Dissecting the pathways of doom - application of spectroscopy in the study of cell death and survival

• Autorzy: Godlewski M. , Gorka M. , Gajkowska B. , Wojewodzka U.
• Języki publikacji: EN

Abstrakty

EN

Biological studies rely on measurements performed on large populations, which allow the statistic evaluation of gathered data. On the other hand, the need to precisely localize observed processes and the facts occurring in the microscale results in the need of high resolution qualitative imaging. These two approaches are complementary and without anyone of them no valuable experimental data can be gathered from studies of fluorescent dyes. Both approaches are based on common origin of laser-induced fluorescence, but due to the method of analysis they split into the quantitative (laser scanning cytometry) and qualitative (confocal microscopy) fields of research.

Słowa kluczowe

EN

spectroscopy; laser scanning cytometry; confocal microscopy; programmed cell death

• Wydawca: Oficyna Wydawnicza Politechniki Wrocławskiej
• Czasopismo: Optica Applicata
• Rocznik: 2006
• Tom: Vol. 36, nr 2-3
• Strony: 257--270
• Opis fizyczny: Bibliogr.22 poz.,

Twórcy

autor

Godlewski M.

autor

Gorka M.

autor

Gajkowska B.

autor

Wojewodzka U.

• Warsaw Agricultural University, Nowoursynowska 159, 02-776 Warsaw Poland

Bibliografia

• [1] KIM J.K., LEE C.J., SONG K.W., DO B.R., YOON Y.D., Gamma-radiation accelerates ovarian follicular atresia in immature mice, In Vivo 13(1), 1999, pp. 21–4.
• [2] GODLEWSKI M.M., MOTYL M.A., GAJKOWSKA B., WARĘSKI P., KORONKIEWICZ M., MOTYL T., Subcellular redistribution of BAX during apoptosis induced by anticancer drugs, Anti-Cancer Drugs 12(7), 2001, pp. 607–17.
• [3] GÓRKA M., DANIEWSKI W.M., GAJKOWSKA B., ŁYSAKOWSKA E., GODLEWSKI M.M., MOTYL T., Autophagy is the dominant type of programmed cell death in breast cancer MCF-7 cells exposed to AGS 115 and EFDAC, new sesquiterpene analogs of paclitaxel, Anti-Cancer Drugs 16(7), 2005, pp. 777–88.
• [4] ZIMOWSKA W., MOTYL T., WARĘSKI P., SKIERSKI J., PŁOSZAJ T., ORZECHOWSKI A., Apoptosis induced by serum deprivation and apoptogenic factors of cellular origin is dependent on bcl-2 and bax expression in L1210 leukaemic cells, Polish Journal of Veterinary Sciences 3(1), 2000, pp. 63–7.
• [5] SHIMIZU S., IDE T., YANAGIDA T., TSUJIMOTO Y., Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c, Journal of Biological Chemistry 275(16), 2000, pp. 12321–5.
• [6] GROSS A., YIN X.M., WANG K., WEI M.C., JOCKEL J., MILLIMAN C., ERDJUMENT-BROMAGE H., TEMPST P., KORSMEYER S.J., Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death, Journal of Biological Chemistry 274(2), 1999, pp. 1156–63.
• [7] SHIMIZU S, NARITA M., TSUJIMOTO Y., Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC, Nature 399(6735), 1999, pp. 483–7.
• [8] SRINIVASULA S.M., AHMAD M., FERNANDES-ALNEMRI T., ALNEMRI E.S., Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization, Molecular Cell 1(7), 1998, pp. 949–57.
• [9] CECCONI F., Apaf1 and the apoptotic machinery, Cell Death and Differentiation 6(11), 1999, pp. 1087–98.
• [10] CAIN K., BROWN D.G., LANGLAIS C., COHEN G.M., Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex, Journal of Biological Chemistry 274(32), 1999, pp. 22686–92.
• [11] SHI Y., A structural view of mitochondria-mediated apoptosis, Nature Structural Biology 8(5), 2001, pp. 394–401.
• [12] SLEE E.A., HARTE M.T., KLUCK R.M., WOLF B.B., CASIANO C.A., NEWMAYER D.D., WANG H.G., REED J.C., NICHOLSON D.W., ALNEMRI E.S., GREEN D.R., MARTIN S.J., Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner, Journal of Cell Biology 144(2), 1999, pp. 281–92.
• [13] DATTA R., OKI E., ENDO K., BIEDERMANN V., REN J., KUFE D., XIAP regulates DNA damage-induced apoptosis downstream of caspase-9 cleavage, Journal of Biological Chemistry 275(41), 2000, pp. 31733–8.
• [14] SRINIVASULA S.M., DATTA P., FAN X.J., FERNANDES-ALNEMRI T., HUANG Z., ALNEMRI E.S., Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway, Journal of Biological Chemistry 275(46), 2000, pp. 36152–7.
• [15] HIROTANI M., ZHANG Y., FUJITA N., NAITO M., TSURUO T., NH2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis, Journal of Biological Chemistry 274(29), 1999, pp. 20415–20.
• [16] MIKHAILOV V., MIKHAILOVA M., PULKRABEK D.J., DONG Z., VENKATACHALAM M.A., SAIKUMAR P., Bcl-2 prevents Bax oligomerization in the mitochondrial outer membrane, Journal of Biological Chemistry 276(21), 2001, pp. 18361–74.
• [17] YOSHIMORI T., Autophagy: a regulated bulk degradation process inside cells, Biochemical and Biophysical Research Communications 313(2), 2004, pp. 453–8.
• [18] MEIJER A.J., CODOGNO P., Regulation and role of autophagy in mammalian cells, The International Journal of Biochemistry and Cell Biology 36(12), 2004, pp. 2445–62.
• [19] GOZUACIK D., KIMCHI A., Autophagy as a cell death and tumor suppressor mechanism, Oncogene 23(16), 2004, pp. 2891–906.
• [20] GODLEWSKI M.M., GÓRKA M., LAMPARSKA-PRZYBYSZ M., MOTYL T., Minute kinetics of proapoptotic proteins: BAX and Smac/DIABLO in living tumor cells revealed by homeostatic confocal microscopy, Cytotechnology 45(3), 2004, pp. 141–53.
• [21] GODLEWSKI M.M., GAJKOWSKA B., LAMPARSKA-PRZYBYSZ M., MOTYL T., Colocalization of BAX with BID and VDAC-1 in nimesulide-induced apoptosis of human colon adenocarcinoma COLO 205 cells, Anti-Cancer Drugs 13(10), 2002, pp. 1017–29.
• [22] GÓRKA M., GODLEWSKI M.M., GAJKOWSKA B., WOJEWÓDZKA U., MOTYL T., Kinetics of Smac/DIABLO release from mitochondria during apoptosis of MCF-7 breast cancer cells, Cell Biology International 28(11), 2004, pp. 741–54.