Page 236 - Williams Hematology ( PDFDrive )

210 Part IV: Molecular and Cellular Hematology Chapter 15: Apoptosis Mechanisms: Relevance to the Hematopoietic System 211

caspases 1, 4, and 5 in humans) has as its primary role the proteolytic 21. Brunger AT, Adams PD, Clore GM, et al: Crystallography & NMR system: A new
processing and activation of inflammatory cytokines (pro–IL-1β, pro– software suite for macromolecular structure determination. Acta Crystallogr D Biol
Crystallogr 54(Pt 5):905–921, 1998.
IL-18, etc.), with apoptosis representing a secondary function that is 22. Abuamer Y, Ross F, McHugh K, et al: Tumor necrosis factor-a activation of nuclear
observed mostly in the context of excessive stimulation. transcription factor-k-B in marrow macrophages is mediated by C-SRC tyrosine phos-
phorylation of I-k-B-a. J Biol Chem 273(45):29417–29423, 1998.
23. Adams MD, Celniker SE, Holt RA, et al: The genome sequence of Drosophila melano-
CONCLUSIONS gaster. Science 287(5461):2185–2195, 2000.
24. Ng FWH, Nguyen M, Kwan T, et al: p28 Bap31, a Bcl-2/Bcl-X -and procaspase-8-asso-
L
Programmed cell-death mechanisms play critical roles in hematopoietic ciated protein in the endoplasmic reticulum. J Cell Biol 139:327–338, 1997.
and immune cell homeostasis. Elaboration of the complex cell-death 25. Vaux DL, Strasser A: The molecular biology of apoptosis. Proc Natl Acad Sci U S A
93:2239–2244, 1996.
pathways and the networks of proteins that modulate these pathways 26. Chen G, Henter ID, Manji HK: Translational research in bipolar disorder: Emerging
have provided insights into the underlying mechanisms of cell life– insights from genetically based models. Mol Psychiatry 15(9):883–895, 2010.
death decisions, although many mechanistic details remain still to be 27. Salvesen GS, Dixit VM: Caspase activation: The induced-proximity model. Proc Natl
Acad Sci U S A 96:10964–10967, 1999.
revealed. In several cases, the available information has already sparked 28. Youle RJ, Strasser A: The BCL-2 protein family: Opposing activities that mediate cell
efforts to translate the base of information into therapeutic strategies. death. Nat Rev Mol Cell Biol 9(1):47–59, 2008.
Among the experimental therapeutics targeting components of the 29. Demaurex N, Distelhorst C: Apoptosis—The calcium connection. Science 300(5616):
65–67, 2003.
cell death machinery that have entered clinical testing are small mole- 30. Bouillet P, Purton JF, Godfrey DI, et al: BH3-only Bcl-2 family member Bim is required
cule inhibitors of Bcl-2 family and IAP family proteins, as well as large for apoptosis of autoreactive thymocytes. Nature 415(6874):922–926, 2002.
molecule modulators of TNF family DRs. Compounds that modulate 31. Nechushtan A, Smith C, Hsu Y-T, Youle R: Conformation of the Bax C-terminus regu-
lates subcellular location and cell death. EMBO J 18:2330–2341, 1999.
upstream inputs into cell death pathways are also advancing through 32. Muchmore SW, Sattler M, Liang H, et al: X-ray and NMR structure of human Bcl-XL,
clinical evaluations, such as small molecule inhibitors of Mdm2 (which an inhibitor of programmed cell death. Nature 381:335–341, 1996.
cause p53 protein accumulation) and small molecule inhibitors of Akt 33. Chou J, Li H, Salvesen G, et al: Solution structure of BID, an intracellular amplifier of
apoptotic signaling. Cell 96:615–624, 1999.
family kinases. Many other targets within the cell-death pathways are 34. McDonnell JM, Fushman D, Milliman CL, et al: Solution structure of the proapop-
the subject of preclinical drug discovery efforts today. The stage is thus totic molecule BID: A structural basis for apoptotic agonists and antagonists. Cell 96:
set for continued progress in manipulating cell-death pathways for ther- 625–634, 1999.
apeutic benefit of multiple diseases, including disorders of the hemato- 35. Schendel S, Montal M, Reed JC: Bcl-2 family proteins as ion-channels. Cell Death Differ
5:372–380, 1998.
poietic system. 36. Minn AJ, Velez P, Schendel SL, et al: Bcl-x forms an ion channel in synthetic lipid
membranes. Nature 385:353–357, 1997. L
37. Schendel SL, Xie Z, Montal MO, et al: Channel formation by antiapoptotic protein
REFERENCES Bcl-2. Proc Natl Acad Sci U S A 94:5113–5118, 1997.
38. Antonsson B, Conti F, Ciavatta A, et al: Inhibition of Bax channel-forming activity by
1. Kerr JF, Wyllie AH, Currie AR: Apoptosis: A basic biological phenomenon with Bcl-2. Science 277:370–372, 1997.
wide-ranging implications in tissue kinetics. Br J Cancer 26(4):239–257, 1972. 39. Schlesinger P, Gross A, Yin X-M, et al: Comparison of the ion channel characteristics of
2. Thornberry NA, Lazebnik Y: Caspases: Enemies within. Science 281:1312–1316, 1998. proapoptotic BAX and antiapoptotic BCL-2. Proc Natl Acad Sci U S A 94:11357–11362,
3. Cryns V, Yuan Y: Proteases to die for. Genes Dev 12:1551–1570, 1999. 1997.
4. Alnemri ES, Livingston DJ, Nicholson DW, et al: Human ICE/CED-3 Protease Nomen- 40. Schendel S, Azimov R, Pawlowski K, et al: Ion channel activity of the BH3 only Bcl-2
clature. Cell 87:171, 1996. family member, BID. J Biol Chem 274:21932–21936, 1999.
5. Salvesen GS, Dixit VM: Caspases: Intracellular signaling by proteolysis. Cell 91: 41. Kelekar A, Thompson CB: Bcl-2-family proteins—The role of the BH3 domain in apop-
443–446, 1996, 1997. tosis. Trends Cell Biol 8:324–330, 1998.
6. Motyka B, Korbutt G, Pinkoski MJ, et al: Mannose 6-phosphate/insulin-like growth 42. Huang DC, Strasser A: BH3-only proteins-essential initiators of apoptotic cell death.
factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced Cell 103:839–842, 2000.
apoptosis. Cell 103:491–500, 2000. 43. Walensky LD, Pitter K, Morash J, et al: A stapled BID BH3 helix directly binds and
7. Martin SJ, Amarante-Mendes GP, Shi L, et al: The cytotoxic cell protease granzyme activates BAX. Mol Cell 24(2):199–210, 2006.
B initiates apoptosis in a cell-free system by proteolytic processing and activation of 44. Kuwana T, Mackey MR, Perkins G, et al: Bid, bax, and lipids cooperate to form supra-
the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism. EMBO J molecular openings in the outer mitochondrial membrane. Cell 111(3):331–342, 2002.
15(10):2407–2416, 1996. 45. Korsmeyer SJ, Wei MC, Saito M, et al: Pro-apoptotic cascade activates BID, which
8. Zhou Q, Krebs J, Snipas S, et al: Interaction of the baculovirus antiapoptotic protein p35 oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell
with caspases. Specificity, kinetics, and characterization of the caspase/p35 complex. Death Differ 7:1166–1173, 2000.
Biochemistry 37:10757–10765, 1998. 46. Spierings D, McStay G, Saleh M, et al: Connected to death: The (unexpurgated) mito-
9. Quan LT, Caputo A, Bleackley RC, et al: Granzyme B is inhibited by the cowpox virus chondrial pathway of apoptosis. Science 310:66–67, 2005.
serpin cytokine response modifier A. J Biol Chem 270:10377–10379, 1995. 47. Green DR, Kroemer G: The pathophysiology of mitochondrial cell death. Science
10. Sun J, Ooms L, Bird CH, et al: A new family of 10 murine ovalbumin serpins includes 305:626–629, 2004.
two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor 48. Sattler M, Liang H, Nettesheim D, et al: Structure of Bcl-xL-Bak peptide complex:
(proteinase inhibitor 9). J Biol Chem 272:15434–15441, 1997. Recognition between regulators of apoptosis. Science 275:983–986, 1997.
11. Locksley RM, Killeen N, Lenardo MJ: The TNF and TNF receptor superfamilies: Inte- 49. Hetz C, Bernasconi P, Fisher J, et al: Proapoptotic BAX and BAK modulate the unfolded
grating mammalian biology. Cell 104:487–501, 2001. protein response by a direct interaction with IRE1alpha. Science 312:572–576, 2006.
12. Wallach D, Varfolomeev EE, Malinin NL, et al: Tumor necrosis factor receptor and Fas 50. Pattingre S, Tassa A, Qu X, et al: Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent
signaling mechanisms. Annu Rev Immunol 17:331–367, 1999. autophagy. Cell 122(6):927–939, 2005.
13. Yuan J: Transducing signals of life and death. Curr Opin Cell Biol 9:247–251, 1997. 51. Levine B, Kroemer G: Autophagy in the pathogenesis of disease. Cell 132(1):27–42, 2008.
14. Varfolomeev EE, Schuchmann M, Luria V, et al: Targeted disruption of the mouse Cas- 52. Tschopp J, Thome M, Hofmann K, Meinl E: The fight of viruses against apoptosis. Curr
pase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and Opin Genet Dev 8(1):82–87, 1998.
is lethal prenatally. Immunity 9:267–276, 1998. 53. Chang DW, Xing Z, Pan Y, et al: c-FLIP is a dual function regulator for caspase-8
L
15. Reed JC, Doctor KS, Godzik A: The domains of apoptosis: A genomics perspective. Sci activation and CD95-mediated apoptosis. EMBO J 21:3704–3714, 2002.
STKE 2004(239):re9, 2004. 54. Tschopp J, Irmler M, Thome M: Inhibition of Fas death signals by FLIPs. Curr Opin
16. Reed JC: Cytochrome C: Can’t live with it; Can’t live without it. Cell 91:559–562, 1997. Immunol 10:552–558, 1998.
17. Green DR, Reed JC: Mitochondria and apoptosis. Science 281:1309–1312, 1998. 55. Tschopp J, Martinon F, Hofmann K: Apoptosis: Silencing the death receptors. Curr Biol
18. Hakem R, Hakem A, Duncan GS, et al: Differential requirement for caspase 9 in apop- 9:R381-R384.
totic pathways in vivo. Cell 94:339–352, 1998. 56. Vanlangenakker N, Bertrand MJ, Bogaert P, et al: TNF-induced necroptosis in L929
19. Haraguchi M, Torii S, Matsuzawa S, et al: Apoptotic protease activating factor cells is tightly regulated by multiple TNFR1 complex I and II members. Cell Death Dis
(Apaf-1)-independent cell death suppression by Bcl-2. J Exp Med 191:1709–1720, 2:e230, 2011.
2000. 57. Oberst A, Dillon CP, Weinlich R, et al: Catalytic activity of the caspase-8-FLIP(L) com-
20. Kroemer G, Reed JC: Mitochondrial control of cell death. Nat Med 6:513–519, 2000. plex inhibits RIPK3-dependent necrosis. Nature 471(7338):363–367, 2011.

Kaushansky_chapter 15_p0203-0212.indd 211 17/09/15 6:38 pm