Kyushu University Academic Staff Educational and Research Activities Database
List of Papers
Takane Kaneko Last modified date:2021.10.26

Assistant Professor / Agricultural Bioresource Sciences / Department of Bioresource Sciences / Faculty of Agriculture

1. Ogata, H., Tsukamoto, M., Yamashita, K., Iwamori, T., Takahashi, H., Kaneko, T., Iwamori, N., Inai, T. and Iida, H., Effects of Calyculin A on the Motility and Protein Phosphorylation in Frozen-thawed Bull Spermatozoa. , Zoological Science, doi:10.2108/zs210046, 38, 2021.12, In this study, we examined the effects of calyculin A, a phosphatase inhibitor, on motility, protein phosphorylation, and the distribution of phospho-(Ser/Thr) PKA substrates in frozen-thawed bull spermatozoa that are actually used by most farmers for breeding. The data showed that calyculin A, which has been reported to have a positive effect on the motility of ejaculated fresh spermatozoa, distinctly decreased the motility of frozen-thawed bull spermatozoa even if a cell activator, such as caffeine, was present in the incubation medium and that the suppressive effect of calyculin A was dose-dependent and continued for at least 200 min. Immunoblot analyses revealed that de novo protein phosphorylation was not detected in spermatozoa exposed to caffeine or dbcAMP (a cell-permeable cAMP analog), while the addition of calyculin A to the medium brought about the appearance of several phosphorylated proteins at 50 kDa and 75 kDa, suggesting that 50 kDa and 75 kDa proteins, which were phosphorylated by activation of cAMP-dependent PKA, were not dephosphorylated and were accumulated in spermatozoa due to the suppression of calyculin A-sensitive protein phosphatases. Immunofluorescence microscopy revealed that calyculin A caused, alone or in conjunction with caffeine or dbcAMP, the accumulation of phospho-PKA substrates at the annulus, although caffeine or dbcAMP alone did not. This study suggested that calyculin A decreases the motility of frozen-thawed bull spermatozoa concomitant with the accumulation of phospho-(Ser/Thr) PKA substrates at the annulus of flagella..
2. Wang, Y., Iwamori, T., Kaneko, T., Iida, H. and Iwamori, N., Comparative distributions of RSBN1 and methylated histone H4 Lysine 20 in the mouse spermatogenesis., PLoS One, pone.0253897, 16, 6, e0253897, 2021.01, During spermatogenesis, nuclear architecture of male germ cells is dynamically changed and epigenetic modifications, in particular methylation of histones, highly contribute to its regulation as well as differentiation of male germ cells. Although several methyltransferases and demethylases for histone H3 are involved in the regulation of spermatogenesis, roles of either histone H4 lysine 20 (H4K20) methyltransferases or H4K20 demethylases during spermatogenesis still remain to be elucidated. Recently, RSBN1 which is a testis-specific gene expressed in round spermatids was identified as a demethylase for dimethyl H4K20. In this study, therefore, we confirm the demethylase function of RSBN1 and compare distributions between RSBN1 and methylated H4K20 in the seminiferous tubules. Unlike previous report, expression analyses for RSBN1 reveal that RSBN1 is not a testis-specific gene and is expressed not only in round spermatids but also in elongated spermatids. In addition, RSBN1 can demethylate not only dimethyl H4K20 but also trimethyl H4K20 and could convert both dimethyl H4K20 and trimethyl H4K20 into monomethyl H4K20. When distribution pattern of RSBN1 in the seminiferous tubule is compared to that of methylated H4K20, both dimethyl H4K20 and trimethyl H4K20 but not monomethyl H4K20 are disappeared from RSBN1 positive germ cells, suggesting that testis-specific distribution patterns of methylated H4K20 might be constructed by RSBN1. Thus, novel expression and function of RSBN1 could be useful to comprehend epigenetic regulation during spermatogenesis..
3. Kaneko, T., Toh, S., Mochida, I., Iwamori, N., Inai, T. and Iida, H., , Identification of TMCO2 as an acrosome-associated protein during rat spermiogenesis. , Molecular Reproduction and Development, 10.1002/mrd.23396, 87, 7, 808-818, 2020.07, We isolated the transmembrane and coiled-coil domains 2 (Tmco2) gene using a PCR-based subtraction technique. Tmco2 is predominantly expressed in rat testes starting at 4 weeks of age. Rat TMCO2 consists of 187 amino acids with predicted molecular mass of 20.6 kDa. When expressed in COS7 cells, TMCO2 was found as vesicle-like structures in the cytoplasm, while TMCO2ΔTM lacking the transmembrane region (TM) was found diffused in the cytoplasm. These results suggest that the transmembrane region in TMCO2 is essential for its specificity of localization. Immunocytochemical analyses indicated that rat TMCO2 was localized as small semiluminate bodies or cap-like structures in the vicinity of round spermatid nuclei, and as curved lines associated with nuclei of elongated spermatids and caput epididymal spermatozoa. However, it was detected in only small part of cauda epididymal spermatozoa. Double immunolabeling of the spermatids and spermatozoa with the anti-TMCO2 antibody and the monoclonal anti-MN7 antibody showed that TMCO2 was predominantly associated with the inner acrosomal membrane in spermatids and caput epididymal spermatozoa. Our findings suggest that TMCO2 might be involved in the process of acrosome biogenesis, especially binding of acrosome to a nucleus, during spermiogenesis..
4. Kaneko, T., Minohara, T., Shima, S., Yoshida, K., Fukuda, A., Iwamori, N., Inai, T. and Iida, H.,, A membrane protein, TMCO5A, has a close relationship with manchette microtubules in rat spermatids during spermiogenesis, Molecular Reproduction and Development, 10.1002/mrd.23108, 86, 3, 330-341, 2019.03, We isolated the transmembrane and coiled-coil domains 5A (Tmco5A) gene using polymerase chain reaction-based subtraction technique and showed that Tmco5A was predominantly expressed in rat testes starting at 4 weeks of postnatal development. When expressed in COS7 cells, TMCO5A was found to be distributed in the endoplasmic reticulum-nuclear membrane (ER-NM) of cells as a membrane-associated protein, while TMCO5AΔC lacking the transmembrane region (TM) mislocalized and diffused throughout the cytoplasm. The result suggested that TM is responsible for the retention of TMCO5A at the ER-NM. Immunocytochemical and immunoblotting analyses indicated that TMCO5A was localized along the posterior part of the nuclei in both round and elongated rat spermatids but disappeared from epididymal spermatozoa. Double immunolabeling of isolated spermatids with the anti-TMCO5A and the anti-β tubulin antibodies showed that TMCO5A was always found to be closely associated with developing manchette microtubules but did not completely colocalize with them. On the other hand, we found that almost all TMCO5A colocalized with SUN4, a linker of nucleoskeleton and cytoskeleton complex protein present at the posterior part of spermatid nuclei. These data suggested that TMCO5A is located closer to the nuclei than the manchette microtubules. It is likely that TMCO5A, in association with manchette microtubules, is involved in the process of spermiogenesis..
5. Yusuke Sato, Hideaki Ohtsubo, Naohiro Nihei, Takane Kaneko, Yoriko Sato, Shin Ichi Adachi, Shinji Kondo, Mako Nakamura, Wataru Mizunoya, Hiroshi Iida, Ryuichi Tatsumi, Cristina Rada, Fumiaki Yoshizawa, Apobec2 deficiency causes mitochondrial defects and mitophagy in skeletal muscle, FASEB Journal, 10.1096/fj.201700493R, 32, 3, 1428-1439, 2018.03, Apobec2 is a member of the activation-induced deaminase/apolipoprotein B mRNA editing enzyme catalytic polypeptide cytidine deaminase family expressed in differentiated skeletal and cardiac muscle. We previously reported that Apobec2 deficiency in mice leads to a shift in muscle fiber type, myopathy, and diminished muscle mass. However, the mechanisms ofmyopathy caused by Apobec2 deficiency and its physiologic functions are unclear. Here we show that, although Apobec2 localizes to the sarcomeric Z-lines in mouse tissue and cultured myotubes, the sarcomeric structure is not affected in Apobec2-deficient muscle. In contrast, electron microscopy reveals enlarged mitochondria and mitochondria engulfed by autophagic vacuoles, suggesting that Apobec2 deficiency causes mitochondrial defects leading to increased mitophagy in skeletal muscle. Indeed, Apobec2 deficiency results in increased reactive oxygen species generation and depolarized mitochondria, leading to mitophagy as a defensive response. Furthermore, the exercise capacity of Apobec2-/- mice is impaired, implying Apobec2 deficiency results in ongoing muscle dysfunction. The presence of rimmed vacuoles in myofibers from 10-mo-old mice suggests that the chronic muscle damage impairs normal autophagy. We conclude that Apobec2 deficiency causes mitochondrial defects that increase muscle mitophagy, leading to myopathy and atrophy. Our findings demonstrate that Apobec2 is required for mitochondrial homeostasis to maintain normal skeletal muscle function..
6. Kaneko, T., Toshimori, K. and Iida H., Subcellular localization of MS4A13 isoform 2 in mouse spermatozoa., Reproduction, doi: 10.1530/REP-17-0477, 154, 6, 843-857, 2017.12, To identify upregulated genes during the development of spermatozoa, we performed PCR-selected subtraction analysis of testes RNA samples from 10-day-old and 12-week-old shrews. A transcript, highly homologous to two mouse transcripts, Ms4a13-1 and Ms4a13- 2, was differentially regulated. Ms4a13-2, but not Ms4a13-1, was shown to be primarily expressed in mouse testes in an agedependent manner. Ms4a13-2 cDNA contains an open-reading frame of 522 nucleotides, encoding a protein of 174 amino acids, with predicted molecular mass, 19,345 Da. MS4A13-2 protein was expressed along the periphery of nuclei of round and elongated spermatids (steps 3–16) in adult mouse testes, and in the equatorial region of the heads of fresh mature mouse spermatozoa. In addition, MS4A13-2 was found to localize to the outer acrosomal membrane in the equatorial region of heads in fresh spermatozoa. In acrosome-reacted spermatozoa, the MS4A13-2 expression extended to the entire sperm head including the postacrosomal region and acrosomal cap. MS4A family proteins are known to facilitate intracellular protein–protein interactions as ion channel/adaptor proteins by oligomerization, and have important regulatory roles in cellular growth, survival and activation. We report that the MS4A family member, MS4A13-2, may form oligomers in sperm membranes, which may be involved in an interaction with the zona pellucida or cumulus during fertilization..
7. Shotaro Nishimura, Miyu Yamashita, Takane Kaneko, Fuminori Kawabata, Shoji Tabata, Cytokeratin-positive folliculo-stellate cells in chicken adenohypophysis, Animal Science Journal, 10.1111/asj.12866, 88, 11, 1835-1841, 2017.11, Folliculo-stellate (FS) cells are non-endocrine cells found in the adenohypophysis and are identified in many animals by the S100 protein marker. Although keratin is another FS marker in several animals, there is no information on localization of keratin in the avian adenohypophysis. In this study, localization of cytokeratin in chicken adenohypophyseal cells was investigated immunohistochemically. Basic cytokeratin (bCK)-positive cells were arranged radially in the cell cords with their cytoplasmic processes reaching the basal lamina. The cell bodies encircled a follicle in the center of the cell cord. Furthermore, the bCK-positive cells were also S100B-positive. Growth hormone, prolactin, adrenocorticotrophic hormone, and luteinizing hormone β-subunit did not co-localize with the bCK-positive cells. In addition, the bCK-positive cells had a laminin-positive area in their cytoplasm. Transmission electron microscopy observed agranular cells equipped with several microvilli that encircled a follicle. These results indicate that bCK-positive cells in the chicken adenohypophysis may be a predominant FS cell population and produce laminin. It is suggested that they function as sustentacular cells to sustain the adjacent endocrine cells and the structure of the cell cords in the chicken adenohypophysis..
8. Airi Yamaguchi, Takane Kaneko, hiroshi iida, Molecular Cloning and Subcellular Localization of Tektin2-Binding Protein1 (Ccdc 172) in Rat Spermatozoa., Journal of Histochemistry and Cytochemistry, 62, 4, 286-297, 2014.04.
9. Takiguchi, H., Murayama, E., Kaneko, T., Kurio, H., Toshimori, K. and Iida, H. , Characterization and subcellular localization of Tektin 3 in rat spermatozoa., Molecular Reproduction and Development, 78, 611-620, 2011.08.
10. Kurio, H., Hatsuda, H., Murayama, E., Kaneko, T. and Iida, H., Identification of CEACAM6 as an intermediate filament-associated protein expressed in Sertoli cells of rat testis., Biology of Reproduction, 85, 924-933, 2011.06.
11. Kaneko, T., Iwamoto, S., Murayama, E., Kurio, H., Inai, T., Oda, S. and Iida, H. , Immunolocalization of Spetex-1 at the connecting piece in spermatozoa of the musk shrew (Suncus murinus)., Zoological Science, 28, 6, 444-452, 2011.06.
12. Shimasaki, S., Yamamoto, E., Murayama, E., Kurio, H., Kaneko, T., Shibata, Y., Inai, T. and Iida, H. , Subcellular Localization of Tektin2 in Rat Sperm Flagellum., Zoological Science, 27, 755-761, 2010.09.
13. Kaneko, T., Murayama, E., Kurio, H., Yamaguchi, A. and Iida, H. , Characterization of Spetex-1, a new component of satellite fibrils associated with outer dense fibers in the middle piece of rodent sperm flagella. , Molecular Reproduction and Development, 77, 363-372, 2010.04.
14. Yano, R., Matsuyama, T., Kaneko, T., Kurio, H., Murayama, E., Toshimori, K. and Iida, H. , Bactericidal/permeability - increasing protein (BPI) is associated with the acrosome region of rodent epididymal spermatozoa. , Journal of Andrology, 31, 201-214, 2010.03.
15. Morphological Studies of Functional Molecules Building Mammalian Sperm Flagella..
16. The reexamined mammalian systematics..
17. Kurio, H., Murayama, E., Kaneko, T., Shibata, Y., Inai, T. and Iida, H., Intron 
retention generates a novel isoform of CEACAM6 that possibly acts as 
an adhesion molecule at ectoplasmic specialization between spermatids 
and sertoli cells in rat testis., Biology of Reproduction, 79:1062-1073., 2008.08.
18. Murayama, E., Yamamoto, E., Kaneko, T., Shibata, Y., Inai, T. and Iida, H., Tektin5, a new TEKTIN family member, is a component of the middle piece of flagella in rat spermatozoa., Molecular Reproduction and Development, 75:650–658, 2008.04.
19. Murayama, E., Katoh, M., Kanebayashi, A., Kaneko, T., Shibata, Y., Inai, T. and Iida, H. , Germ cell-less like 2 protein is a new component of outer dense fibers in rat sperm flagella. , Reproduction, 134:749-756, 2007.12.
20. Acrosome reaction of suncus spermatozoa. (2007) Kaneko, T. and Iida, H. Laboratory Animal Technology and Science, 19(4): 25-29..
21. Kaneko, T., Mori, T. and Ishijima, S., Digital image analysis of the flagellar beat of activated and hyperactivated Suncus spermatozoa., Molecular Reproduction and Development, 74:478-485, 2007.01.
22. Doiguchi, M., Kaneko, T., Urasoko, A., Nishitani, H. and Iida, H., Identification of a heat shock protein Hsp40, DjB1, as an acrosome- and a tail-associated component in rodent spermatozoa., Molecular Reproduction and Development, 74:223-232, 2007.01.
23. Iida, H., Noda, M., Kaneko, T., Doiguchi, M. and Mori, T., Identification of rab12 as a vesicle-associated small GTPase highly expressed in Sertoli cells of rat testis., Molecular Reproduction and Development, 10.1002/mrd.20294, 71, 2, 178-185, 71:178-185, 2005.05.
24. Iwamoto, Y., Kaneko, T., Ichinose, J., Mori, T., Shibata, Y., Toshimori, K. and Iida, H., Molecular cloning of rat Spetex-2 family genes mapped on chromosome 15p16, encoding a 23-kilodalton protein associated with the plasma membranes of haploid spermatids., Biology of Reproduction, 10.1095/biolreprod.104.032516, 72, 2, 284-292, 72:284-292, 2005.02.
25. Iida, H., Yamashita, H., Doiguchi, M. and Kaneko, T., Molecular cloning of rat spergen-3, a spermatogenic cell-specific gene-3, encoding a novel 75 kDa protein bearing EF-hand motifs., Journal of Andrology, 25, 6, 885-892, 25:885-892, 2004.11.
26. Iida, H., Ichinose, J., Kaneko, T., Mori, T. and Shibata Y., Complementary DNA cloning of rat Spetex-1, a spermatid-expressing gene-1, encoding a 63 kDa cytoplasmic protein of elongate spermatids., Molecular Reproduction and Development, 10.1002/mrd.20101, 68, 4, 385-393, 68:385-393, 2004.08.
27. Kaneko, T., Iida, H., Bedford, J. M., Oda, S. and Mori, T., Mating-induced cumulus-oocyte maturation in the shrew, Suncus murinus., Reproduction, 10.1530/rep.0.1260817, 126, 6, 817-826, 126:817-826, 2003.12.
28. Oh, H., Yoshinaga, Y., Kaneko, T., Iida H. and Mori, T., Taxonomic reexamination of the Apodemus agrarius chejuensis, comparing external and cranial morphological characters among four Asian Apodemus species., Journal of the Faculty of Agriculture Kyushu University, 47: 131-144, 2003.02.
29. Iida, H., Mori, T., Kaneko, T., Urasoko, A., Yamada, F. and Shibata, Y., Disturbed spermatogenesis in mice prenatally exposed to an endocrine disruptor, Bisphenol A., Mammal Study, 27: 73-82, 2002.05.
30. Kaneko, T., Iida, H., Bedford, J. M. and Mori, T., Spermatozoa of the shrew, Suncus murinus, undergo the acrosome reaction and then selectively kill cells in penetrating the cumulus oophorus., Biology of Reproduction, 10.1095/biolreprod65.2.544, 65, 2, 544-553, 65: 544-553, 2001.05.
31. Iida, H., Kaneko, T., Tanaka, S. and Mori, T., Association of the developing acrosome with multiple small Golgi units, the Golgi satellites, in spermatids of the musk shrew, Suncus murinus., Journal of Reproduction and Fertility, 10.1530/reprod/119.1.49, 119, 1, 49-58, 119: 49-58, 2000.01.