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  1. Article: Distinct sets of olfactory receptors highly expressed in different human tissues evaluated by meta-transcriptome analysis: Association of OR10A6 in skin with keratinization.

    Nakanishi, Shinobu / Tsutsui, Taiki / Itai, Nao / Denda, Mitsuhiro

    Frontiers in cell and developmental biology

    2023  Volume 11, Page(s) 1102585

    Abstract: Olfactory receptors (ORs) are expressed in many tissues and have multiple functions. However, most studies have focused on individual ORs. Here, we aimed to conduct a comprehensive meta-transcriptome analysis of OR gene expression in human tissues by ... ...

    Abstract Olfactory receptors (ORs) are expressed in many tissues and have multiple functions. However, most studies have focused on individual ORs. Here, we aimed to conduct a comprehensive meta-transcriptome analysis of OR gene expression in human tissues by using open-source tools to search a large, publicly available genotype-tissue expression (GTEx) data set. Analysis of RNA-seq data from GTEx revealed that OR expression patterns were tissue-dependent, and we identified distinct sets of ORs that were highly expressed in 12 tissues, involving 97 ORs in total. Among them,
    Language English
    Publishing date 2023-01-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2023.1102585
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Lymphangiogenesis and Lymphatic Zippering in Skin Associated with the Progression of Lymphedema.

    Itai, Nao / Gantumur, Enkhtuul / Tsujita-Inoue, Kyoko / Mitsukawa, Nobuyuki / Akita, Shinsuke / Kajiya, Kentaro

    The Journal of investigative dermatology

    2023  Volume 144, Issue 3, Page(s) 659–668.e7

    Abstract: Secondary lymphedema often develops after lymph node dissection or radiation therapy for cancer treatment, resulting in marked skin fibrosis and increased stiffness owing to insufficiency of the lymphatic system caused by abnormal structure and ... ...

    Abstract Secondary lymphedema often develops after lymph node dissection or radiation therapy for cancer treatment, resulting in marked skin fibrosis and increased stiffness owing to insufficiency of the lymphatic system caused by abnormal structure and compromised function. However, little is known about the associated changes of the dermal lymphatic vessels. In this study, using the lower limb skin samples of patients with secondary lymphedema, classified as types 1-4 by lymphoscintigraphy, we first confirmed the presence of epidermal thickening and collagen accumulation in the dermis, closely associated with the progression of lymphedema. Three-dimensional characterization of lymphatic capillaries in skin revealed prominent lymphangiogenesis in types 1 and 2 lymphedema. In contrast, increased recruitment of smooth muscle cells accompanied by development of the basement membrane in lymphatic capillaries was observed in types 3 and 4 lymphedema. Remarkably, the junctions of dermal lymphatic capillaries were dramatically remodeled from a discontinuous button-like structure to a continuous zipper-like structure. This finding is consistent with previous findings in an infection-induced mouse model. Such junction tightening (zippering) could reduce fluid transport and cutaneous viral sequestration during the progression of lymphedema and might explain the aggravation of secondary lymphedema. These findings may be helpful in developing stage-dependent treatment of patients with lymphedema.
    MeSH term(s) Mice ; Animals ; Humans ; Lymphangiogenesis ; Lymphatic Vessels ; Lymphedema/etiology ; Lymph Node Excision/adverse effects ; Lower Extremity/pathology ; Fibrosis
    Language English
    Publishing date 2023-09-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80136-7
    ISSN 1523-1747 ; 0022-202X
    ISSN (online) 1523-1747
    ISSN 0022-202X
    DOI 10.1016/j.jid.2023.08.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Jaw1/LRMP has a role in maintaining nuclear shape via interaction with SUN proteins.

    Kozono, Takuma / Tadahira, Kazuko / Okumura, Wataru / Itai, Nao / Tamura-Nakano, Miwa / Dohi, Taeko / Tonozuka, Takashi / Nishikawa, Atsushi

    Journal of biochemistry

    2018  Volume 164, Issue 4, Page(s) 303–311

    Abstract: Jaw1/LRMP is characterized as a Type II integral membrane protein that is localized to endoplasmic reticulum, however, its physiological functions have been poorly understood. An alignment of amino acid sequence of Jaw1 with Klarsicht/ANC-1/Syne/homology ...

    Abstract Jaw1/LRMP is characterized as a Type II integral membrane protein that is localized to endoplasmic reticulum, however, its physiological functions have been poorly understood. An alignment of amino acid sequence of Jaw1 with Klarsicht/ANC-1/Syne/homology (KASH) proteins, outer nuclear membrane proteins, revealed that Jaw1 has a partial homology to the KASH domain. Here, we show that the function of Jaw1 is to maintain nuclear shape in mouse melanoma cell line. The siRNA-mediated knockdown of Jaw1 caused a severe defect in nuclear shape, and the defect was rescued by ectopic expression of siRNA-resistant Jaw1. Since co-immunoprecipitation assay indicates that Jaw1 interacts with Sad-1/UNC-84 (SUN) proteins that are inner nuclear proteins and microtubules, this study suggests that Jaw1 has a role in maintaining nuclear shape via interactions with SUN proteins and microtubules.
    MeSH term(s) Animals ; Blotting, Western ; Cell Nucleus/metabolism ; Cell Shape ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mice ; Microscopy, Electron, Transmission
    Chemical Substances IRAG2 protein, human ; Membrane Proteins
    Language English
    Publishing date 2018-05-31
    Publishing country England
    Document type Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvy053
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.202: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: The phosphorylation of sorting nexin 5 at serine 226 regulates retrograde transport and macropinocytosis.

    Itai, Nao / Shimazu, Tsukasa / Kimura, Takayuki / Ibe, Issei / Yamashita, Ryo / Kaburagi, Yasushi / Dohi, Taeko / Tonozuka, Takashi / Takao, Toshifumi / Nishikawa, Atsushi

    PloS one

    2018  Volume 13, Issue 11, Page(s) e0207205

    Abstract: Sorting nexin 5 (SNX5), a member of sorting nexin family, plays an important role in membrane trafficking, including the retrograde trafficking of the cation independent mannose 6-phosphate receptor (CI-M6PR) and macropinocytosis. Using ESI-LCMS/MS ... ...

    Abstract Sorting nexin 5 (SNX5), a member of sorting nexin family, plays an important role in membrane trafficking, including the retrograde trafficking of the cation independent mannose 6-phosphate receptor (CI-M6PR) and macropinocytosis. Using ESI-LCMS/MS analysis, we confirmed that SNX5 serine 226 is phosphorylated. Since SNX5 forms heterodimers with SNX1 or SNX2, we examined the effect of phosphorylation at S226 on the heterodimer formations. Wild-type and mutants of SNX5, in which S226 was mutated to a glutamic acid or an alanine, were expressed in 8505C cells. In pull-down assays using SNX5 as bait, only the S226E mutant failed to precipitate both SNX1 and SNX2. Confocal microscopy data indicated that the wild type and S226A mutant were colocalized with SNX1 and SNX2 in endosomes, but the S226E was not. SNX5 and SNX6 support each other's functions and are involved with CI-M6PR retrograde trafficking. In SNX5 and SNX6 double knockdown cells, CI-M6PR was dispersed and colocalized with the endosomal marker EEA1. In a rescue experiment using SNX5 mutants, the S226A rescued CI-M6PR localization, similar to control cells, but S226E did not. Furthermore, the decrease in the uptake of dextran by macropinocytosis in SNX5 knockdown cells was recovered by the expression of rescue-wild type or S226A mutant, but not by the rescue-S226E mutant. These observations indicate that SNX5 constitutive phosphorylation that mimics the mutant S226E decreases the active SNX5 in these cells. The phosphorylation of SNX5 regulates the dimerization with SNX1 or SNX2, and this suggests that it controls membrane trafficking and protein sorting.
    MeSH term(s) Amino Acid Sequence ; Biological Transport/physiology ; Cell Line, Tumor ; Dextrans/metabolism ; Endosomes/metabolism ; Humans ; Mutation ; Phosphorylation ; Pinocytosis/physiology ; Protein Multimerization ; Receptor, IGF Type 2/metabolism ; Sorting Nexins/genetics ; Sorting Nexins/metabolism
    Chemical Substances Dextrans ; Receptor, IGF Type 2 ; SNX1 protein, human ; SNX2 protein, human ; SNX5 protein, human ; SNX6 protein, human ; Sorting Nexins ; cation-dependent mannose-6-phosphate receptor
    Language English
    Publishing date 2018-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0207205
    Database MEDical Literature Analysis and Retrieval System OnLINE

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