Synthesis of aminophospholipids in Saccharomyces cerevisiae and Chinese hamster ovary cells. From mutagenesis to genes and cellular function

• Autorzy: Lenart J. , Pikula S.
• Języki publikacji: EN

Abstrakty

EN

The purpose of this article is to provide a concise overview of the characterization of auxotrophic mutated cells to the precursors of lipid synthesis, and of the identification of specific genes encoding enzymatic proteins involved in this process. The focus is on enzymes catalyzing the synthesis of phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae and Chinese hamster ovary cells, two cell types frequently used by investigators studying the mechanisms of genetic control of metabolic processes.

Słowa kluczowe

EN

Chinese hamster; phosphatidylethanolamine; intracellular membrane; enzyme; mutant; gene; lipid; metabolic process; tissue; genetic control; yeast; phospholipid synthesis; cell; mutagenesis; hamster; Saccharomyces cerevisiae; ovarian cell; regulation; plasma; yeast mutant; protein; cellular function; phosphatidylserine; aminophospholipid; cell type

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1998
• Tom: 03
• Numer: 3
• Opis fizyczny: p.223-236,fig.

Twórcy

autor

Lenart J.

• Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland

autor

Pikula S.

Bibliografia

• 1. Berridge, M. J. Annu. Rev. Biochem. 56 (1987) 159-193
• 2. Hurley, J. B. Nature 373 (1995) 194
• 3. Dowhan, W. Annu. Rev. Biochem. 66 (1997) 199-232
• 4. Esko, J. D. and Raetz, C. R. H. Proc. Natl. Acad. Sci. USA 75 (1978) 1190- 1193
• 5. Kinney, A. J. and Carman, G. M. Proc. Natl. Acad. Sci. USA 85 (1988) 7962-7966
• 6. Henry, S. A. in: The molecular biology of the yeast Saccharomyces: Metabolism and gene expression (Strathem, J. N., Jones, E. W. and Broach, J. R., Eds.) Cold Spring Harbor, 1982, 101-158
• 7. Ohtsuka, T., Nishijima, M. and Akamatsu, Y. J. Biol. Chem. 268 (1993) 22908-22913
• 8. Gaigg, B., Simbeni, R., Hrastnik, C., Paltauf, F. and Daum, G. Biochim. Biophys. Acta 1234 (1995) 214-220
• 9. Achleitner, G., Zweytick, D., Trotter, P. J., Voelker, D. R. and Daum, G. J. Biol. Chem. 270 (1995) 29836-29842
• 10. Swairjo, M. A. and Seaton, B. A. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 193-213
• 11. Mattai, J. Hauser, H. Demel, R. A. and Shipley, G. G. Biochemistry 28 (1989) 2322-2330
• 12. Haverstick, D. M. and Glaser, M. Proc. Natl. Acad. Sci. USA 84 (1987) 4475- 4479
• 13. Smeets, E. F. Comfurius, P., Bevers, E. M. and Zwaal, R. F. A. Biochim. Biophys. Acta 1195 (1994) 281-286
• 14. Kent, C. Annu. Rev. Biochem. 64 (1995) 315-343
• 15. Nikoloff, D. M. and Henry, S. A. Annu. Rev. Genet. 25 (1991) 559-583.
• 16. Silbert, D. F. Annu. Rev. Biochem. 44 (1975) 315-339
• 17. Schwaitzer, E. and Bolling, H. Proc. Natl. Acad. Sci. USA 67 (1970) 660-666
• 18. Swede, M. J., Hudak, K. A., Lopes, J. M. and Henry, S. A. Meth. Enzymol. 209 (1992) 21-34
• 19. Letts, V. A. and Dawes, I. W. Biochem. Soc. Trans. 7 (1979) 976-977
• 20. Nikawa, J-I. and Yamashita, S. Biochim. Biophys. Acta 665 (1981) 420-426
• 21. Kovac, L., Gbelska, I., Poliachova, V., Subik, J. and Kovacova, V. Eur. J. Biochem. 111 (1980) 491-501
• 22. Atkinson, K., Fogel, S. and Henry, S. A. J. Biol. Chem. 255 (1980) 6653-6661
• 23. Hamamatsu, S., Shibuya, I., Takagi, M. and Ohta, A. FEBS Lett. 348 (1994) 33-36
• 24. Letts, V. A., Klig, L. S., Bae-Lee, M., Carman, G. M. and Henry, S. A. Proc. Natl. Acad. Sci. USA 80 (1983) 7279-7283
• 25. Yamashita, S. and Nikawa, J-I. Biochim. Biophys. Acta 1348 (1997) 228-235
• 26. Sperka-Gottlieb, C., Fasch, E-V., Kuchler, K., Bailis, A. M., Henry, S. A., Paltauf, F. and Kohlwein, S. D. Yeast 6 (1990) 331-343
• 27. Trotter, P. J., Pedretti, J. and Voelker, D. R. J. Biol .Chem. 268 (1993) 21416-21424
• 28. Clancey, C. J., Chang, S. C. and Dowhan, W. J. Biol. Chem. 268 (1993) 24580- 24590
• 29. Trotter, P. J. and Voelker, D. R. J. Biol. Chem. 270 (1995) 6062-6070
• 30. Trotter, P. J., Pedretti, J., Yates, R. and Voelker, D. R. J. Biol. Chem. 270 (1995) 6071-6080
• 31. Mewes, W., Albermann, K., Bahr, M., Frishman, D., Gleissner, A., Hani, J., Heumann, K., Kleine, K., Maieri, A., Oliver, S. G., Pfeiffer, F. and Zollner, A. Nature 387 (suppl.) (1997) 7-74
• 32. Kao, F-T. and Puck, T. T. Proc. Natl. Acad. Sci. USA 60 (1968) 1275-1281
• 33. Kanfer, J. N. and McCartney, D. FEBS Lett. 291 (1991) 63-66
• 34. Kanfer, J. N. and McCartney, D. J. Neurochem. 60 (1993) 1228-1235
• 35. Jasinska, R., Rakowska, M., Lenart, J., Komanska, I. and Pikula, S. FEBS Lett. 386 (1996) 33-38
• 36. Makowski, P., Szewczyk, A., Jasinska, R. and Pikula, S. FEBS Lett. 409 (1997) 292-296
• 37. Wiktorek-Wojcik, M., Banasiak, M., Czarny, M., Stepkowski, D. and Baranska, J. Biochem. Biophys. Res. Commun. 241 (1997) 73-78
• 38. Miller, M. A. and Kent, C. J. Biol. Chem. 261 (1986) 9753-9761
• 39. Voelker, D. R. and Frazier, J. L. J. Biol. Chem. 261 (1986) 1002-1008
• 40. Nishijima, M., Kuge, O. and Akamatsu, Y. J. Biol. Chem. 261 (1986) 5784- 5789
• 41. Kuge, O., Nishijima, M. and Akamatsu, Y. J .Biol. Chem. 261 (1986) 5790-5794
• 42. Kuge, O., Nishijima, M. and Akamatsu, Y. J. Biol. Chem. 261 (1986) 5795-5798
• 43. Hasegawa, K., Kuge, O., Nishijima, M. and Akamatsu, Y. J. Biol. Chem. 264 (1989) 19887-19892
• 44. Kuge, O., Nishijima, M. and Akamatsu, Y. J. Biol. Chem. 266 (1991) 24184-24189
• 45. Saito, K., Kuge, O., Akamatsu, Y. and Nishijima, M. FEBS Lett. 395 (1996) 262-266
• 46. Kuge, O., Nishijima, M. and Akamatsu, Y. J. Biol. Chem. 266 (1991) 6370- 6376
• 47. Kuge, O., Saito, K., Koima, M., Akamatsu, Y. and Nishijima, M. Biochem. J. 319 (1996) 33-38
• 48. Suzuki, T. T. and Kanfer, J. J. Biol. Chem. 260 (1985) 1394-1399
• 49. Kuge, O. and Nishijima, M. Biochim. Biophys. Acta 1348 (1997) 151-156
• 50. Rakowska, M., Jasinska, R., Lenart, J., Komanska, I., Makowski, P., Dygas, A. and Pikula, S. Mol. Cell. Biochem. 168 (1997) 163-176
• 51. Lenart, J., Komanska, I., Jasinska, R. and Pikula, S. Acta Biochim. Polon. 45 (1998) 119-126
• 52. Ellingson, J. S. and Seenaiah, B. Biochim. Biophys. Acta 1213 (1994) 113-117
• 53. Sundler, R. and Akessson, B. J. Biol. Chem. 250 (1975) 3359-3367
• 54. Carman, G. M. and Henry, S. A. Annu. Rev. Biochem. 58 (1989) 635-669
• 55. Kai, M., Wada, I., Imai, S-I., Sanake, F. and Kanoh, H. J. Biol. Chem. 271 (1996) 18931-18938
• 56. Shen, H., Heacock, P. N., Clancey, C. J. and Dowhan, W. J. Biol. Chem. 271 (1996) 789-795
• 57. Uchida, T. and Yamashita, S. J. Biol. Chem. 267 (1992) 10156-10162
• 58. Nishijima, M., Kuge, O. and Hanada, K. Trends Cell Biol. 7 (1997) 324-329
• 59. Pavlidis, P., Ramaswami, M. and Tanouye, M. A. Cell 79 (1994) 23-33
• 60. Hjelmstad, R. H., Morash, S. C., McMaster, C. R. and Bell, R. M. J. Biol. Chem. 269 (1994) 20995-21002
• 61. Hosaka, K., Tanaka, S., Nikawa, J. and Yamashita, S. FEBS Lett. 304 (1992) 229-232
• 62. Morash, S. C., McMaster, C. R., Hjelmstad, R. H. and Bell, R. M. J. Biol. Chem. 269 (1994) 28769-28776
• 63. McMaster, C. R. and Bell, R. M. J. Biol. Chem. 269 (1994) 28010-28016
• 64. Cui, Z., Vance, J. E., Chen, M. H., Voelker, D. R. and Vance, D. E. J. Biol. Chem. 268 (1993) 16655-16663
• 65. Nakashima, A., Hosaka, K. and Nikawa, J. J. Biol. Chem. 272 (1997) 9567- 9572
• 66. Vance, J. E. and Vance, D. E. Experientia 46 (1990) 560-569
• 67. Vance, J. E. and Vance, D. E. J. Biol. Chem. 261 (1986) 4486-4491