIA;

EID: 0033828175     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-472X(00)00485-9     Document Type: Article

References (42)

1. Raff M.C. Social controls on cell survival and cell death. Nature. 356:1992;397.
2. Schulze-Oshfoff K., Ferrari D., Los M., Wesselborg S., Peter M.E. Apoptosis signaling by death receptors. Eur J Biochem. 254:1998;439.
3. Koury M.J. Programmed cell death (apoptosis) in hematopoiesis. Exp Hematol. 20:1992;391.
4. Savill J.S., Wyllie A.H., Henson J.E., Walport M.J., Henson P.M., Haslett C. Macrophage phagocytosis of aging neutrophils in inflammation. Progarammed cell death in the neutrophils leads to its recognization by macrophages. J Clin Invest. 83:1989;865.
5. Williams G.T., Smith C.A., Spooncer E., Dexter T.M., Taylor D.R. Hemopoietic colony stimulating factors promote cell survival by suppressing apoptosis. Nature. 343:1990;76.
6. + human bone marrow cells is induced by interferon γ and tumor necrosis factor α and potentiates cytokine-mediated hematopoietic suppression in vitro. Blood. 85:1995;3183.
7. De Maria R., Testa U., Luchetti L.et al. Apoptotic role of Fas/Fas ligand system in the regulation of erythropoiesis. Blood. 93:1999;796.
8. Peters R., Leyvraz S., Perey L. Apoptotic regulation in primitive hematopoietic precursors. Blood. 92:1998;2041.
9. Saini K.S., Walker N.I. Biochemical and molecular mechanisms regulating apoptosis. Mol Cell Biochem. 178:1998;9.
10. Liebermann D.A., Hoffman B., Steinman R.A. Molecular controls of growth arrest and apoptosis. p53-dependent and independent pathways Oncogene. 11:1995;199.
11. Thornberry N.A., Lazebnik Y. Caspases. enemies within Science. 281:1998;1312.
12. Nunez G., Benedict M.A., Hu Y., Inohara N. Caspases. the proteases of the apoptotic pathway Oncogene. 17:1998;3237.
13. Cohen G.M. Caspases. the executioners of apoptosis Biochem J. 326:1997;1.
14. Tewari M., Quan L.T., O'Rourke K.et al. Yama/CPP32β, a mammalian homolog of CED-3, is CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801.
15. Xue D., Shaham S., Horvitz H.R. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 10:1996;1073.
16. Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell. 75:1993;641.
17. Datta R., Banach D., Kojima H.et al. Activation of the CPP32 protease in apoptosis induced by 1-β-D-arabinofuranosylcytosine and other DNA-damaging agents. Blood. 88:1996;1936.
18. Kothakota S., Azuma T., Reinhard C.et al. Caspase-3-generated fragment of gelsolin. effector of morphological change in apoptosis Science. 278:1997;294.
19. Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175.
20. Gervais F.G., Thornberry N.A., Ruffolo S.C., Nicholson D.W., Roy S. Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J Biol Chem. 273:1998;17102.
21. Frutos S., Moscat J., Diaz-Meco M.T. Cleavage of ζPKC but not λ/ιPKC by caspase-3 during UV-induced apoptosis. J Biol Chem. 274:1999;10765.
22. Nicholson D.W., Ali A., Thornberry N.A.et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 376:1995;37.
23. Wafl/Cip1 converts cancer cells from growth arrest to undergoing apoptosis. Oncogene. 18:1999;1131.
24. Khelifa T., Beck W.T. Merbarone, a catalytic inhibitor of DNA topoisomerase II, induces apoptosis in CEM cells through activation of ICE/CED-3-like protease. Mol Pharmacol. 55:1999;548.
25. Zhang J., Reedy M.C., Hannun Y.A., Obeid L.M. Inhibition of caspases inhibits the release of apoptotic bodies. Bcl-2 inhibits the initiation of formation of apoptotic bodies in chemotherapeutic agent-induced apoptosis J Cell Biol. 145:1999;99.
26. Ohta T., Kinoshita T., Naito M.et al. Requirement of the caspase-3/CPP32 protease cascade for apoptotic death following cytokine deprivation in hematopoietic cells. J Biol Chem. 272:1997;23111.
27. Dai C., Krantz S.B. Interferon γ induces upregulation and activation of caspases 1, 3, and 8 to produce apoptosis in human erythroid progenitor cells. Blood. 93:1999;3309.
28. Yamashita K., Takahashi A., Kobayashi S.et al. Caspases mediate tumor necrosis factor-α-induced neutrophil apoptosis and downregulation of reactive oxygen production. Blood. 93:1999;674.
29. 0 and entry into the cell cycle of primitive human hemopoietic progenitors. Proc Natl Acad Sci U S A. 89:1992;4013.
30. Lu L., Heinrich M.C., Wang L.-S.et al. Retroviral-mediated gene transduction of c-kit into single hematopoietic progentior cells from cord blood enhances erythroid colony formation and decreases sensitivity to inhibition by tumor necrosis factor-α and transforming growth factor-β1. Blood. 94:1999;2319.
31. Kerr J.F.R., Winterford C.M., Harmon B.V. Apoptosis. Its significance in cancer and cancer therapy. Cancer. 73:1994;2013.
32. Niho Y., Asano Y. Fas/Fas ligand and hematopoietic progenitor cells. Curr Opin Hematol. 5:1998;163.
33. Barcena A., Park S.W., Banapour B., Muench M.O., Mechetner E. Expression of Fas/CD95 and Bcl-2 by primitive hematopoietic progenitors freshly isolated from human fetal liver. Blood. 88:1996;2013.
34. Takenaka K., Nagafuji K., Harada M.et al. In vitro expansion of hematopoietic progenitor cells induces functional expression of Fas antigen (CD95). Blood. 88:1996;2871.
35. Nagafuji K., Shibuya T., Harada M.et al. Functional expression of Fas antigen (CD95) on hematopoietic progenitor cells. Blood. 86:1995;883.
36. - fetal liver cells. Exp Hematol. 27:1999;1428.
37. - hematopoietic progenitor cells by suppressing apoptosis. Exp Hematol. 27:1999;1451.
38. Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E.S. Molecular ordering of the Fas-apoptotic pathway. the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases Proc Natl Acad Sci U S A. 93:1996;14486.
39. Muzio M., Chinnaiyan A.M., Kischkel F.C.et al. FLICE, a novel FADD-homologous ICE-CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell. 85:1996;817.
40. Zheng T.S., Schlosser S.F., Dao T.et al. Caspase-3 controls both cytoplasmic and nuclear events associated with Fas-mediated apoptosis in vivo. Proc Natl Acad Sci U S A. 95:1998;13618.
41. + bone marrow cell survival. Blood. 93:1999;3302.
42. Lin Y.-Z., Yao S.Y., Veach R.A., Torgerson T.R., Hawiger J. Inhibition of nuclear translocation of transcription factor NF-κB by a synthetic peptide containing a cell membrane-permeable motif and nuclear localization sequence. J Biol Chem. 270:1995;14255.