1994;107:353C366

1994;107:353C366. and in synaptic boutons, as illustrated in the cerebellar cortex. The distribution of MCP in the rat CNS and its subcellular localization are discussed in relation to (1) the distribution of calpain, the other major nonlysosomal cellular protease, and (2) the possible role of MCP in the degradation of regulatory proteins and important transcription factors that are essential in many neuronal responses. marks the white matter; the point to the pial surface.point to the pyramidal layer of the piriform cortex. in CA1 is usually shown at a higher magnification inEFpoint to MCP-IR in the initial segments of apical dendrites; A 967079 the mark an apical dendrite traversing the cortical field.and are shown in point to immunoreactive structures outlining the Purkinje cell somata, and below them, another row of Purkinje cells appears out of focus. The molecular layer displays a moderate MCP-IR in which scattered MCP-positive cell nuclei are prominent. The granule cell layer is usually faintly immunoreactive, whereas intensely immunoreactive cells, likely Golgi cells, are scattered in this layer. points to a cluster of reaction product between two cisternae of endoplasmic reticulum. Level bars:by an axon from your cerebral cortex. Open in a separate windows Fig. 7. Electron micrographs showing MCP-IR within neuronal processes. Bshows a nonimmunoreactive preterminal nerve fiber closely related to immunoreactive dendritic processes. mark the points of synaptic contact. mark the points of synaptic contact.and neurons (Chain et al., 1995), and ubiquitin-dependent degradation of the regulatory subunit of the cAMP-dependent protein kinase was correlated with long-term presynaptic facilitation in this system (Hegde et al., 1993). Those results, together with the results offered in this study, and the fact that we also found MCP by immunoblot analysis in synaptosomal preparations from rat brain strongly support the hypothesis that this proteasome may participate in the mechanism of maintenance of LTP. In a similar A 967079 context, it has been explained recently in at 3.4?A resolution [see feedback]. Science. 1995;268:533C539. [PubMed] [Google Scholar] 26. Machiels BM, Henfling ME, Broers JL, Hendil KB, Ramekers FC. Changes in immunocytochemical detectability of proteasome epitopes depending on cell growth and fixation conditions of lung A 967079 malignancy cell lines. Eur J Cell Biol. 1995;66:282C292. [PubMed] [Google Scholar] 27. Masaki T, Ishiura S, Sugita H, Kwak S. PTPRQ Multicatalytic proteinase is usually associated with characteristic oval structures in cortical Lewy body: an immunocytochemical study with light and electron microscopy. J Neurol Sci. 1994;122:127C134. [PubMed] [Google Scholar] 28. Olink-Coux M, Arcangeletti C, Pinardi F, Minisini R, Huesca M, Chezzi C, Scherrer K. Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type. J Cell Sci. 1994;107:353C366. [PubMed] [Google Scholar] 29. Orlowski M. The multicatalytic proteinase complex, a major extralysosomal proteolytic system. Biochemistry. 1990;29:10289C10297. [PubMed] [Google A 967079 Scholar] 30. Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NFkappa B1 precursor protein and the activation of NF-kappa B. Cell. 1994;78:773C785. [PubMed] [Google Scholar] 31. Paxinos G, Watson C. Academic; New York: 1986. The rat brain in stereotaxic coordinates. . [Google Scholar] 32. Perlmutter LS, Gall C, Baudry M, Lynch G. Distribution of calcium-activated protease calpain in the rat brain. J Comp Neurol. 1990;296:269C276. [PubMed] [Google Scholar] 33. Rivett JA. Proteasomes: multicatalytic proteinase complexes. Biochem J. 1993;291:1C10. [PMC free article] [PubMed] [Google Scholar] 34. Rivett JA, Knecht E. Proteasome location. Curr Biol. 1993;3:127C129. [PubMed] [Google Scholar] 35. Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides offered on MHC class I molecules. Cell. 1994;78:761C771. [PubMed] [Google Scholar] 36. Scheffner M, Werness BA, Huibregtse JM, Levine AJ, Howley PM. The E6 oncoprotein encoded by human papillomavirus types 16?and 18?promotes the degradation of p53. Cell. 1990;63:1129C1136. [PubMed] [Google Scholar] 37. Tamura T, Nagy I, Lupas A, Lottspeich F, Schoofs G, Tanaka K, De Mot R, Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of is usually mediated.