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. 1982 Sep 1;94(3):743–748. doi: 10.1083/jcb.94.3.743

Putative 51,000-Mr protein marker for postsynaptic densities is virtually absent in cerebellum

PMCID: PMC2112213  PMID: 7130281

Abstract

Cerebrum and cerebellum contain numerous asymmetric synapses characterized by the presence of a postsynaptic thickening prominently stained by phosphotungstic acid and other electron-dense stains suitable for electron microscopy. A 51,000-Mr protein, copurified in postsynaptic density-enriched fractions from cerebrum, is considered to be a well established marker for the postsynaptic density. On the basis of two criteria, our studies demonstrate that the 51,000-Mr protein marker for postsynaptic densities is virtually absent in cerebellum, First, it is present in negligible amounts in deoxycholate-insoluble fractions from cerebellum but abundant in parallel fractions from cerebrum. Secondly, the 51,000-Mr protein, which binds 125I-calmodulin after SDS PAGE is readily visualized in membrane samples from cerebrum but is virtually undetectable in cerebellar samples. It is apparent that these results require reexamination of the role of the 51,000-Mr protein in postsynaptic density structures.

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Selected References

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  1. Acton R. T., Addis J., Carl G. F., McClain L. D., Bridgers W. F. Association of Thy-1 differentiation alloantigen with synaptic complexes isolated from mouse brain. Proc Natl Acad Sci U S A. 1978 Jul;75(7):3283–3287. doi: 10.1073/pnas.75.7.3283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andreasen T. J., Keller C. H., LaPorte D. C., Edelman A. M., Storm D. R. Preparation of azidocalmodulin: a photoaffinity label for calmodulin-binding proteins. Proc Natl Acad Sci U S A. 1981 May;78(5):2782–2785. doi: 10.1073/pnas.78.5.2782. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blomberg F., Cohen R. S., Siekevitz P. The structure of postsynaptic densities isolated from dog cerebral cortex. II. Characterization and arrangement of some of the major proteins within the structure. J Cell Biol. 1977 Jul;74(1):204–225. doi: 10.1083/jcb.74.1.204. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bloom F. E., Ueda T., Battenberg E., Greengard P. Immunocytochemical localization, in synapses, of protein I, an endogenous substrate for protein kinases in mammalian brain. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5982–5986. doi: 10.1073/pnas.76.11.5982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Carlin R. K., Grab D. J., Cohen R. S., Siekevitz P. Isolation and characterization of postsynaptic densities from various brain regions: enrichment of different types of postsynaptic densities. J Cell Biol. 1980 Sep;86(3):831–845. doi: 10.1083/jcb.86.3.831. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Carlin R. K., Grab D. J., Siekevitz P. Function of a calmodulin in postsynaptic densities. III. Calmodulin-binding proteins of the postsynaptic density. J Cell Biol. 1981 Jun;89(3):449–455. doi: 10.1083/jcb.89.3.449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Carlin R. K., Grab D. J., Siekevitz P. Postmortem accumulation of tubulin in postsynaptic density preparations. J Neurochem. 1982 Jan;38(1):94–100. doi: 10.1111/j.1471-4159.1982.tb10858.x. [DOI] [PubMed] [Google Scholar]
  8. Celio M. R., Heizmann C. W. Calcium-binding protein parvalbumin as a neuronal marker. Nature. 1981 Sep 24;293(5830):300–302. doi: 10.1038/293300a0. [DOI] [PubMed] [Google Scholar]
  9. Cohen R. S., Blomberg F., Berzins K., Siekevitz P. The structure of postsynaptic densities isolated from dog cerebral cortex. I. Overall morphology and protein composition. J Cell Biol. 1977 Jul;74(1):181–203. doi: 10.1083/jcb.74.1.181. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Colonnier M. Synaptic patterns on different cell types in the different laminae of the cat visual cortex. An electron microscope study. Brain Res. 1968 Jul;9(2):268–287. doi: 10.1016/0006-8993(68)90234-5. [DOI] [PubMed] [Google Scholar]
  11. Cotman C. W., Banker G., Churchill L., Taylor D. Isolation of postsynaptic densities from rat brain. J Cell Biol. 1974 Nov;63(2 Pt 1):441–455. doi: 10.1083/jcb.63.2.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Elder J. H., Pickett R. A., 2nd, Hampton J., Lerner R. A. Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein. J Biol Chem. 1977 Sep 25;252(18):6510–6515. [PubMed] [Google Scholar]
  13. Flanagan S. D., Storni A. An 125I-labeled binding probe for the muscarinic cholinergic receptor. Brain Res. 1979 May 25;168(2):261–274. doi: 10.1016/0006-8993(79)90168-9. [DOI] [PubMed] [Google Scholar]
  14. GRAY E. G. Axo-somatic and axo-dendritic synapses of the cerebral cortex: an electron microscope study. J Anat. 1959 Oct;93:420–433. [PMC free article] [PubMed] [Google Scholar]
  15. Gray E. G., Guillery R. W. Synaptic morphology in the normal and degenerating nervous system. Int Rev Cytol. 1966;19:111–182. doi: 10.1016/s0074-7696(08)60566-5. [DOI] [PubMed] [Google Scholar]
  16. Gysin R., Wirth M., Flanagan S. D. Structural heterogeneity and subcellular distribution of nicotinic synapse-associated proteins. J Biol Chem. 1981 Nov 25;256(22):11373–11376. [PubMed] [Google Scholar]
  17. Jones D. H., Matus A. I. Isolation of synaptic plasma membrane from brain by combined flotation-sedimentation density gradient centrifugation. Biochim Biophys Acta. 1974 Aug 9;356(3):276–287. doi: 10.1016/0005-2736(74)90268-5. [DOI] [PubMed] [Google Scholar]
  18. Kelly P. T., Cotman C. W. Intermolecular disulfide bonds at central nervous system synaptic junctions. Biochem Biophys Res Commun. 1976 Dec 20;73(4):858–864. doi: 10.1016/0006-291x(76)90200-x. [DOI] [PubMed] [Google Scholar]
  19. Kelly P. T., Cotman C. W. Synaptic proteins. Characterization of tubulin and actin and identification of a distinct postsynaptic density polypeptide. J Cell Biol. 1978 Oct;79(1):173–183. doi: 10.1083/jcb.79.1.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Kelly P. T., Montgomery P. R. Subcellular localization of the 52,000 molecular weight major postsynaptic density protein. Brain Res. 1982 Feb 11;233(2):265–286. doi: 10.1016/0006-8993(82)91202-1. [DOI] [PubMed] [Google Scholar]
  21. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  22. Matus A. I., Taff-Jones D. H. Morphology and molecular composition of isolated postsynaptic junctional structures. Proc R Soc Lond B Biol Sci. 1978 Dec 4;203(1151):135–151. doi: 10.1098/rspb.1978.0097. [DOI] [PubMed] [Google Scholar]
  23. Matus A. I., Walters B. B., Mughal S. Immunohistochemical demonstration of tubulin associated with microtubules and synaptic junctions in mammalian brain. J Neurocytol. 1975 Dec;4(6):733–744. doi: 10.1007/BF01181633. [DOI] [PubMed] [Google Scholar]
  24. Matus A. I., Walters B. B. Ultrastructure of the synaptic junctional lattice isolated from mammalian brain. J Neurocytol. 1975 Jun;4(3):369–375. doi: 10.1007/BF01102119. [DOI] [PubMed] [Google Scholar]
  25. Matus A., Pehling G., Ackermann M., Maeder J. Brain postsynaptic densities: the relationship to glial and neuronal filaments. J Cell Biol. 1980 Nov;87(2 Pt 1):346–359. doi: 10.1083/jcb.87.2.346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Mushynski W. E., Glen S., Thérien H. M. Actin-like and tubulin-like proteins in synaptic junctional complexes. Can J Biochem. 1978 Aug;56(8):820–830. doi: 10.1139/o78-125. [DOI] [PubMed] [Google Scholar]
  27. Nicolson G. L. Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over surface components. Biochim Biophys Acta. 1976 Apr 13;457(1):57–108. doi: 10.1016/0304-4157(76)90014-9. [DOI] [PubMed] [Google Scholar]
  28. Salvaterra P. M., Matthews D. A. Isolation of rat brain subcellular fraction enriched in putative neurotransmitter receptors and synaptic junctions. Neurochem Res. 1980 Feb;5(2):181–195. doi: 10.1007/BF00964331. [DOI] [PubMed] [Google Scholar]
  29. Sampedro M. N., Bussineau C. M., Cotman C. W. Postsynaptic density antigens: preparation and characterization of an antiserum against postsynaptic densities. J Cell Biol. 1981 Sep;90(3):675–686. doi: 10.1083/jcb.90.3.675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Stossel T. P. Contractile proteins in cell structure and function. Annu Rev Med. 1978;29:427–457. doi: 10.1146/annurev.me.29.020178.002235. [DOI] [PubMed] [Google Scholar]
  31. Uchizono K. Characteristics of excitatory and inhibitory synapses in the central nervous system of the cat. Nature. 1965 Aug 7;207(997):642–643. doi: 10.1038/207642a0. [DOI] [PubMed] [Google Scholar]
  32. Ueda T., Greengard P., Berzins K., Cohen R. S., Blomberg F., Grab D. J., Siekevitz P. Subcellular distribution in cerebral cortex of two proteins phosphorylated by a cAMP-dependent protein kinase. J Cell Biol. 1979 Nov;83(2 Pt 1):308–319. doi: 10.1083/jcb.83.2.308. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Walters B. B., Matus A. I. Tubulin in postynaptic junctional lattice. Nature. 1975 Oct 9;257(5526):496–498. doi: 10.1038/257496a0. [DOI] [PubMed] [Google Scholar]
  34. de Blas A., Mahler H. R. Studies on nicotinic acetylcholine receptors in mammalian brain. Characterization of a microsomal subfraction enriched in receptor function for different neurotransmitters. J Neurochem. 1978 Mar;30(3):563–577. doi: 10.1111/j.1471-4159.1978.tb07810.x. [DOI] [PubMed] [Google Scholar]

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