Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection

Journal of Cell Science

Volumn 109, Issue 7, 1996, Pages 1727-1738

  Yamamoto, Akitsugu ^a   Masaki, Ryuichi ^a   Tashiro, Yutaka ^a  

^a KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

cDNA transfection; Crystalloid endoplasmic reticulum; Endoplasmic reticulum; Microsomal aldehyde dehydrogenase

Indexed keywords

ALDEHYDE DEHYDROGENASE; CHIMERIC PROTEIN; CHLORAMPHENICOL ACETYLTRANSFERASE; COMPLEMENTARY DNA; MICROSOME ENZYME;

ARTICLE; CELL STRAIN COS1; CONFOCAL LASER MICROSCOPY; CRYSTALLOID; DELETION MUTANT; DNA TRANSFECTION; ELECTRON MICROSCOPY; PRIORITY JOURNAL; ROUGH ENDOPLASMIC RETICULUM; SMOOTH ENDOPLASMIC RETICULUM;

ALDEHYDE DEHYDROGENASE; AMINO ACID SEQUENCE; ANIMALS; COS CELLS; DNA, COMPLEMENTARY; ENDOPLASMIC RETICULUM; GENE EXPRESSION REGULATION; MICROSCOPY, CONFOCAL; MICROSCOPY, ELECTRON; MICROSOMES, LIVER; MOLECULAR SEQUENCE DATA; RATS; TRANSFECTION;

EID: 0029993184     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (45)

1. Akagi, S., Yamamoto, A., Yoshimori, T., Masaki, R., Ogawa, R. and Tashiro, Y. (1988). Distribution of protein disulfide isomerase in rat hepatocytes. J. Histochem. Cytochem. 36, 1533-1542.
2. Anderson, R. G. W., Orci, L., Brown, M. S., Garcia-Segura, L. M. and Goldstein, J. L. (1983). Ultrastructural analysis of crystalloid endoplasmic reticulum in UT-1 cells and its disappearance in response to cholesterol. J. Cell Sci. 63, 1-20.
3. Bassot, J. M. (1966). Une forme microtubulaire et paracristalline de reticulum endoplasmique dans les photocytes des Annelides polynoinæ. J. Cell Biol. 31, 135-158.
4. Bergmann, J. E. and Fusco, P. J. (1990). The G protein of vesicular stomatitis virus has free access into and egress from the smooth endoplasmic reticulum of UT-1 cells. J. Cell Biol. 110, 625-635.
5. Brown, D. A. and Simoni, R. D. (1984). Biogenesis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, an integral glycoprotein of the endoplasmic reticulum. Proc. Nat. Acad. Sci. USA 81, 1674-1678.
6. Chin, D. J., Luskey, K. L., Anderson, R. G. W., Faust, J. R., Goldstein, J. L. and Brown, M. S. (1982). Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc. Nat. Acad. Sci. USA 79, 1185-1189.
7. Chin, D. J., Gil, G., Russell, D. W., Liscum, L., Luskey, K. L., Basu, S. K., Okayama, H., Berg, P., Goldstein, J. L. and Brown, M. S. (1984). Nucleotide sequence of 3-hydroxy-3-methylglutaryl CoA reductase, a glycoprotein of the endoplasmic reticulum. Nature 308, 613-617.
8. Hobman, T. C., Woodward, L. and Farquar, M. G. (1992). The rubella virus EI glycoprotein is arrested in a novel post-ER, pre-Golgi compartment. J. Cell Biol. 118, 795-811.
9. Ishihara, N., Yamashina, S., Sakaguchi, M., Mihara, K. and Omura, T. (1995). Malfolded cytochrome P-450(M1) localized in unusual membrane structures of the endoplasmic reticulum in cultured animal cells. J. Biochem. 118, 397-404.
10. Jingami, H., Brown, M. S., Goldstein, J. L., Anderson, R. G. W. and Luskey, K. L. (1987). Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl-coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum. J. Cell Biol. 104, 1693-1704.
11. Kessel, R. G. (1992). Annulate lamellae: A last frontier in cellular organelles. Int. Rev. Cytol. 133, 43-120.
12. Kochevar, D. T. and Anderson, R. G. W. (1987). Purified crystalloid endoplasmic reticulum from UT-1 cells contains multiple proteins in addition to 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 262, 10321-10326.
13. Kramer, W. and Frits, H.-J. (1987). Oligonucleotide-directed construction of mutations via gapped duplex DNA. Meth. Enzymol. 154, 350-367.
14. Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B. and Kapoport, T. A. (1995). Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J. 14, 217-223.
15. Lippincott-Schwartz J., Yuan, L. C., Bonifacno, J. S. and Klausner, R. D. (1989). Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from the Golgi to ER. Cell 56, 801-813.
16. Liscum, L., Finner-Moore, J., Stroud, R. M., Luskey, K. L., Brown, M. S. and Goldstein, J. L. (1985). Domain structure of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260, 522-530.
17. Luskey, K. L. and Stevens, B. (1985). Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. J. Biol. Chem. 260, 10271-10277.
18. Masaki, R., Yamamoto, A. and Tashiro, Y. (1994). Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids. J. Cell Biol. 126, 1407-1420.
19. Metzelaar, M. J., Wijngaard, P. L. J., Peters, P. J., Sixma, J. J., Nieuwenhuis, H. K. and Clevers, H. C. (1991). CD63 antigen. A novel lysosomal membrane glycoprotein, cloned by a screening procedure for intercellular antigens in eukaryotic cells. J. Biol. Chem. 266, 3239-3245.
20. Misumi, Y., Miki, A., Takatsuki, A., Tamura, G. and Ikehara, Y. (1986). Novel blockage by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol. Chem. 261, 11398-11403.
21. Miyauchi, K., Masaki, R., Taketani, S., Yamamoto, A., Akayama, M. and Tashiro, Y. (1991). Molecular cloning, sequencing and expression of cDNA for rat liver microsomal aldehyde dehydrogenase. J. Biol. Chem. 266, 19536-19542.
22. Nishikawa, S., Hirata, A. and Nakano, A. (1994). Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell 5, 1129-1143.
23. Orci, L., Brown, M. S., Goldstein, J. L., Garcia-Segura, L. M. and Anderson, R. G. W. (1984). Increase in membrane cholesterol: A possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells. Cell 36, 835-845.
24. Orrenius, S., Ericsson, J. L. E. and Ernster, L. (1965). Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic reticulum. A morphological and biochemical study. J. Cell Biol. 25, 627-639.
25. 3) receptor in mouse cerebellar Purkinje cells using three monoclonal antibodies. Cell Struct. Funct. 15, 163-173.
26. Parrish, M. L., Sengstag, C., Rine, J. D. and Wright, R. L. (1995). Identification of the sequence in HMG-CoA reductase required for karmellae assembly. Mol. Biol. Cell 6, 1535-1547.
27. Pathak, R. K., Luskey, K. L. and Anderson, R G. W. (1986). Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: Evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope. J. Cell Biol. 102, 2158-2168.
28. Rajasekaran, A., Morimoto, T., Hanzel, D. K., Rodriguez-Boulan, E. and Kreibich, G. (1993). Structural reorganization of the rough endoplasmic reticulum without size expansion accounts for dexamethasone-induced secretory activity in AR42J cells. J. Cell Sci. 105, 333-345.
29. Raposo, G., Van Santen, H. M., Leijendekker, R., Geuse, H. J. and Ploegh, H. L. (1995). Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 131, 1403-1419.
30. Remmer, H. and Merker, H. J. (1963). Drug-induced changes in the liver endoplasmic reticulum: Association with drug metabolizing enzymes. Science 142, 1657-1658.
31. Roitelman, J., Olender, E. H., Bar-Nun, S., Dunn, W. A. and Simoni, R. D. (1992). Immunological evidence for eight spans in membrane domain of 3-hydroxy-3-methylglutaryl-coenzyme A reductase: Implications for enzyme degradation in the endoplasmic reticulum. J. Cell Biol. 117, 959-973.
32. Satoh, T., Ross, C. A., Villa, A., Supattapone, S., Pozzan, T., Snyder, S. H. and Meldolesi, J. (1990). The inositol 1,4,5-trisphosphate receptor in cerebellar Purkinje cells: Quantitative immunogold labeling reveals concentration in an endoplasmic reticulum subcompartment. J. Cell Biol. 111, 615-624.
33. Sitia, R. and Meldolesi, J. (1992). Endoplasmic reticulum: A dynamic patchwork of specialized subregions. Mol. Biol. Cell 3, 1067-1072.
34. Stäubli, W., Hess, R. and Weibel, E. R. (1969). Correlated morphometric and biochemical studies on the liver cell. II. Effect of phenobarbital on rat hepatocytes. J. Cell Biol. 42, 92-112.
35. Takagi, Y., Ito, A. and Omura, T. (1985). Biogenesis of microsomal aldehyde dehydrogenase in rat liver. J. Biochem. 98, 1647-1652.
36. 2+-ATPase and calsequestrin. J. Neurosci. 12, 489-505.
37. Takei, K., Mignery, G. A., Mugnaini, E., Südhof, T. C. and De Camilli, P. (1994). Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells. Neuron 12, 327-342.
38. 2+-ATPase. Proc. Nat. Acad. Sci. USA 87, 2466-2470.
39. Tokuyasu, K. T. (1986). Application of cryoultramicrotomy to immunocytochemistry. J. Microsc. 143, 139-149.
40. 5 in yeast results in marked proliferation of the intracellular membrane. J. Cell Sci. 106, 249-259.
41. Wiest, D. L., Burkhardt, J. K., Hester, S., Hortsch, M., Meyer, D. I. and Argon, Y. (1990). Membrane biogenesis during B cell differentiation: Most endoplasmic reticulum proteins are expressed coordinately. J. Cell Biol, 110, 1501-1511.
42. Wigler, M., Pellicer, A., Silverstein, S. and Axel, R. (1978). Biochemical transfer of single-copy eukaryotic genes using total cellular DNA as donor. Cell 14, 725-731.
43. Wolf, K. W. and Motzko, D. (1995). Paracrystalline endoplasmic reticulum is typical of gametogenesis in hemiptera species. J. Struct. Biol. 114, 105-114.
44. Wright, R., Basson, M., D'Ari, L. and Rine, J. (1988). Increased amounts of HMG-CoA reductase induce 'Karmellae': A proliferation of stacked membrane pairs surrounding the yeast nucleus. J. Cell Biol. 107, 101-114.
45. 3) receptor in mouse cerebellar Purkinje cells. Cell Struct. Funct. 16, 419-432.