Abstract
The Golgi apparatus is a key element in the ordered movement of secretory polypeptides from the rough endoplasmic reticulum to the plasma membrane during secretion. It has been shown that cisternae that receive membranes from the reticulum are morphologically similar to the latter and that cisternae liberating secretory granules resemble that plasma membrane. By using an ultrastructural probe for membrane cholesterol, filipin, on freeze-fractured and thin-sectioned exocrine and endocrine pancreatic cells, we have shown that an enrichment in filipin-cholesterol complexes takes places across the stacked cisternae of the Golgi apparatus; the reticulum-related (forming) cisternae are poor in such complexes, but the secretory granule-related (maturing) cisternae contain numerous complexes. Secretory granule membrane is also richly labeled with filipin-cholesterol complexes. The heterogeneous cholesterol distribution in the membranes of the Golgi apparatus, as shown by filipin, emphasizes the polarity of this organelle, in agreement with its role in organizing the traffic of the secretory polypeptides from the rough endoplasmic reticulum to the plasma membrane.
Full text
PDF




Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Amar-Costesec A., Wibo M., Thinès-Sempoux D., Beaufay H., Berthet J. Analytical study of microsomes and isolated subcellular membranes from rat liver. IV. Biochemical, physical, and morphological modifications of microsomal components induced by digitonin, EDTA, and pyrophosphate. J Cell Biol. 1974 Sep;62(3):717–745. doi: 10.1083/jcb.62.3.717. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Andrews L. D., Cohen A. I. Freeze-fracture evidence for the presence of cholesterol in particle-free patches of basal disks and the plasma membrane of retinal rod outer segments of mice and frogs. J Cell Biol. 1979 Apr;81(1):215–228. doi: 10.1083/jcb.81.1.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bergeron J. J., Ehrenreich J. H., Siekevitz P., Palade G. E. Golgi fractions prepared from rat liver homogenates. II. Biochemical characterization. J Cell Biol. 1973 Oct;59(1):73–88. doi: 10.1083/jcb.59.1.73. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Borgese N., Meldolesi J. Localization and biosynthesis of NADH-cytochrome b5 reductase, an integral membrane protein, in rat liver cells. I. Distribution of the enzyme activity in microsomes, mitochondria, and golgi complex. J Cell Biol. 1980 Jun;85(3):501–515. doi: 10.1083/jcb.85.3.501. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cheng H., Farquhar M. G. Presence of adenylate cyclase activity in Golgi and other fractions from rat liver. II. Cytochemical localization within Golgi and ER membranes. J Cell Biol. 1976 Sep;70(3):671–684. doi: 10.1083/jcb.70.3.671. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elias P. M., Friend D. S., Goerke J. Membrane sterol heterogeneity. Freeze-fracture detection with saponins and filipin. J Histochem Cytochem. 1979 Sep;27(9):1247–1260. doi: 10.1177/27.9.479568. [DOI] [PubMed] [Google Scholar]
- FRIEND D. S., MURRAY M. J. OSMIUM IMPREGNATION OF THE GOLGI APPARATUS. Am J Anat. 1965 Jul;117:135–149. doi: 10.1002/aja.1001170109. [DOI] [PubMed] [Google Scholar]
- Farquhar M. G., Bergeron J. J., Palade G. E. Cytochemistry of Golgi fractions prepared from rat liver. J Cell Biol. 1974 Jan;60(1):8–25. doi: 10.1083/jcb.60.1.8. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Friend D. S. Cytochemical staining of multivesicular body and golgi vesicles. J Cell Biol. 1969 Apr;41(1):269–279. doi: 10.1083/jcb.41.1.269. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Grove S. N., Bracker C. E., Morré D. J. Cytomembrane differentiation in the endoplasmic reticulum-Golgi apparatus-vesicle complex. Science. 1968 Jul 12;161(3837):171–173. doi: 10.1126/science.161.3837.171. [DOI] [PubMed] [Google Scholar]
- Hand A. R. Morphology and cytochemistry of the Golgi apparatus of rat salivary gland acnar cells. Am J Anat. 1971 Feb;130(2):141–157. doi: 10.1002/aja.1001300203. [DOI] [PubMed] [Google Scholar]
- Jamieson J. D., Palade G. E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J Cell Biol. 1967 Aug;34(2):577–596. doi: 10.1083/jcb.34.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Keenan T. W., Morré D. J. Phospholipid class and fatty acid composition of golgi apparatus isolated from rat liver and comparison with other cell fractions. Biochemistry. 1970 Jan 6;9(1):19–25. doi: 10.1021/bi00803a003. [DOI] [PubMed] [Google Scholar]
- Kinsky S. C. Antibiotic interaction with model membranes. Annu Rev Pharmacol. 1970;10:119–142. doi: 10.1146/annurev.pa.10.040170.001003. [DOI] [PubMed] [Google Scholar]
- Lacy P. E., Kostianovsky M. Method for the isolation of intact islets of Langerhans from the rat pancreas. Diabetes. 1967 Jan;16(1):35–39. doi: 10.2337/diab.16.1.35. [DOI] [PubMed] [Google Scholar]
- Meldolesi J., Jamieson J. D., Palade G. E. Composition of cellular membranes in the pancreas of the guinea pig. 3. Enzymatic activities. J Cell Biol. 1971 Apr;49(1):150–158. doi: 10.1083/jcb.49.1.150. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meldolesi J., Jamieson J. D., Palade G. E. Composition of cellular membranes in the pancreas of the guinea pig. II. Lipids. J Cell Biol. 1971 Apr;49(1):130–149. doi: 10.1083/jcb.49.1.130. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Montesano R., Perrelet A., Vassalli P., Orci L. Absence of filipin-sterol complexes from large coated pits on the surface of culture cells. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6391–6395. doi: 10.1073/pnas.76.12.6391. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morré D. J., Kartenbeck J., Franke W. W. Membrane flow and intercoversions among endomembranes. Biochim Biophys Acta. 1979 Apr 23;559(1):71–52. doi: 10.1016/0304-4157(79)90008-x. [DOI] [PubMed] [Google Scholar]
- Morré D. J., Ovtracht L. Dynamics of the Golgi apparatus: membrane differentiation and membrane flow. Int Rev Cytol Suppl. 1977;(5):61–188. [PubMed] [Google Scholar]
- Norman A. W., Demel R. A., de Kruyff B., van Deenen L. L. Studies on the biological properties of polyene antibiotics. Evidence for the direct interaction of filipin with cholesterol. J Biol Chem. 1972 Mar 25;247(6):1918–1929. [PubMed] [Google Scholar]
- Norman A. W., Spielvogel A. M., Wong R. G. Polyene antibiotic - sterol interaction. Adv Lipid Res. 1976;14:127–170. [PubMed] [Google Scholar]
- Novikoff A. B., Novikoff P. M. Cytochemical contributions to differentiating GERL from the Golgi apparatus. Histochem J. 1977 Sep;9(5):525–551. doi: 10.1007/BF01002901. [DOI] [PubMed] [Google Scholar]
- Novikoff P. M., Novikoff A. B., Quintana N., Hauw J. J. Golgi apparatus, GERL, and lysosomes of neurons in rat dorsal root ganglia, studied by thick section and thin section cytochemistry. J Cell Biol. 1971 Sep;50(3):859–886. doi: 10.1083/jcb.50.3.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Orci L. A portrait of the pancreatic B-cell. The Minkowski Award Lecture delivered on July 19, 1973, during the 8th Congress of the International Diabetes Federation, held in Brussels, Belgium. Diabetologia. 1974 Jun;10(3):163–187. doi: 10.1007/BF00423031. [DOI] [PubMed] [Google Scholar]
- Orci L., Miller R. G., Montesano R., Perrelet A., Amherdt M., Vassalli P. Opposite polarity of filipin-induced deformations in the membrane of condensing vacuoles and zymogen granules. Science. 1980 Nov 28;210(4473):1019–1021. doi: 10.1126/science.7434010. [DOI] [PubMed] [Google Scholar]
- Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
- Robinson J. M., Karnovsky M. J. Evaluation of the polyene antibiotic filipin as a cytochemical probe for membrane cholesterol. J Histochem Cytochem. 1980 Feb;28(2):161–168. doi: 10.1177/28.2.6766487. [DOI] [PubMed] [Google Scholar]
- Staehelin L. A., Kiermayer O. Membrane differentiation in the Golgi complex of Micrasterias denticulata Bréb. visualized by freeze-etching. J Cell Sci. 1970 Nov;7(3):787–792. doi: 10.1242/jcs.7.3.787. [DOI] [PubMed] [Google Scholar]
- Tillack T. W., Kinsky S. C. A freeze-etch study of the effects of filipin on liposomes and human erythrocyte membranes. Biochim Biophys Acta. 1973 Sep 27;323(1):43–54. doi: 10.1016/0005-2736(73)90430-6. [DOI] [PubMed] [Google Scholar]
- Verkleij A. J., de Kruijff B., Gerritsen W. F., Demel R. A., van Deenen L. L., Ververgaert P. H. Freeze-etch electron microscopy of erythrocytes, Acholeplasma laidlawii cells and liposomal membranes after the action of filipin and amphotericin B. Biochim Biophys Acta. 1973 Jan 26;291(2):577–581. doi: 10.1016/0005-2736(73)90509-9. [DOI] [PubMed] [Google Scholar]
- Whaley W. G., Dauwalder M. The Golgi apparatus, the plasma membrane, and functional integration. Int Rev Cytol. 1979;58:199–245. doi: 10.1016/s0074-7696(08)61476-x. [DOI] [PubMed] [Google Scholar]
- Yunghans W. N., Keenan T. W., Morré D. J. Isolation of golgi apparatus from rat liver. 3. Lipid and protein composition. Exp Mol Pathol. 1970 Feb;12(1):36–45. doi: 10.1016/0014-4800(70)90073-0. [DOI] [PubMed] [Google Scholar]
- de Kruijff B., Gerritsen W. J., Oerlemans A., Demel R. A., van Deenen L. L. Polyene antibiotic-sterol interactions in membranes of Acholeplasma laidlawii cells and lecithin liposomes. I. Specificity of the membrane permeability changes induced by the polyene antibiotics. Biochim Biophys Acta. 1974 Feb 26;339(1):30–43. doi: 10.1016/0005-2736(74)90330-7. [DOI] [PubMed] [Google Scholar]