論文 - 鈴木　健史

Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome

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

HISTOCHEMISTRY AND CELL BIOLOGY ( SPRINGER )  126 ( 2 ) 251 - 259  2006年08月  [査読有り]

　概要を見る

In vertebrate cells, the centrosome consists of a pair of centrioles and surrounding pericentriolar material. Using anti-Golgi 58K protein antibodies that recognize formiminotransferase cyclodeaminase (FTCD), we investigated its localization to the centrosome in various cultured cells and human oviductal secretory cells by immunohistochemistry. In addition to the Golgi apparatus, FTCD was localized to the centrosome, more abundantly around the mother centriole. The centrosome localization of FTCD continued throughout the cell cycle and was not disrupted after Golgi fragmentation, which was induced by colcemid and brefeldin A. Centriole microtubules are polyglutamylated and stable against tubulin depolymerizing drugs. FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD.

DOI

Expression and immunolocalization of water-channel aquaporins in the rat and mouse mammary gland

T Matsuzaki, N Machida, Y Tajika, A Ablimit, T Suzuki, T Aoki, H Hagiwara, K Takata

HISTOCHEMISTRY AND CELL BIOLOGY ( SPRINGER )  123 ( 4-5 ) 501 - 512  2005年06月  [査読有り]

　概要を見る

We examined the expression and immunolocalization of water-channel aquaporins in the mammary gland by reverse transcriptase polymerase chain reaction (RT-PCR), immunoblotting, and immunohistochemistry. RT-PCR and immunoblotting revealed the expression of aquaporin-1 (AQP1) and AQP3 in the lactating rat mammary gland. AQP3 was detected in the alveolar epithelium and duct system whereas AQP1 was found in the capillaries and venules. AQP3 was present in the basolateral membrane of secretory epithelial cells and intralobular and interlobular duct epithelial cells. The main duct near the orifice in the nipple, which is comprised of a stratified epithelium, bore AQP3 in its basal and intermediate layers. AQP1 was located in both the apical and basolateral membranes of capillary and venule endothelia. AQP3 was not detected in virgin females. AQP3 was found in some differentiating mammary epithelial cells in the pregnant rat. AQP1 was present in capillaries and venules in the differentiating mammary gland of the pregnant rat and in the mammary fat pad of virgin females. We found a similar distribution of AQP1 and AQP3 in the mouse. AQP1 and AQP3 seem to play roles in the synthesis and/or secretion of milk.

DOI

Aquaporin water channels in the kidney

K Takata, T Matsuzaki, Y Tajika, A Ablimit, T Suzuki, T Aoki, H Hagiwara

ACTA HISTOCHEMICA ET CYTOCHEMICA ( JAPAN SOC HISTOCHEMISTRY & CYTOCHEMISTRY )  38 ( 3 ) 199 - 207  2005年  [査読有り]

　概要を見る

Aquaporins (AQPs) are water channel proteins of cellular membranes serving in the permeation of water across the membrane. AQP families are found virtually in all types of life ranging from bacteria to plant and animal cells. In mammals, at least 13 isoforms of AQPs have been identified. They are classified into three subtypes: classical aquaporins, aquaglyceroporins, and superaquaporins. These AQPs are differentially expressed in a wide variety of cells and tissues in the body, and play important roles in water metabolism. In the kidney, at least 6 isoforms of AQPs, namely AQP1, AQP2, AQP3, AQP4, AQP6, and AQP7, are reported to be expressed. Water transfer occurs mainly in the proximal tubules and collecting ducts in the kidney. In the proximal tubules, AQP1 and AQP7 are expressed, among which AQP1 plays a major role in water reabsorption. In the collecting ducts, AQP2, AQP3, AQP4, and AQP6 are expressed. AQP3 and AQP4 are localized at the basolateral membrane. AQP2 is stored in the cytoplasmic vesicles and is translocated to the apical plasma membrane in response to antidiuretic hormone. Mutations of AQP2 lead to either loss of channel function or mistrafficking and result in nephrogenic diabetes insipidus, the inability to concentrate urine.

DOI

Water channel aquaporin 1 (AQP1) is present in the perineurium and perichondrium

T Matsuzaki, A Ablimit, Y Tajika, T Suzuki, T Aoki, H Hagiwara, K Takata

ACTA HISTOCHEMICA ET CYTOCHEMICA ( JAPAN SOC HISTOCHEMISTRY & CYTOCHEMISTRY )  38 ( 1 ) 37 - 42  2005年  [査読有り]

　概要を見る

Aquaporin 1 (AQPI) is an isoform of membrane water channels. We examined the distribution of AQP1 in peripheral nerves. Immunofluorescence microscopy with specific antibodies to AQP1 was performed in the tissue sections of the rat tongue, esophagus, trachea, and sciatic nerve. AQP1 was present in the perineurium of nerve fiber bundles in the sciatic nerve and nerve fiber bundles in the tongue, esophagus, and trachea. Laser confocal microscopy of the double-labeled specimens for AQP1 and sugar transporter GLUT1 revealed that AQP1 was localized in the outer layer(s) of the perineurial cell layers, whereas GLUT1 was present throughout the entire perineurial cell layers. AQP1 and GLUT1 were also present in blood vessels inside the nerve fiber bundle. They were rarely found in the same blood vessels, namely, AQP1 was hardly detectable in GLUT1-positive blood vessels and GLUT1 was hardly detectable in AQP1-positive vessels. AQP1 in these sites of the blood-nerve barrier may participate in the water transfer across the barrier and contribute to the maintenance of the milieu of the nerve. In addition, we showed the presence of AQP1 in the perichondrium of the tracheal cartilage suggesting a possible role in water transfer between the cartilage and surrounding connective tissues.

DOI CiNii

Immunohistochemical characterization of the intracellular pool of water channel aquaporin-2 in the rat kidney.

Yuki Tajika, Toshiyuki Matsuzaki, Takeshi Suzuki, Takeo Aoki, Haruo Hagiwara, Shigeyasu Tanaka, Eiki Kominami, Kuniaki Takata

Anatomical science international   77 ( 3 ) 189 - 95  2002年09月  [国内誌]

　概要を見る

Aquaporin-2 (AQP2) is a member of water channel proteins expressed in the kidney collecting duct cells, where it is stored in the intracellular compartment. Upon stimulation of antidiuretic hormone (ADH), AQP2 is recruited to the plasma membrane, and plays a critical role in urine concentration. We immunohistochemically characterized the intracellular compartment harboring AQP2 in the rat kidney using antibodies to the endoplasmic reticulum, Golgi apparatus, trans-Golgi network, lysosome, and endosome. Aquaporin-2 did not colocalize with calnexin, TGN38, Golgi 58K, cathepsin D or Igp-110. Small portions of AQP2-bearing vesicles were positive for early endosome antigen 1. These localization patterns were basically the same in water-loaded and ADH-treated animals. These results indicate that AQP2-bearing vesicles constitute a unique intracellular compartment distinct from the endoplasmic reticulum, Golgi apparatus, trans-Golgi network and lysosome. Partial colocalization of AQP2 with early endosomes suggests that the endosomal system might be involved in the trafficking of AQP2.

PubMed

Aquaporins: a water channel family.

Matsuzaki T, Tajika Y, Tserentsoodol N, Suzuki T, Aoki T, Hagiwara H, Takata K

Anatomical science international ( 2 )  77 ( 2 ) 85 - 93  2002年06月  [査読有り]  [国内誌]

　概要を見る

Water channel proteins, aquaporins, are integral membrane proteins serving in the permeation of water and some other small molecules. Eleven isoforms of aquaporins have been identified from various tissues to date. They are expressed in tissue- and cell-specific manners, and are closely related to the specific functions of tissues and cells. Aquaporins are usually localized to the plasma membrane. Some isoforms are present in cytoplasmic compartments, and their translocation to the plasma membrane is crucial in the regulation of water transfer. This review focuses on the localization of aquaporins in mammalian tissues and discusses the physiological importance of water channels.

DOI PubMed

Plastid Gene Expression during Amyloplast Formation in Cultured Tobacco Cells

Atsushi Sakai, Yutaka Miyazawa, Takeshi Suzuki, Narie Sasaki, Shigeyuki Kawano, Tsuneyoshi Kuroiwa

Journal of Plant Physiology ( Elsevier BV )  154 ( 1 ) 71 - 78  1999年01月  [査読有り]

DOI

Nucleotide sequence of the cytochrome oxidase subunit I gene from rice mitochondria.

K Kadowaki, T Suzuki, S Kazama, T Oh-fuchi, W Sakamoto

Nucleic Acids Res   17   1759  1989年  [査読有り]

DOI