Abstract
Annulate lamellae (AL) are a membranous structure frequently observed in differentiating gametes and tumor cells. In spite of numerous morphological studies, the function and biochemical composition of this membrane system are not well understood. In this study, we have examined the AL membrane system of vinblastine-treated mouse L cells using immunocytochemistry and Western blot analysis. Our results show that antibodies directed against nuclear envelope lamins, i.e., lamins A, B, and C, did not cross react with constituents of the AL membrane system. Furthermore an AL-specific antibody failed to react with the nuclear envelope and reacted minimally producing only a background stain over other cellular components. The data suggest that the AL membrane system has a distinct molecular make-up that is antigenically distinct from that of other subcellular structures.
Full Text
The Full Text of this article is available as a PDF (3.3 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- André-Schwartz J., Datta S. K., Shoenfeld Y., Isenberg D. A., Stollar B. D., Schwartz R. S. Binding of cytoskeletal proteins by monoclonal anti-DNA lupus autoantibodies. Clin Immunol Immunopathol. 1984 May;31(2):261–271. doi: 10.1016/0090-1229(84)90246-0. [DOI] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
- Brown W. J., Farquhar M. G. The mannose-6-phosphate receptor for lysosomal enzymes is concentrated in cis Golgi cisternae. Cell. 1984 Feb;36(2):295–307. doi: 10.1016/0092-8674(84)90223-x. [DOI] [PubMed] [Google Scholar]
- Davis L. I., Blobel G. Identification and characterization of a nuclear pore complex protein. Cell. 1986 Jun 6;45(5):699–709. doi: 10.1016/0092-8674(86)90784-1. [DOI] [PubMed] [Google Scholar]
- Gerace L., Blobel G. Nuclear lamina and the structural organization of the nuclear envelope. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):967–978. doi: 10.1101/sqb.1982.046.01.090. [DOI] [PubMed] [Google Scholar]
- Gerace L., Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 1980 Jan;19(1):277–287. doi: 10.1016/0092-8674(80)90409-2. [DOI] [PubMed] [Google Scholar]
- Gerace L., Blum A., Blobel G. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution. J Cell Biol. 1978 Nov;79(2 Pt 1):546–566. doi: 10.1083/jcb.79.2.546. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gershoni J. M., Palade G. E. Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to a positively charged membrane filter. Anal Biochem. 1982 Aug;124(2):396–405. doi: 10.1016/0003-2697(82)90056-2. [DOI] [PubMed] [Google Scholar]
- Holt G. D., Snow C. M., Senior A., Haltiwanger R. S., Gerace L., Hart G. W. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol. 1987 May;104(5):1157–1164. doi: 10.1083/jcb.104.5.1157. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hsu S. M., Raine L., Fanger H. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem. 1981 Apr;29(4):577–580. doi: 10.1177/29.4.6166661. [DOI] [PubMed] [Google Scholar]
- Kessel R. G., Katow H. Effects of prolonged antitubulin culture on annulate lamellae in mouse alpha L929 fibroblasts. J Morphol. 1984 Mar;179(3):291–304. doi: 10.1002/jmor.1051790307. [DOI] [PubMed] [Google Scholar]
- Kessel R. G. The structure and function of annulate lamellae: porous cytoplasmic and intranuclear membranes. Int Rev Cytol. 1983;82:181–303. doi: 10.1016/s0074-7696(08)60826-8. [DOI] [PubMed] [Google Scholar]
- Krishan A., Hsu D., Hutchins P. Hypertrophy of granular endoplasmic reticulum and annulate lamellae in Earle's L cells exposed to vinblastine sulfate. J Cell Biol. 1968 Oct;39(1):211–216. doi: 10.1083/jcb.39.1.211. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krohne G., Franke W. W., Scheer U. The major polypeptides of the nuclear pore complex. Exp Cell Res. 1978 Oct 1;116(1):85–102. doi: 10.1016/0014-4827(78)90067-8. [DOI] [PubMed] [Google Scholar]
- Lerner M. R., Boyle J. A., Hardin J. A., Steitz J. A. Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus. Science. 1981 Jan 23;211(4480):400–402. doi: 10.1126/science.6164096. [DOI] [PubMed] [Google Scholar]
- Maul G. G. Annulate lamellae and single pore complexes in normal, SV40-transformed and tumor cells in vitro. A semiquantitative analysis. Exp Cell Res. 1977 Feb;104(2):233–245. doi: 10.1016/0014-4827(77)90087-8. [DOI] [PubMed] [Google Scholar]
- Maul G. G. The nuclear and the cytoplasmic pore complex: structure, dynamics, distribution, and evolution. Int Rev Cytol Suppl. 1977;(6):75–186. [PubMed] [Google Scholar]
- McKeon F. D., Tuffanelli D. L., Kobayashi S., Kirschner M. W. The redistribution of a conserved nuclear envelope protein during the cell cycle suggests a pathway for chromosome condensation. Cell. 1984 Jan;36(1):83–92. doi: 10.1016/0092-8674(84)90076-x. [DOI] [PubMed] [Google Scholar]
- McLean I. W., Nakane P. K. Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem. 1974 Dec;22(12):1077–1083. doi: 10.1177/22.12.1077. [DOI] [PubMed] [Google Scholar]
- Merril C. R., Goldman D., Sedman S. A., Ebert M. H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science. 1981 Mar 27;211(4489):1437–1438. doi: 10.1126/science.6162199. [DOI] [PubMed] [Google Scholar]
- Park M. K., D'Onofrio M., Willingham M. C., Hanover J. A. A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6462–6466. doi: 10.1073/pnas.84.18.6462. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Reeves W. H., Chaudhary N., Salerno A., Blobel G. Lamin B autoantibodies in sera of certain patients with systemic lupus erythematosus. J Exp Med. 1987 Mar 1;165(3):750–762. doi: 10.1084/jem.165.3.750. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwartz R. S., Stollar B. D. Origins of anti-DNA autoantibodies. J Clin Invest. 1985 Feb;75(2):321–327. doi: 10.1172/JCI111704. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Snow C. M., Senior A., Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol. 1987 May;104(5):1143–1156. doi: 10.1083/jcb.104.5.1143. [DOI] [PMC free article] [PubMed] [Google Scholar]
