研究者詳細 - 鈴木　健史

Misc - 鈴木　健史

分割表示 153 件中 1 - 20 件目／全件表示 >>

線維芽細胞における一次線毛伸長について

萩原治夫, 中倉敬, 浅野安信, 有澤謙二郎, 田中秀幸, 鈴木健史

日本臨床分子形態学会総会・学術集会講演プログラム・要旨集 45th 98 2013年

J-GLOBAL

Double-label immunoelectron microscopy for studying the colocalization of proteins in cultured cells

Hagiwara H, Aoki T, Suzuki T, Takata K

Methods in Molecular Biology 657 249 - 57 2010年

DOI

Pre-embedding immunoelectron microscopy of chemically fixed mammalian tissue culture cells

Hagiwara H, Aoki T, Suzuki T, Takata K

Methods in Molecular Biology 657 145 - 54 2010年

DOI

頂部膜剥離法によって作製した試料によるAQP2動態の観察

青木武生, 萩原治夫, 鈴木健史, 松崎利行, 高田邦昭

解剖学雑誌 85 ( Supplement ) 2010年

J-GLOBAL

Roles of gap junctions in glucose transport from glucose transporter 1-positive to -negative cells in the lateral wall of the rat cochlea

Toshihiro Suzuki, Tatsuya Matsunami, Yasuo Hisa, Kuniaki Takata, Tetsuro Takamatsu, Masahito Oyamada

HISTOCHEMISTRY AND CELL BIOLOGY ( SPRINGER ) 131 ( 1 ) 89 - 102 2009年01月

Despite the importance of glucose metabolism for auditory function, the mechanisms of glucose transport in the cochlea are not completely understood. We hypothesized that gap junctions mediate intercellular glucose transport in the cochlea in cooperation with facilitative glucose transporter 1 (GLUT1). Immunohistochemistry showed that GLUT1 and the tight junction protein occludin were expressed in blood vessels, and GLUT1, the gap junction proteins connexin26 and connexin30, and occludin were also present in strial basal cells in the lateral wall of the rat cochlea. Gap junctions were found among not only these GLUT1-positive strial basal cells but also GLUT1-negative fibrocytes in the spiral ligaments and strial intermediate cells. Glucose imaging using 6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino]-6-deoxyglucose (6-NBDG, MW 342) together with Evans Blue Albumin (EBA, MW 68,000) showed that 6-NBDG was rapidly distributed throughout the stria vascularis and spiral ligament, whereas EBA was localized only in the vessels. The gap junctional uncouplers heptanol and carbenoxolone inhibited the distribution of 6-NBDG in the spiral ligament without decreasing the fluorescence of EBA in the blood vessels. These findings suggest that gap junctions mediate glucose transport from GLUT1-positive cells (strial basal cells) to GLUT1-negative cells (fibrocytes in the spiral ligament and strial intermediate cells) in the cochlea.

DOI

PI-28 MDCK細胞における頂部細胞膜カベオラと水チャネルアクアポリン2との関係(免疫組織化学,ポスター1,第50回日本組織細胞化学会総会・学術集会)

青木武生, 萩原治夫, 鈴木健史, 高田邦昭

日本組織細胞化学会総会プログラムおよび抄録集 ( 日本組織細胞化学会 ) ( 50 ) 76 - 76 2009年

CiNii

蛍光タンパク質の基礎と実際(E.顕微鏡観察技術の新しい展開)

鈴木健史, 高田邦昭

組織細胞化学 ( 日本組織細胞化学会 ) 2008 101 - 109 2008年07月

CiNii

Internalization of caveolae and their relationship with endosomes in cultured human and mouse endothelial cells

Takeo Aoki, Haruo Hagiwara, Toshiyuki Matsuzaki, Takeshi Suzuki, Kuniaki Takata

ANATOMICAL SCIENCE INTERNATIONAL ( BLACKWELL PUBLISHING ) 82 ( 2 ) 82 - 97 2007年06月

Treatment of cells with pervanadate or vanadate induces the phosphorylation of caveolin-1 and its internalization from the cell surface, but the intracellular fate of caveolae has not been fully elucidated. In the present study, we examined the fate of endocytosed caveolae in human umbilical vein endothelial cells and mouse endothelial KOP2.16 cells. The localization of internalized caveolae and their relationship with the endosomes were examined by immunofluorescence microscopy as well as by immunoprecipitation and chasing of biotinylated transferrin. In untreated cells, caveolin-1 was mostly confined to the cell surface. When cells were treated with either pervanadate for 30 min or vanadate for 3 h, many caveolin-1-labeled vesicles were formed inside the cells, some of which were colocalized with Rab5 or Rab4. The internalized caveolin-1 was colocalized with the endocytosed transferrin in the Rab5-, Rab4- or early endosome antigen-1-labeled compartment where caveolin-1 was phosphorylated. It then moved to the Rab11-associated compartment. Immunogold electron microscopy revealed that internalized caveolin-1 colocalized with Rab5 or Rab4 in vesicles larger than caveolae. These results suggest that the internalized caveolae interact with early endosomes.

DOI

水チャネル・アクアポリン2のエンドサイトーシスはクラスリン関連経路と関係あるのか?

青木武生, 鈴木健史, 萩原治夫, 長谷川敬展, 高田邦昭

解剖学雑誌 82 ( Supplement ) 135 2007年03月

J-GLOBAL

S2-02 免疫シナプス超分子クラスターの分子機能動態(バイオイメージングで生体機能を観る、測る,シンポジウム2,第48回日本組織細胞化学会総会(第8回日中合同組織細胞化学セミナー) 第39回日本臨床分子形態学会総会合同学術集会)

鈴木健史, 高田邦昭, Kupfer Abraham

日本組織細胞化学会総会プログラムおよび抄録集 ( 日本組織細胞化学会 ) ( 48 ) 52 - 52 2007年

CiNii

Changes of aquaporin 5-distribution during release and reaccumulation of secretory granules in isoproterenol-treated mouse parotid gland

Toshiyuki Matsuzaki, Abduxukur Ablimit, Takeshi Suzuki, Takeo Aoki, Haruo Hagiwara, Kuniaki Takata

JOURNAL OF ELECTRON MICROSCOPY ( OXFORD UNIV PRESS ) 55 ( 3 ) 183 - 189 2006年06月

Water channel aquaporin 5 (AQP5) is present in the apical membrane of the salivary gland acinar cells. We examined changes of AQP5-distribution during the fusion process of secretory granule membranes into the apical membrane and subsequent recovery process in the mouse parotid gland by administering isoproterenol (IPR) in vivo. We performed immunoperoxidase, immunofluorescence and immunoelectron microscopy. In the basal state, AQP5 was localized mainly in the apical membrane of the acinar cell. It was also present in the basolateral membrane to a lesser extent. When IPR was administered to mice, dot-like, vesicle-like and vacuole-like labeling for AQP5 was seen in the subapical regions by light microscopy. By immunoelectron microscopy, AQP5 was localized at both the apical and basolateral plasma membranes in the basal state. At 5 and 30 min after the IPR-administration, acinar lumen became enlarged and small invaginations formed by fusion of secretory granules were seen. AQP5 was positive along the apical plasma membrane and its small invaginations. At 60 min, large invaginations of the lumen were formed. AQP5 remained positive in the membrane of these large invaginations. At 6 h, large invaginations disappeared and AQP5 was localized in the apical plasma membrane. AQP5 was restricted to plasma membranes and continuous invaginations formed by the exocytosis of secretory granules. AQP5 was not detected in the cytoplasm. These observations show that AQP5 does not seem to be endocytosed during the membrane recycling process following the exocytosis.

DOI PubMed CiNii

Gap junctions mediate glucose transport between GLUT1-positive and -negative cells in the spiral limbus of the rat cochlea

T Matsunami, T Suzuki, Y Hisa, K Takata, T Takamatsu, M Oyamada

CELL COMMUNICATION AND ADHESION ( TAYLOR & FRANCIS INC ) 13 ( 1-2 ) 93 - 102 2006年01月

To elucidate the role of the spiral limbus in glucose transport in the cochlea, we analyzed the expression and localization of GLUT1, connexin26, connexin30, and occludin in the spiral limbus of the rat cochlea. GLUT1 and occludin were detected in blood vessels. GLUT1, connexin26, connexin30, and occludin were also expressed in fibrocytes just basal to the supralimbal lining cells. Connexin26 and connexin30 were present among not only these GLUT1-positive fibrocytes but also GLUT1-negative fibrocytes. In vivo glucose imaging using 6-[N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl) amino]-6-deoxyglucose ( 6- NBDG, MW 342) together with Evans Blue Albumin (EBA, MW 68,000) showed that 6- NBDG was rapidly distributed throughout the spiral limbus, whereas EBA was localized only in the vessels. Moreover, the gap junctional uncoupler heptanol inhibited the distribution of 6- NBDG. These findings suggest that gap junctions play an important role in glucose transport in the spiral limbus, i.e., that gap junctions mediate glucose transport from GLUT1-positive fibrocytes to GLUT1-negative fibrocytes in the spiral limbus.

DOI

Apical localization of sodium-dependent glucose transporter SGLT1 is maintained by cholesterol and microtubules

Takeshi Suzuki, Toshiyuki Matsuzaki, Haruo Hagiwara, Takeo Aoki, Yukiko Tajika-Takahashi, Kuniaki Takata

ACTA HISTOCHEMICA ET CYTOCHEMICA ( JAPAN SOC HISTOCHEMISTRY & CYTOCHEMISTRY ) 39 ( 6 ) 155 - 161 2006年

A GFP-labeled sodium-dependent glucose transporter SGLT1 (SGLT-GFP) was transfected into MDCK cells. SGLT-GFP was localized at the apical membrane in confluent cells. When cellular cholesterol was depleted by methyl-beta-cyclodextrin (M beta CD) treatment, the localization of SGLT-GFP gradually switched from apical to whole plasma membrane. Time-lapse microscopy revealed that the effect of M beta CD appeared within 30 min, and that the transition of SGLT-GFP to the whole plasma membrane was completed within 2 hr after the administration. Immunofluorescence microscopy revealed that the tight junction framework remained steady during this process. The effect of M beta CD on SGLT-GFP localization was counterbalanced by the addition of cholesterol into the culture medium. Disruption of microtubules by colcemid also perturbed SGLT-GFP localization. SGLT-GFP localized to the whole plasma membrane by colcemid treatment, and apical localization was restored within 1 hr after removal of colcemid. Inhibition of protein synthesis by cycloheximide had no effect on the transition of SGLT-GFP induced by the M beta CD or colcemid. These results indicated that the apical localization of SGLT-GFP is maintained by cellular cholesterol and microtubules, possibly with an apical recycling machinery.

DOI

デコンボリューション顕微鏡法．

鈴木健史, 高田邦昭

顕微鏡 ( The Japanese Society of Microscopy ) 41 ( 2 ) 120 - 123 2006年 [査読有り]

記事・総説・解説・論説等（その他）

DOI CiNii

アクアポリン2水チャネルの細胞内貯蔵部位と細胞内動態

高田邦昭, 多鹿友喜, 松崎利行, 鈴木健史, 青木武生, 萩原治夫

解剖学雑誌 81 ( Supplement ) 2006年

J-GLOBAL

Differential regulation of AQP2 trafficking in endosomes by microtubules and actin filaments

Y Tajika, T Matsuzaki, T Suzuki, A Ablimit, T Aoki, H Hagiwara, M Kuwahara, S Sasaki, K Takata

HISTOCHEMISTRY AND CELL BIOLOGY ( SPRINGER ) 124 ( 1 ) 1 - 12 2005年07月

Vasopressin-induced trafficking of aquaporin-2 (AQP2) water channels in kidney collecting duct cells is critical to regulate the urine concentration. To better understand the mechanism of subcellular trafficking of AQP2, we examined MDCK cells expressing AQP2 as a model. We first performed double-immunolabeling of AQP2 with endosomal marker proteins, and showed that AQP2 is stored at a Rab11-positive subapical compartment. After the translocation to the plasma membrane, AQP2 was endocytosed to EEA1-positive early endosomes, and then transferred back to the original Rab11-positive compartment. When Rab11 was depleted by RNA interference, retention of AQP2 at the subapical storage compartment was impaired. We next examined the role of cytoskeleton in the AQP2 trafficking and localization. By the treatment with microtubule-disrupting agent such as nocodazole or colcemid, the distribution of AQP2 storage compartment was altered. The disruption of actin filaments with cytochalasin D or latrunculin B induced the accumulation of AQP2 in EEA1-positive early endosomes. Altogether, our data suggest that Rab11 and microtubules maintain the proper distribution of the subapical AQP2 storage compartment, and actin filaments regulate the trafficking of AQP2 from early endosomes to the storage compartment.

DOI

IB-25 Aquaporins in the rat nasal mucosa :

Ablimit Abduxukur, Matsuzaki Toshiyuki, Suzuki Takeshi, Aoki Takeo, Hagiwara Haruo, Takata Kuniaki

日本組織細胞化学会総会プログラムおよび抄録集 ( 日本組織細胞化学会 ) ( 46 ) 77 - 77 2005年

CiNii

共焦点顕微鏡活用法．

鈴木健史, 松崎利行, 高田邦昭

Surgery Frontier 12(4),pp 82-85 2005年

授乳期ラット乳腺におけるアクアポリン水チャネルの分布局在

松崎利行, 多鹿友喜, ABLIMIT Abdushukur, 鈴木健史, 青木武生, 萩原治夫, 高田邦昭

解剖学雑誌 80 ( 1 ) 2005年

J-GLOBAL