67
Views
4
CrossRef citations to date
0
Altmetric
Original

TRAIL, caspases and maturation of normal and leukemic myeloid precursors

, , &
Pages 1459-1468 | Accepted 22 Nov 2005, Published online: 01 Jul 2009

References

  • Heissig B, Ohki Y, Sato Y, Rafii S, Werb Z, Hattori K. A role for niches in hematopoietic cell development. Hematology 2005; 10: 247–253
  • Park J R. Cytokine regulation of apoptosis in hematopoietic precursor cells. Curr Opin Hematol 1996; 3: 191–196
  • Cantor A B, Orkin S H. Transcriptional regulation of erythropoiesis: an affair involving multiple partners. Oncogene 2002; 21: 3368–3376
  • Perry C, Soreq H. Transcriptional regulation of erythropoiesis. Fine tuning of combinatorial multi-domain elements. Eur J Biochem 2002; 269: 3607–3618
  • Skalnik D G. Transcriptional mechanisms regulating myeloid-specific genes. Gene 2002; 284: 1–21
  • Wiley S R, Schooley K, Smolak P J, Din W S, Huang C P, Nicholl J K, et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 1995; 3: 673–682
  • De Maria R, Zeuner A, Eramo A, Domenichelli C, Bonci D, Grignani F, et al. Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1. Nature 1999; 401: 489–493
  • Zamai L, Secchiero P, Pierpaoli S, Bassini A, Papa S, Alnemri E S, et al. TNF-related apoptosis-inducing ligand (TRAIL) as a negative regulator of normal human erythropoiesis. Blood 2000; 95: 3716–3724
  • Secchiero P, Melloni E, Heikinheimo M, Mannisto S, Di Pietro R, Iacone A, et al. TRAIL regulates normal erythroid maturation through an ERK-dependent pathway. Blood 2004; 103: 517–522
  • Mirandola P, Gobbi G, Ponti C, Sponzilli I, Cocco L, Vitale M. PKC{epsilon} controls the protection against TRAIL in erythroid progenitors. Blood Sep 15, 2005, [Epub ahead of print]
  • Crist S A, Elzey B D, Ludwig A T, Griffith T S, Staack J B, Lentz S R, et al. Expression of TNF-related apoptosis-inducing ligand (TRAIL) in megakaryocytes and platelets. Exp Hematol 2004; 32: 1073–1081
  • Melloni E, Secchiero P, Celeghini C, Campioni D, Grill V, Guidotti L, et al. Functional expression of TRAIL and TRAIL-R2 during human megakaryocytic development. J Cell Physiol 2005; 204: 975–982
  • Secchiero P, Gonelli A, Mirandola P, Melloni E, Zamai L, Celeghini C, et al. Tumor necrosis factor-related apoptosis-inducing ligand induces monocytic maturation of leukemic and normal myeloid precursors through a caspase-dependent pathway. Blood 2002; 100: 2421–2429
  • Secchiero P, Milani D, Gonelli A, Melloni E, Campioni D, Gibellini D, et al. Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and TNF-alpha promote the NF-kappaB-dependent maturation of normal and leukemic myeloid cells. J Leukoc Biol 2003; 74: 223–232
  • Pitti R M, Marsters S A, Ruppert S, Donahue C J, Moore A, Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem 1996; 271: 12687–12690
  • Almasan A, Ashkenazi A. Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. Cytokine Growth Factor Rev 2003; 14: 337–348
  • Mariani S M, Krammer P H. Differential regulation of TRAIL and CD95 ligand in transformed cells of the T and B lymphocyte lineage. Eur J Immunol 1998; 28: 973–982
  • Liabakk N B, Sundan A, Torp S, Aukrust P, Froland S S, Espevik T. Development, characterization and use of monoclonal antibodies against sTRAIL: measurement of sTRAIL by ELISA. J Immunol Methods 2002; 259: 119–128
  • Gruss H J. Molecular, structural, and biological characteristics of the tumor necrosis factor ligand superfamily. Int J Clin Lab Res 1996; 26: 143–159
  • Pan G, O'Rourke K, Chinnaiyan A M, Gentz R, Ebner R, Ni J, et al. The receptor for the cytotoxic ligand TRAIL. Science 1997; 276: 111–113
  • Hymowitz S G, Ultsch M H, Hurst A, Totpal K, Ashkenazi A, De Vos A M, et al. A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL. Biochemistry 2000; 39: 633–640
  • Di Pietro R, Zauli G. Emerging non-apoptotic functions of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)/Apo2L. J Cell Physiol 2004; 201: 331–340
  • Ashkenazi A, Pai R C, Fong S, Leung S, Lawrence D A, Marsters S A, , et al. Safety and anti tumor activity of recombinant soluble Apo2 ligand. J Clin Investig 1999; 104: 155–162
  • Walczak H, Miller R E, Ariail K, Gliniak B, Griffith T S, Kubin M, et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med 1999; 5: 157–163
  • Bouralexis S, Findlay D M, Evdokiou A. Death to the bad guys: targeting cancer via Apo2L/TRAIL. Apoptosis 2005; 10: 35–51
  • Secchiero P, Vaccarezza M, Gonelli A, Zauli G. TNF-related apoptosis-inducing ligand (TRAIL): a potential candidate for combined treatment of hematological malignancies. Curr Pharm Des 2004; 10: 3673–3681
  • Plasilova M, Zivny J, Jelinek J, Neuwirtova R, Cermak J, Necas E, et al. TRAIL (Apo2L) suppresses growth of primary human leukemia and myelodysplasia progenitors. Leukemia 2002; 16: 67–73
  • Jones D T, Ganeshaguru K, Mitchell W A, Foroni L, Baker R J, Prentice H G, et al. Cytotoxic drugs enhance the ex vivo sensitivity of malignant cells from a subset of acute myeloid leukaemia patients to apoptosis induction by tumour necrosis factor receptor-related apoptosis-inducing ligand. Br J Haematol 2003; 121: 713–720
  • Insinga A, Monestiroli S, Ronzoni S, Gelmetti V, Marchesi F, Viale A, et al. Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway. Nat Med 2005; 11: 71–76
  • Nebbioso A, Clarke N, Voltz E, Germain E, Ambrosino C, Bontempo P, et al. Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat Med 2005; 11: 77–84
  • Zang D Y, Goodwin R G, Loken M R, Bryant E, Deeg H J. Expression of tumor necrosis factor-related apoptosis-inducing ligand, Apo2L, and its receptors in myelodysplastic syndrome: effects on in vitro hemopoiesis. Blood 2001; 98: 3058–3065
  • Uno K, Inukai T, Kayagaki N, Goi K, Sato H, Nemoto A, et al. TNF-related apoptosis-inducing ligand (TRAIL) frequently induces apoptosis in Philadelphia chromosome-positive leukemia cells. Blood 2003; 101: 3658–3667
  • Gazitt Y. TRAIL is a potent inducer of apoptosis in myeloma cells derived from multiple myeloma patients and is not cytotoxic to hematopoietic stem cells. Leukemia 1999; 13: 1817–1824
  • Gazitt Y, Shaughnessy P, Montgomery W. Apoptosis-induced by TRAIL and TNF-alpha in human multiple myeloma cells is not blocked by BCL-2. Cytokine 1999; 11: 1010–1019
  • Liu Q, El-Deiry W S, Gazitt Y. Additive effect of Apo2L/TRAIL and Adeno-p53 in the induction of apoptosis in myeloma cell lines. Exp Hematol 2001; 29: 962–970
  • Spencer A, Yeh S L, Koutrevelis K, Baulch-Brown C. TRAIL-induced apoptosis of authentic myeloma cells does not correlate with the procaspase-8/cFLIP ratio. Blood 2002; 100: 3049
  • Fandy T E, Shankar S, Ross D D, Sausville E, Srivastava R K. Interactive effects of HDAC inhibitors and TRAIL on apoptosis are associated with changes in mitochondrial functions and expressions of cell cycle regulatory genes in multiple myeloma. Neoplasia 2005; 7: 646–657
  • Sheridan J P, Marsters S A, Pitti R M, Gurney A, Skubatch M, Baldwin D, et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science 1997; 277: 818–821
  • Ashkenazi A. Targeting death and decoy receptors of the tumour necrosis factor superfamily. Nat Rev Cancer 2002; 2: 420–430
  • Kimberley F C, Screaton G R. Following a TRAIL: update on a ligand and its five receptors. Cell Res 2004; 14: 359–372
  • Chaudhary P M, Eby M, Jasmin A, Bookwalter A, Murray J, Hood L. Death receptor 5, a new member of the TNFR family, and DR4 induce FADD- dependent apoptosis and activate the NF-kappaB pathway. Immunity 1997; 7: 821–830
  • MacFarlane M, Ahmad M, Srinivasula S M, Fernandes-Alnemri T, Cohen G M, Alnemri E S. Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL. J Biol Chem 1997; 272: 25417–25420
  • Screaton G R, Mongkolsapaya J, Xu X N, Cowper A E, McMichael A J, Bell J I. TRICK2, a new alternatively spliced receptor that transduces the cytotoxic signal from TRAIL. Curr Biol 1997; 7: 693–696
  • Walczak H, Degli-Esposti M A, Johnson R S, Smolak P J, Waugh J Y, Boiani N, et al. TRAILR2: a novel apoptosis-mediating receptor for TRAIL. Embo J 1997; 16: 5386–5397
  • Wu G S, Burns T F, McDonald E R, Jiang W, Meng R, Krantz I D, et al. KILLER/DR5 is a DNA damage-inducible p53 regulated death receptor gene. Nat Genet 1997; 17: 141–143
  • Degli-Esposti M A, Smolak P J, Walczak H, Waugh J, Huang C P, DuBose R F, et al. Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. J Exp Med 1997; 186: 1165–1170
  • Pan G, Ni J, Yu G, Wei Y F, Dixit V M. TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL signaling. FEBS Lett 1998; 424: 41–45
  • Marsters S A, Sheridan J P, Pitti R M, Huang A, Skubatch M, Baldwin D, et al. A novel receptor for Apo2L/TRAIL contains a truncated death domain. Curr Biol 1997; 7: 1003–1006
  • Degli-Esposti M A, Dougall W C, Smolak P J, Waugh J Y, Smith C A, Goodwin R G. The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-mediated apoptosis, yet retains an incomplete death domain. Immunity 1997; 7: 813–820
  • Sheikh M S, Fornace A J, Jr. Death and decoy receptors and p53-mediated apoptosis. Leukemia 2000; 14: 1509–1513
  • Ozoren N, El-Deiry W S. Cell surface death receptor signaling in normal and cancer cells. Semin Cancer Biol 2003; 13: 135–147
  • Sheikh M S, Huang Y, Fernandez-Salas E A, El-Deiry W S, Friess H, Amundson S, et al. The antiapoptotic decoy receptor TRID/TRAIL-R3 is a p53-regulated DNA damage-inducible gene that is overexpressed in primary tumors of the gastrointestinal tract. Oncogene 1999; 18: 4153–4159
  • Meng R D, McDonald E R, Sheikh M S, Fornace A J, Jr, El-Deiry W S. The TRAIL decoy receptor TRUNDD (DcR2, TRAIL-R4) is induced by adenovirus-p53 overexpression and can delay TRAIL-, p53-, and KILLER/DR5-dependent colon cancer apoptosis. Mol Ther 2000; 1: 130–144
  • Ruiz de Almodovar C, Ruiz-Ruiz C, Rodriguez A, Ortiz-Ferron G, Redondo J M, Lopez-Rivas A. TRAIL decoy receptor TRAIL-R3 is upregulated by p53 in breast tumor cells through a mechanism involving an intronic p53 binding site. J Biol Chem 2004; 279: 4093–4101
  • Emery J G, McDonnell P, Burke M B, Deen K C, Lyn S, Silverman C, et al. Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL. J Biol Chem 1998; 273: 14363–14367
  • Truneh A, Sharma S, Silverman C, Khandekar S, Reddy M P, Deen K C, et al. Temperature-sensitive differential affinity of TRAIL for its receptors. DR5 is the highest affinity receptor. J Biol Chem 2000; 275: 23319–23325
  • Holen I, Croucher P I, Hamdy F C, Eaton C L. Osteoprotegerin (OPG) is a survival factor for human prostate cancer cells. Cancer Res 2002; 62: 1619–1623
  • Miyashita T, Kawakami A, Nakashima T, Yamasaki S, Tamai M, Tanaka F, et al. Osteoprotegerin (OPG) acts as an endogenous decoy receptor in tumour necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis of fibroblast-like synovial cells. Clin Exp Immunol 2004; 137: 430–436
  • Kim K, Fisher M J, Xu S Q, el-Deiry W S. Molecular determinants of response to TRAIL in killing of normal and cancer cells. Clin Cancer Res 2000; 6: 335–346
  • Pan G, Ni J, Wei Y F, Yu G, Gentz R, Dixit V M. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 1997; 277: 815–818
  • Mongkolsapaya J, Cowper A E, Xu X N, Morris G, McMichael A J, Bell J I, et al. Lymphocyte inhibitor of TRAIL (TNF-related apoptosis-inducing ligand): a new receptor protecting lymphocytes from the death ligand TRAIL. J Immunol 1998; 160: 3–6
  • Wuchter C, Krappmann D, Cai Z, Ruppert V, Scheidereit C, Dorken B, et al. In vitro susceptibility to TRAIL-induced apoptosis of acute leukemia cells in the context of TRAIL receptor gene expression and constitutive NF-kB activity. Leukemia 2001; 15: 921–928
  • Lincz L F, Yeh T X, Spencer A. TRAIL-induced eradication of primary tumour cells from multiple myeloma patient bone marrows is not related to TRAIL receptor expression or prior chemotherapy. Leukemia 2001; 15: 1650–1657
  • Secchiero P, Gonelli A, Carnevale E, Milani D, Pandolfi A, Zella D, et al. TRAIL promotes the survival and proliferation of primary human vascular endothelial cells by activating the Akt and ERK pathways. Circulation 2003; 107: 2250–2256
  • Secchiero P, Zerbinati C, Rimondi E, Corallini F, Milani D, Grill V, et al. TRAIL promotes the survival, migration and proliferation of vascular smooth muscle cells. Cell Mol Life Sci 2004; 61: 1965–1974
  • Mirandola P, Ponti C, Gobbi G, Sponzilli I, Vaccarezza M, Cocco L, et al. Activated human NK and CD8 + T cells express both TNF-related apoptosis inducing ligand (TRAIL) and TRAIL receptors, but are resistant to TRAIL-mediated cytotoxicity. Blood 2004; 104: 2418–2424
  • Secchiero P, Tiribelli M, Barbarotto E, Celeghini C, Michelutti A, Masolini P, et al. Aberrant expression of TRAIL in B chronic lymphocytic leukemia (B-CLL) cells. J Cell Physiol 2005; 205: 246–252
  • Griffith T S, Chin W A, Jackson G C, Lynch D H, Kubin M Z. Intracellular regulation of TRAIL-induced apoptosis in human melanoma cells. J Immunol 1998; 161: 2833–2840
  • Zhang X D, Franco A, Myers K, Gray C, Nguyen T, Hersey P. Relation of TNF-related apoptosis-inducing ligand (TRAIL) receptor and FLICE-inhibitory protein expression to TRAIL-induced apoptosis of melanoma. Cancer Res 1999; 59: 2747–2753
  • Chinnaiyan A M, O'Rourke K, Tewari M, Dixit V M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995; 81: 505–512
  • Boldin M P, Mett I L, Varfolomeev E E, Chumakov I, Shemer-Avni Y, Camonis J H, et al. Self-association of the “death domains” of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects. J Biol Chem 1995; 270: 387–391
  • Kischkel F C, Lawrence D A, Tinel A, LeBlanc H, Virmani A, Schow P, et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 2001; 276: 46639–46646
  • Muhlenbeck F, Haas E, Schwenzer R, Schubert G, Grell M, Smith C, et al. TRAIL/Apo2L activates c-Jun NH2-terminal kinase (JNK) via caspase-dependent and caspase-independent pathways. J Biol Chem 1998; 273: 33091–33098
  • Herr I, Wilhelm D, Meyer E, Jeremias I, Angel P, Debatin K M. JNK/SAPK activity contributes to TRAIL-induced apoptosis. Cell Death Differ 1999; 6: 130–135
  • Wachter T, Sprick M, Hausmann D, Kerstan A, McPherson K, Stassi G, et al. cFLIPL inhibits tumor necrosis factor-related apoptosis-inducing ligand-mediated NF-kappaB activation at the death-inducing signaling complex in human keratinocytes. J Biol Chem 2004; 279: 52824–52834
  • Ricci M S, Jin Z, Dews M, Yu D, Thomas-Tikhonenko A, Dicker D T, et al. Direct repression of FLIP expression by c-myc is a major determinant of TRAIL sensitivity. Mol Cell Biol 2004; 24: 8541–8555
  • Sharp D A, Lawrence D A, Ashkenazi A. Selective knockdown of the long variant of cellular FLICE inhibitory protein augments death receptor-mediated caspase-8 activation and apoptosis. J Biol Chem 2005; 280: 19401–19409
  • Sprick M R, Walczak H. The interplay between the Bcl-2 family and death receptor-mediated apoptosis. Biochim Biophys Acta 2004; 1644: 125–132
  • Harper N, Farrow S N, Kaptein A, Cohen G M, MacFarlane M. Modulation of tumor necrosis factor apoptosis-inducing ligand-induced NF-kappaB activation by inhibition of apical caspases. J Biol Chem 2001; 276: 34743–34752
  • Zauli G, Pandolfi A, Gonelli A, Di Pietro R, Guarnieri S, Ciabattoni G, et al. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) sequentially upregulates nitric oxide and prostanoid production in primary human endothelial cells. Circ Res 2003; 92: 732–740
  • Hu W H, Johnson H, Shu H B. Tumor necrosis factor-related apoptosis-inducing ligand receptors signal NF-kappaB and JNK activation and apoptosis through distinct pathways. J Biol Chem 1999; 274: 30603–30610
  • Campioni D, Secchiero P, Corallini F, Melloni E, Capitani S, Lanza F, et al. Evidence for a role of TNF-related apoptosis-inducing ligand (TRAIL) in the anemia of myelodysplastic syndromes. Am J Pathol 2005; 166: 557–563
  • Schmidt U, van den Akker E, Parren-van Amelsvoort M, Litos G, De Bruijn M, Gutierrez L, et al. Btk is required for an efficient response to erythropoietin and for SCF-controlled protection against TRAIL in erythroid cells. J Exp Med 2004; 199: 785–795
  • Silvestris F, Cafforio P, Tucci M, Dammacco F. Negative regulation of erythroblast maturation by Fas-L(+)/TRAIL(+) highly malignant plasma cells: a major pathogenetic mechanism of anemia in multiple myeloma. Blood 2002; 99: 1305–1313
  • Miyazaki R, Ogata H, Kobayashi Y. Requirement of thrombopoietin-induced activation of ERK for megakaryocyte differentiation and of p38 for erythroid differentiation. Ann Hematol 2001; 80: 284–291
  • Choi J W. Relationships between tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) and hematopoietic activity in healthy adults. Ann Hematol 2005; 84: 728–733
  • Kawamoto H, Minato N. Myeloid cells. Int J Bioch Cell Biol 2004; 36: 1374–1379
  • Ferrari S, Tagliafico E, Ceccherelli G, Selleri L, Calabretta B, Donelli A, et al. Expression of the myeloperoxidase gene in acute and chronic myeloid leukemias: relationship to the expression of cell cycle-related genes. Leukemia 1989; 3: 423–430
  • Schwaller J, Pabst T, Koeffler H P, Niklaus G, Loetscher P, Fey M F, et al. Expression and regulation of G1 cell-cycle inhibitors (p16INK4A, p15INK4B, p18INK4C, p19INK4D) in human acute myeloid leukemia and normal myeloid cells. Leukemia 1997; 11: 54–63
  • Bennett J M, Catovsky D, Daniel M T, Flandrin G, Galton D A, Gralnick H R, et al. Proposals for the classification of the acute leukaemias. French-American-British (FAB) co-operative group. Br J Haematol 1976; 33: 451–458
  • Drexler H G. Classification of acute myeloid leukemias: a comparison of FAB and immunophenotyping. Leukemia 1987; 1: 697–705
  • Ferrari S, Grande A, Manfredini R, Tagliafico E, Zucchini P, Torelli G, et al. Expression of interleukins 1, 3, 6, stem cell factor and their receptors in acute leukemia blast cells and in normal peripheral lymphocytes and monocytes. Eur J Haematol 1993; 50: 141–148
  • Ferrari S, Grande A, Zucchini P, Manfredini R, Tagliafico E, Rossi E, et al. Overexpression of c-kit in a leukemic cell population carrying a trisomy 4 and its relationship with the proliferative capacity. Leuk Lymphoma 1993; 9: 495–501
  • Olsson I, Bergh G, Ehinger M, Gullberg U. Cell differentiation in acute myeloid leukemia. Eur J Haematol 1996; 57: 1–16
  • Irvine A E, Berney J J, Francis G E. Dissociation of the proliferation and differentiation stimuli of granulocyte colony-stimulating factor (G-CSF). Leukemia 1990; 4: 203–209
  • Castaigne S, Chomienne C, Daniel M T, Ballerini P, Berger R, Fenaux P, et al. All-trans retinoic acid as a differentiation therapy for acute promyelocytic leukemia: clinical results. Blood 1990; 76: 1704–1709
  • Chomienne C, Fenaux P, Degos L. Retinoid differentiation therapy in promyelocytic leukemia. FASEB J 1996; 10: 1025–1030
  • Collins S J. The HL-60 promyelocytic leukemia cell line: proliferation, differentiation, and cellular oncogene expression. Blood 1987; 70: 1233–1244
  • Sokoloski J A, Hodnick W F, Mayne S T, Cinquina C, Kim C S, Sartorelli A C. Induction of the differentiation of HL-60 promyelocytic leukemia cells by vitamin E and other antioxidants in combination with low levels of vitamin D3: possible relationship to NF-kappa B. Leukemia 1997; 11: 1546–1553
  • Medupalli A, Li Z, Hromchak R, Bloch A. NF-kappaB (p65/RelA) as a regulator of TNF alpha-mediated ML-1 cell differentiation. Leukemia 2001; 15: 808–813
  • Richter G, Hayden-Ledbetter M, Irgang M, Ledbetter J A, Westermann J, Korner I, et al. Tumor necrosis factor-alpha regulates the expression of inducible costimulator receptor ligand on CD34(+) progenitor cells during differentiation into antigen presenting cells. J Biol Chem 2001; 276: 45686–45693
  • Berry D M, Clark C S, Meckling-Gill K A. 1α,25-dihydroxyvitamin D3 stimulates phosphorylation of IκBα and synergizes with TPA to induce nuclear translocation of NFκB during monocytic differentiation of NB4 leukemia cells. Exp Cell Res 2002; 272: 176–184
  • Wang J, Lenardo M J. Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies. J Cell Sci 2000; 113: 753–757
  • Zermati Y, Garrido C, Amsellem S, Fishelson S, Bouscary D, Valensi F, et al. Caspase activation is required for terminal erythroid differentiation. J Exp Med 2001; 193: 247–254
  • Alam A, Cohen L Y, Aouad S, Sekaly R P. Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J Exp Med 1999; 190: 1879–1890
  • Kennedy N, Kataoka T, Tschopp J, Budd R C. Caspase activation is required for T cell proliferation. J Exp Med 1999; 190: 1891–1895
  • Chun H J, Zheng L, Ahmad M, Wang J, Speirs C K, Siegel R M, et al. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 2002; 419: 395–399
  • Trauzold A, Wermann H, Arlt A, Schutze S, Schafer H, Oestern S, et al. CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells. Oncogene 2001; 20: 4258–4269
  • Chaudhary P M, Eby M T, Jasmin A, Kumar A, Liu L, Hood L. Activation of the NF-kB pathway by caspase 8 and its homologs. Oncogene 2000; 19: 4451–4460
  • Hu W H, Johnson H, Shu H B. Activation of NF-kB by FADD, casper, and caspase 8. J Biol Chem 2000; 275: 10838–10844
  • Rathore N, Matta H, Chaudhary P M. An evolutionary conserved pathway of nuclear factor-kappaB activation involving caspase-mediated cleavage and N-end rule pathway-mediated degradation of IkappaBalpha. J Biol Chem 2004; 279: 39358–39365

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.