Stacks of Flattened Smooth Endoplasmic Reticulum Highly Enriched in Inositol 1,4,5-Trisphosphate(InsP3)Receptor in Mouse Cerebellar Purkinje Cells.

Yamamoto, Akira; Otsu, Hiroko; Yoshimori, Tamotsu; Maeda, Nobuaki; Mikoshiba, Katsuhiko; Tashiro, Yutaka

doi:10.1247/csf.16.419

Cited by 39 publications

(24 citation statements)

References 36 publications

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“…Mammalian Purkinje cells show a high level of IP 3 binding activity (Worley et al, 1989) and express a high density of IP 3 R protein associated with the ER (Mignery et al, 1989;Otsu et al, 1990;Nakanishi et al, 1991;Yamamoto et al, 1991;Furuichi et al, 1993;Suburo et al, 1993;Sharp et al, 1993;Miyata et al, 1999). Typically, Purkinje cells of the cerebellum show the highest label intensity for IP 3 R throughout the central nervous system and express the IP 3 R protein intracellularly in all compartments (axon, soma, dendrites) with the exception Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Studies that used mammalian cerebella clearly showed the presence of all major components of IP 3 -mediated Ca release using a variety of different techniques (Nakanishi et al, 1991;Watras et al, 1991;Eilers et al, 1996;Finch and Augustine, 1998). Indeed, the IP 3 R is expressed at very high levels on the ER of mammalian cerebellar Purkinje neurons (Otsu et al, 1990;Yamamoto et al, 1991;Yamada et al, 1992). The present study had three aims: 1) to characterize further the distribution of IP 3 R type 1 (IP 3 R1) in mammalian cerebella by determining its localization in hamster and comparing it to that of two other rodent species, rat and mouse; 2) to localize the IP 3 R1 in cerebella of zebrafish Danio rerio, claw frog Xenopus laevis and skate Raja erinacea, vertebrate species that are important model animals in neurogenetics or neurophysiology; and 3) to compare the cerebellar localization pattern of IP 3 R1 immunoreactivity in different vertebrate phyla.…”

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confidence: 99%

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Conservation of localization patterns of IP3 receptor type 1 in cerebellar Purkinje cells across vertebrate species

et al. 2000

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The distribution of inositol 1,4,5‐trisphosphate (IP3) receptor type 1 (IP3R1) protein was studied in the adult cerebella of six different vertebrate species, zebrafish, skate, claw frog, rat, hamster, and mouse. The receptor was found at high expression levels in Purkinje cells in all species examined using a subtype‐specific polyclonal antiserum against IP3R1 and fluorescence immunocytochemistry. The immunoreactivity for IP3R1 was found intracellularly at high concentrations in dendrites and somata and at lower levels in axons of these cells. Despite the morphological and functional differences of the cerebella the staining patterns of IP3R1 labeling in Purkinje cells was preserved. This is notable because the cerebella were taken from organisms representing a large segment of vertebrate phylogenetic development. The high expression levels of IP3R1 in Purkinje cells were found independent of the degree of the formation of fissures and folia and of the degree of branching of Purkinje cell dendrites. The conservation of cerebellar structures not only at the cellular level but more importantly at the molecular level suggests that identical intracellular calcium signaling mechanisms are used in a number of species that represent different areas of phylogenetic development and specialization. J. Neurosci. Res. 61:493–499, 2000. © 2000 Wiley‐Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Conservation of localization patterns of IP3 receptor type 1 in cerebellar Purkinje cells across vertebrate species

et al. 2000

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“…Immunoelectron Microscopy-Cryo-ultramicrotomy and immunogold staining were followed as described previously (14) with a slight modification. Briefly, cells were fixed in 4% paraformaldehyde and 0.2% glutaraldehyde in 0.1 M sodium phosphate buffer, pH 7.4, for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Subcellular Localization and Physiological Significance of Intracellular Mannan-binding Protein

Nonaka

Yong

Ohtani

et al. 2007

Journal of Biological Chemistry

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Mannan-binding protein (MBP) is a C-type mammalian lectin specific for mannose and N-acetylglucosamine. MBP is mainly synthesized in the liver and occurs naturally in two forms, serum MBP (S-MBP) and intracellular MBP (I-MBP). S-MBP activates Mannan-binding protein (MBP),4 also known as mannanbinding lectin, is a Ca 2ϩ -dependent (C-type) mammalian lectin exhibiting primary specificity for mannose, fucose, and N-acetylglucosamine (1). Because its discovery as a vital serum component associated with innate immunity, this lectin has been regarded as a multifunctional protein. MBP occurs naturally in two forms, secretory serum MBP (S-MBP) and intracellular MBP, which is termed I-MBP in this study and was called liver MBP (L-MBP) in our previous studies (2-4). Human S-MBP and I-MBP are mainly synthesized in the liver and translated from a single form of mRNA. Both S-MBP and I-MBP are homooligomers composed of 32-kDa subunits. Each subunit has an NH 2 -terminal region containing cysteines involved in interchain disulfide bond formation, a collagen-like domain containing hydroxyproline and hydroxylysine residues, and a carbohydrate-recognition domain (CRD) with an amino acid sequence highly homologous to those of other C-type lectins (5). The CRD is specific for high-mannose oligosaccharide structures on exogenous and endogenous ligands, whereas the collagen-like domain is believed to be responsible for interactions with other effector proteins involved in host defense. S-MBP activates complement through interaction with three novel MBP-associated serine proteases, which is called the lectin pathway (6). Furthermore, S-MBP was shown to exhibit novel cytotoxic activity toward some in vivo colorectal carcinoma cell experiments, which we proposed to term MBP-dependent cell-mediated cytotoxicity (4, 7). However, little is known about the subcellular localization and physiological significance of I-MBP. Recently, the functions of glycoprotein glycan chains in protein quality control have been attracting more attention, highmannose-type oligosaccharides especially having been shown to play important roles in this process (8,9). Glycosylation with an asparagine-linked (N-linked) oligosaccharides is a co-translational process that occurs in the ER. High-mannose-type oligosaccharides, presumably representing nascent core-glycosylated proteins, are subsequently transferred to the Golgi

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“…For immunoelectron microscopy, the post-embedding immunogold method was used to label cultured cells embedded in LR white resin (London Resin Co.) as previously described (Yamamoto et al, 1991).…”

Section: Electron Microscopymentioning

confidence: 99%

GFP-like Proteins Stably Accumulate in Lysosomes

Katayama

Yamamoto

Mizushima³

et al. 2008

Cell Struct. Funct.

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219

189

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ABSTRACT. Green fluorescent protein (GFP) from the jellyfish Aequorea victoria, its GFP variants (Aequorea GFPs), and more recently the novel GFP-like proteins from Anthozoa have greatly advanced our technologies for fluorescently labeling cells, organelles, and proteins. It has been shown, however, that some GFP-like proteins have a tendency to oligomerize and aggregate. Transfection of GFP-like proteins into cultured mammalian cells results in bright punctate structures, which are thought to be cytosolic protein aggregates. In this study, we demonstrate that these structures are not cytosolic aggregates but lysosomes that have accumulated the GFP-like proteins. Our biochemical and immunocytochemical experiments have revealed that certain GFP-like proteins expressed in the cytosol enter lysosomes possibly by an autophagy-related mechanism, but retain their fluorescence because of resistance not only to acidity but also to lysosomal proteases.

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Stacks of Flattened Smooth Endoplasmic Reticulum Highly Enriched in Inositol 1,4,5-Trisphosphate(InsP3)Receptor in Mouse Cerebellar Purkinje Cells.

Cited by 39 publications

References 36 publications

Conservation of localization patterns of IP3 receptor type 1 in cerebellar Purkinje cells across vertebrate species

Conservation of localization patterns of IP3 receptor type 1 in cerebellar Purkinje cells across vertebrate species

Subcellular Localization and Physiological Significance of Intracellular Mannan-binding Protein

GFP-like Proteins Stably Accumulate in Lysosomes

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