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Cellular Biochemistry Laboratory, Graduate school of Pharmaceutical Sciences, Nagoya University

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Mizuno T, Nagano F, Ito Y, Tatsukawa H, Shinoda Y, Takeuchi T, Takahashi K, Tsuboi N, Nagamatsu T, Yamada S, Maruyama S, Hitomi K.
Novel function of transglutaminase 2 in extracellular histone-induced acute lung injury.
Biochem Biophys Res Commun. 2023 Aug 23;678:179-185. doi: 10.1016/j.bbrc.2023.08.051. Online ahead of print. PMID: 37643535

Watanabe Y, Katsumura E, Domon T, Ishikawa Y, Oguri R, Takashima M, Meng Q, Kinoshita M, Hashimoto H, Hitomi K.
Establishment of transgenic epithelium-specific Cre-recombinase driving medaka (Oryzias latipes) by homology repair mediated knock-in.
Biosci Biotechnol Biochem. 2023 Aug 22:zbad116. doi: 10.1093/bbb/zbad116. Online ahead of print. PMID: 37607777

Tatsukawa H, Aoyama R, Hitomi K.
Development of peptide-based biosensors for detecting cross-linking and deamidation activities of transglutaminases.
Amino Acids. 2023 Jun;55(6):807-819. doi: 10.1007/s00726-023-03272-7. PMID: 37165293

Shinoda Y*, Tatsukawa H*, Yonaga A, Wakita R, Takeuchi T, Tsuji T, Tanaka M, Suganami T, Hitomi K.
Tissue transglutaminase exacerbates renal fibrosis via alternative activation of monocyte-derived macrophages.
Cell Death Dis. 2023 Mar 2;14(2):136. doi: 10.1038/s41419-023-05622-5. PMID: 36864028
<2023年3月3日 名古屋大学プレスリリース>
「腎臓の機能不全を引き起こすマクロファージの制御因子を発見 ~線維化、癌、動脈硬化などの新たな治療法開発に繋がることが期待~」


<March 23, 2023 Press release(英語版)>

Kunoki S, Tatsukawa H, Sakai Y, Kinashi H, Kariya T, Suzuki Y, Mizuno M, Yamaguchi M, Sasakura H, Ikeno M, Takeuchi K, Ishimoto T, Hitomi K, Ito Y.
Inhibition of transglutaminase 2 reduces peritoneal injury in a chlorhexidine-induced peritoneal fibrosis model.
Lab Invest. 2023 Jan 10;103(4):100050. doi: 10.1016/j.labinv.2022.100050. PMID: 36870292

Teshima H, Endo M, Furuyama Y, Takama H, Akiyama M, Tsuji T, Tatsukawa H, Hitomi K.
Involvement of hypoxia-inducible factor activity in inevitable air-exposure treatment upon differentiation in a three-dimensional keratinocyte culture.
FEBS J. 2022 Dec 22. doi: 10.1111/febs.16707 PMID: 36549886

Meng Q, Watanabe Y, Tatsukawa H, Hashimoto H, Hitomi K.
Biochemical characterization of medaka (Oryzias latipes) fibrinogen gamma and its gene disruption resulting in anemia as a model fish.
J Biochem. 2022 Oct 19;172(5):293-302. doi: 10.1093/jb/mvac065. PMID: 35997167

Kuribayashi M, Kawaguchi Y, Teshima H, Yamaguchi H, Tatsukawa H, Hitomi K.
Investigation of mouse amniotic fluid for stimulating ability of keratinocyte differentiation depending on the fetal stage.
Arch Biochem Biophys. 2021 Oct 30;711:109003. doi: 10.1016/j.abb.2021.109003. PMID: 34390735

Takeuchi T*, Tatsukawa H*, Shinoda Y, Kuwata K, Nishiga M, Takahashi H, Hase N, Hitomi K.
Spatially resolved identification of transglutaminase substrates by proteomics in pulmonary fibrosis.
Am J Respir Cell Mol Biol. 2021 Sep;65(3):319-330. doi: 10.1165/rcmb.2021-0012OC. PMID: 34264172
<2021年7月16日 名古屋大学プレスリリース>
「肺線維症の分子標的の探索法開発および同定に成功 ~架橋修飾反応が関わる特発性肺線維症の発症機構の解明~」


Watanabe Y, Oguri R, Suzuki R, Ishikawa Y, Tatsukawa H, Hashimoto H, Hitomi K.
Thrombin-deficient mutant of medaka, a model fish, displays serious retardation in blood coagulation.
Biosci Biotechnol Biochem. 2021 Mar 24;85(4):824-833. doi: 10.1093/bbb/zbaa098. PMID: 32251518

Watanabe Y, Okuya K, Takada Y, Kinoshita M, Yokoi S, Chisada S, Kamei Y, Tatsukawa H, Yamamoto N, Abe H, Hashimoto H, Hitomi K.
Gene disruption of medaka (Oryzias latipes) orthologue for mammalian tissue-type transglutaminase (TG2) causes movement retardation.
J Biochem. 2020 Sep 1;168(3):213-222. doi: 10.1093/jb/mvaa038. PMID: 32251518

Tanabe Y, Yamane M, Kato M, Teshima H, Kuribayashi M, Tatsukawa H, Takama H, Akiyama M, Hitomi K.
Studies on differentiation-dependent expression and activity of distinct transglutaminases by specific substrate peptides using three-dimensional reconstituted epidermis.
FEBS J. 2019 Jul;286(13):2536-2548. doi: 10.1111/febs.14832. PMID: 30941897

Ito Y, Tatsukawa H, Yamaguchi H, Takahashi K, Hitomi K, Yuzawa Y.
Detection and identification of potential transglutaminase 2 substrates in the mouse renal glomeruli.
Arch Biochem Biophys. 2018 Dec 15;660:11-19. doi: 10.1016/j.abb.2018.10.001. PMID: 30300608

Kojima T, Hata J, Oka H, Hayashi K, Hitomi K, Nakano H.
Spatial arrangement of proteins using scCro-tag: application for an in situ enzymatic microbead assay.
Biosci Biotechnol Biochem. 2018 Aug 1:1-11. doi: 10.1080/09168451.2018.1501265. PMID: 30067465

Mižíková I, Pfeffer T, Nardiello C, Surate Solaligue DE, Steenbock H, Tatsukawa H, Silva DM, Vadász I, Herold S, Pease RJ, Iismaa SE, Hitomi K, Seeger W, Brinckmann J, Morty RE.
Targeting transglutaminase 2 partially restores extracellular matrix structure but not alveolar architecture in experimental bronchopulmonary dysplasia.
FEBS J. 2018 Jun 23;285(16):3056-3076. doi: 10.1111/febs.14596. PMID: 29935061

Tatsukawa H, Otsu R, Tani Y, Wakita R, Hitomi K.
Isozyme-specific comprehensive characterization of transglutaminase-crosslinked substrates in kidney fibrosis.
Sci Rep. 2018 May 9;8(1):7306 (18 pages). doi: 10.1038/s41598-018-25674-4. PMID: 29743665

Watanabe Y, Furukawa E, Tatsukawa H, Hashimoto H, Kamei Y, Taniguchi Y, Hitomi K.
Higher susceptibility to osmolality of the medaka (Oryzias latipes) mutants in orthologue genes of mammalian skin transglutaminases.
Biosci Biotechnol Biochem. 82(7), 1165-1168 (2018). doi: 10.1080/09168451.2018.1453294. PMID: 29570037

Horimizu R, Ogawa R, Watanabe Y, Tatsukawa H, Kinoshita M, Hashimoto H, Hitomi K.
Biochemical characterization of a medaka (Oryzias latipes) orthologue for mammalian Factor XIII and establishment of a gene-edited mutant.
FEBS J. 284(17), 2843-2855 (2017). doi: 10.1111/febs.14153. PMID: 28653811

Tatsukawa H, Tani Y, Otsu R, Nakagawa H, Hitomi K.
Global identification and analysis of isozyme-specific possible substrates crosslinked by transglutaminases using substrate peptides in mouse liver fibrosis
Sci Rep. 7:45049 (2017) doi: 10.1038/srep45049. PMID: 28327670

Takada Y, Watanabe Y, Okuya K, Tatsukawa H, Hashimoto H, Hitomi K.
Biochemical characterization of the medaka (Oryzias latipes) orthologue for mammalian tissue-type transglutaminase (TG2).
Biosci Biotechnol Biochem. 81(3), 469-474 (2017). doi: 10.1080/09168451.2016.1256757. PMID: 27855535

Tatsukawa H, Liu HH, Oba S, Kamiya N, Nakanishi Y, Hitomi K.
FRET-based detection of isozyme-specific activities of transglutaminases.
Amino Acids. 49(3), 615-623 (2017). doi: 10.1007/s00726-016-2322-0. PMID: 27586957

Yamane M, Sugimura K, Kawasaki H, Tatsukawa H, Hitomi K.
Analysis on transglutaminase 1 and its substrates using specific substrate peptide in cultured keratinocytes.
Biochem Biophys Res Commun. 478(1), 343-348 (2016). doi: 10.1016/j.bbrc.2016.07.051. PMID: 27416753

Qin XY, Tatsukawa H, Hitomi K, Shirakami Y, Ishibashi N, Shimizu M, Moriwaki H, Kojima S.
Metabolome Analyses Uncovered a Novel Inhibitory Effect of Acyclic Retinoid on Aberrant Lipogenesis in a Mouse Diethylnitrosamine-Induced Hepatic Tumorigenesis Model.
Cancer Prev Res (Phila). 9(3), 205-14 (2016). doi: 10.1158/1940-6207.CAPR-15-0326.

Kojima T, Mizoguchi T, Ota E, Hata J, Homma K, Zhu B, Hitomi K, Nakano H.
Immobilization of proteins onto microbeads using a DNA binding tag for enzymatic assays.
J Biosci Bioeng. 121(2), 147-53 (2016). doi: 10.1016/j.jbiosc.2015.06.003.

Kikuta A, Furukawa E, Ogawa R, Suganuma N, Saitoh M, Nishimaki T, Katsumura T, Oota H, Kawamoto T, Tatsukawa H, Hashimoto H, Kiyotaka Hitomi.
Biochemical characterization of medaka (Oryzias latipes) transglutaminases, OlTGK1 and OlTGK2, as orthologues of human keratinocyte-type transglutaminase.
PLOS One. 10(12), e0144194 (2015) doi: 10.1371/journal.pone.0144194.

Shrestha R, Tatsukawa H, Shrestha R, Ishibashi N, Matsuura T, Kagechika H, Kose S, Hitomi K, Imamoto N, Kojima S.
Molecular mechanism by which acyclic retinoid induces nuclear localization of transglutaminase 2 in human hepatocellular carcinoma cells.
Cell Death Dis. 6, e2002 (2015). doi: 10.1038/cddis.2015.339.

Tatsukawa H, Abe N, Ohashi S, Hitomi K.
Distribution of transglutaminase family members in mouse whole body sections.
Biochem Biophys Res Commun. 467(4), 1046-51 (2015). doi: 10.1016/j.bbrc.2015.10.001.

Furukawa K, Yamane M, Tatsukawa H, Hitomi K.
Early response as shown by enhancement of transglutaminase 1 expression after cisplatin-induced acute kidney injury.
Arch Biochem Biophys. 586, 27-32 (2015). doi: 10.1016/j.abb.2015.09.021.

Lee J, Condello S, Yakubov B, Emerson R, Caperell-Grant A, Hitomi K, Xie J, Matei D.
Tissue Transglutaminase Mediated Tumor-Stroma Interaction Promotes Pancreatic Cancer Progression.
Clin Cancer Res. 21(19), 4482-4493 (2015). doi: 10.1158/1078-0432.CCR-15-0226.

Suga Y, Tsuda T, Nagai M, Sakaguchi Y, Jitsukawa O, Yamamoto M, Hitomi K, Yamanishi K.
Lamellar ichthyosis with pseudoexon activation in the transglutaminase 1 gene.
J Dermatol. 42(6), 642-645 (2015). doi: 10.1111/1346-8138.12846.

Petersen-Jones HG, Johnson KB, Hitomi K, Tykocki NR, Thompson JM, Watts SW.
Transglutaminase activity is decreased in large arteries from hypertensive rats compared with normotensive controls.
Am J Physiol Heart Circ Physiol. 308(6), H592-602 (2015) doi: 10.1152/ajpheart.00402.2014.

Myneni VD, Hitomi K, Kaartinen M.
Factor XIII-A transglutaminase acts as a switch between preadipocyte proliferation and differentiation.
Blood. 124(8), 1344-1353 (2014)

Karashima T, Furumura M, Ishii N, Ohyama B, Saruta H, Natsuaki Y, Nakama T, Ohata C, Tsuruta D, Hitomi K, Hashimoto T.
Distinct protein expression and activity of transglutaminases found in different epidermal tumors.
Exp Dermatol. 23(6), 433-435 (2014)

Wang S, Cui C, Hitomi K, Kaartinen MT.
Detyrosinated Glu-tubulin is a substrate for cellular Factor XIIIA transglutaminase in differentiating osteoblasts.
Amino Acids. 46, 1513-1526 (2014)

Cui C, Wang S, Myneni VD, Hitomi K, Kaartinen MT.
Transglutaminase activity arising from Factor XIIIA is required for stabilization and conversion of plasma fibronectin into matrix in osteoblast cultures.
Bone. 59, 127-138 (2014)

Itoh M, Tatsukawa H, Eun-Seo L, Yamanishi K, Kojima S, Hitomi K.
Variations in both TG1 and TG2 isozyme-specific in situ activities and protein expressions during mouse embryonic development.
J Histochem Cytochem. 61(11), 793-801 (2013)

Kuramoto K, Yamasaki R, Shimizu Y, Tatsukawa H, Hitomi K.
Phage-displayed peptide library screening for preferred human substrate peptide sequences
for transglutaminase 7.

Arch Biochem Biophys. 537, 138-143 (2013)

Shimizu Y, Sugiura K, Aoyama Y, Ogawa Y, Hitomi K, Iwatsuki K, Akiyama M.
Novel ABCA12 missense mutation p.Phe2144Ser underlies congenital ichthyosiform erythroderma.
J Dermatol. 40, 581-582 (2013)

Fukui M, Kuramoto K, Yamasaki R, Shimizu Y, Itoh M, Kawamoto T, Hitomi K.
Identification of a highly reactive peptide for TG6: Detection of its transglutaminase activity in the skin epidermis using the peptide.
FEBS J. 280, 1420-1429 (2013)

Watanabe K., Tsunoda K., Itoh M., Fukui M., Mori H. Hitomi, K.
Transglutaminase 2 and Factor XIII catalyze distinct substrates in differentiating osteoblastic cell line: utility of highly reactive substrate peptides: utility of highly reactive substrate peptides.
Amino Acids 44, 209-214 (2013)

Sugitani, K., Ogai K., Hitomi, K., Nakamura-Yonehara K., Shintani T., Noda M., Koriyama Y., Tanii H., Matsukawa T., Kato S.
A distinct effect of transient and sustained upregulation of cellular factor XIII in the goldfish and optic nerve on optic nerve regeneration.
Neurochem. Int. 61(3), 423-432 (2012)

Yamamoto M., Sakaguchi Y., Itoh M., Nakagawa N., Fukunaga A., Hitomi K., Yamanishi K.
Bathing suit ichthyosis with summer exacerbation: a temperature-sensitive case.
Br. J. Dermatol. 166(3), 672-674 (2012)

Johnson KB., Petersen-Jones H., Thompson JM, Hitomi K, Itoh M, Bakker EN, Johnson GV, Colak G, Watts S.
Vena cava and aortic smooth muscle cells express transglutaminases 1 and 4 in addition to transglutaminase 2.
Am. J. Physiol. Heart Circ. Physiol. 302(7), H1355-1366 (2012)

H.D. de Koning, E.H. van den Bogaard, J.G.M. Bergboer, M. Kamsteeg, I.M.J.J. van Vlijmen-Willems, K. Hitomi, J. Henry, M. Simon, N. Takashita, A. Ishida-Yamamoto, J. Schalkwijk, P.L.J.M. Zeeuwen.
Expression profile of cornified envelope structural proteins and keratinocyte differentiation-regulating proteins during skin barrier repair.
Br. J. Dermatol. 166, 1245-1254 (2012)

Henry J, HSu CY, Hafter M., Nachat R., de Koninig HD., Gardinal-Galera I., Hitomi K., Balica, S., Jean-Decoster C., Schmit, AM., Paul C., Serre, G., Simon M.
Hornein is the component of cornified cell envelops.
FASEB J. 25, 1567-1576 (2011).

Itoh M., Kawamoto T., Tatsukawa H., Kojima S., Yamanishi K., Hitomi K.
In situ detection of active transglutaminases for keratinocyte-type (TGase 1) and tissue-type (TGase 2) using fluorescence-labeled highly reactive substrate peptides.
J. Histochem. Cytochem. 59, 180-187 (2011).

Sugimura Y. Yamashita H., Hitomi K.
Screening of substrate peptide sequecne for tissue-type transglutaminase using T7 phage cDNA library.
Cytotechnol. 63, 111-118 (2011).

Yamane A., Fukui M., Sugimura Y., Itoh M., Alea M. P , Said El Aloui, Akiyama M., Hitomi K.
Identification and Characterization of Preferred Substrate Peptide for Transglutaminase 3 Using Random Peptide Library: Detection of In Situ Isozyme-Specific Activity in the Skin and the Hair Follicles.
FEBS J. 277, 3564 (2010). *The first and second authors contribute equally.

Zeeuwen PM., van Vlijmen-Willems I., Cheng T., Rodijk-Olthuis1 D., Hitomi K., Hara-Nishimura I., John S. Smyth N., Reinheckel T., Hendriks WJ., Schalkwijk J.
The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea.
FASEB J. 10, 3744 (2010).

Akiyama M, Sakai K, Yanagi T., Fukushima S., Ihn H., Hitomi K., Shimizu H.
Transglutaminase1 Preferred Substrate Peptide K5 Is an Efficient Tool in Diagnosis of Lamellar Ichthyosis.
Am. J. Pathol. 129, 2306-2309 (2010).

Hitomi K., Kitamura M., Alea M. P., Ismail Thomas V., Alaoui S El.
A Specific Colorimetric assay for measuring transglutaminase 1 and factor XIII activities.
Anal. Biochem. 394, 281-284 (2009).

Hitomi K., Kitamura Y., Sugimura Y.
Preferred substrate sequences for transglutaminase 2: screening using a phage-displayed peptide library.
Amino Acids 36(4), 619-624 (2009).

Alea M. A., Kitamura M, Martin G., Thomas V., Hitomi K., Alaoui S. E.
Development of an isozyme-specific colorimetric assay for tissue transglutaminase 2 cross-linking assay.
Anal. Biochem. 389, 150-156 (2009).

Sugimura Y, Hosono M, Kitamura M, Tsuda T, Yamanishi K, Maki M, Hitomi K.
Identification of preferred substrate sequences for transglutaminase 1: development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin.
FEBS J. 275, 5667-5677 (2008). *first and second authors equally contribute

Cheng, Ivonne MJJ, van Vlijmen-Willems, Hitomi K., PEJ van Erp, Schalkwijk J., Zeeuwen P.
Colocalization of cystatin M/E and its target proteases suggests a role in terminal differentiation of human nail and hair follicle.
J Invest. Dermatol. 129, 1232-1242 (2009).

T. Cheng, G.S. Tjabringa, I.M.J.J. van Vlijmen-Willems, K. Hitomi, P.E.J. van Erp, J.Schalkwijk, and P.L.J.M. Zeeuwen
A biochemical pathway that controls skin barrier formation: expression of its key components in inflammatory skin diseases and in reconstructed skin.
Br J. Dermatol. 161, 253-264 (2009).

Sugimura, Y., Yokoyama, K., Nio, N., Maki, M., and Hitomi, K.
Identification of the preferred substrate sequences of microbial transglutaminase from Streptomyces mobaraensis using a phage-displayed peptide library.
Arch. Biochem. Biophys. 477, 379-383 (2008)

Kawai, Y., Wada, F., Sugimura, Y., Maki, M., and Hitomi, K.
Transglutaminase 2 activity promotes membrane resealing upon mechanical damages in a lung cancer cell line A549.
Cell Biol Int. 32, 928-934 (2008)

Kondoh, N., Ishikawa, T., Ohkura, S., Arai, M., Hada, A., Yamazaki, Y., (他 6名) Hitomi, K. and Yamamoto, M.
Gene expression signatures that classify the mode of invasion of primary oral squamous cell carcinomas.
Mol. Caricinogen. 47, 744 (2008)

Yorikawa C., Takaya E., Ohsako Y., Terasawa, Y., Hamakubo T., Mochizuki, Y., Iwanari H., Kodama, T., Maeda, T., Hitomi, K., Shibata, H., Maki M.
Human calpain 7/PalBH associates with a subset of ESCRT-III-related proteins in its N-terminal region and partly localizes to endocytic membrane compartments.
J. Biochem. 143, 731-745 (2008)

Sugimura Y., Ueda H., Maki M., and Hitomi K.
Novel site-specific immobilization of functional protein using a preferred substrate sequence
for transglutaminase 2.

J. Biotechnol. 131(2) 121-127 (2007)

Wada, F. Hasegawa, H., Nakamura, A., Kawai, Y., Sasaki, N., Shibata, H., Maki, M., and Hitomi, K.
Identification of substrates for transglutaminase in Physarum polycehalum, an acellualr slime mold, upon cellular mechanical damage.
FEBS J. 274, 2766-2777 (2007)

Jiang, X., Suzuki, H., Hanai, Y., Wada F., Hitomi, K., Yamane, T., Nakano, H.
A novel strategy for generation of monoclonal antibodies from single B cells using rt-PCR technique and in vitro expression.
Biotechnol. Prog. 22, 979-988 (2006)

Sugimura, Y., Hosono, M., Yoshimura, T., Maki, M., and Hitomi, K.
Screening of the preferred subsrtrate sequence of transglutaminase using a phage-displayed peptide library.
J. Biol. Chem. 281, 17699-17706 (2006)

T. Cheng, K. Hitomi, I. M.J.J. van Vlijmen-Willems, D. Olthuis, M. Bergers, K. Yamamoto, K. Nishi, C. Watts, T. Reinheckel, J. Schalkwijk, and P. L.J.M. Zeeuwen (First and second authors equally contribute to this work)
Csytatin is a high affinity inhibitor for cathepsin V and one-chain form of cathepsin L by a reactive site that is from the legumain binding site. A role of cystatin M/E in epidermal cornification.
J .Biol. Chem. 281, 15893-15899 (2006)

Ali, M., Hitomi, K., and Nakano, H.
Generation of monoclonal antibodies using simplified single-cell reverse transcription-polymerase chain reaction and cell-free protein synthesis.
J. Biosci. Bioeng. 101, 284-286 (2006)

El-Halawany M., Shibata, H., Hitomi, K., and Maki, M.,
Reevalutation of the predicted gene structure of Dictyostelium cystatin A3 by nucleotide sequence determination of its cDNA andits phylogenetic position in the cystatin superfamily
Mol. Biol. Rep. 32, 257-264 (2005)

Wada, F., Ogawa, A., Hanai, Y., Nakamura, A. Maki, M., and Hitomi, K.
Analyses of expression and localization of two mammalian-type transglutaminases in Physarum Polycephalum, an acellular slime mold.
J. Biochem. 136, 665-672 (2004)

Zeeuwen, P.M., van Vlijmen-Willems, I., Olthuis1, D., Johansen, H.T., Hitomi, K., Hara-Nishimura, I., Powers, J. C., James, K. E., Camp, H. J., Lemmens1, R., and Schalkwijk1, J.
Evidence that unrestricted legumain activity is involved in disturbed epidermal cornifcation in cystatin M/E deficient mice.
Hum. Mol. Genet. 13, 1069-1079 (2004)

Medhat, El-H., Ohkouchi, S., Shibata, H., Hitomi, K., and Maki, M.
Identification of cysteine protease inhibitors that belong to cystatin family 1 in the cellular slime mold Dictyostelium discoideum.
Biol. Chem. 385, 547-550 (2004)

Ohkouchi, S., Medhat, El-H., Maeda, M., Shibata, H., Hitomi, K., and Maki, M.
DdAlix, an Alix/AIP1 homolog in Dictyostelium discoideum, is required for multicellular development under low Ca conditions.
Gene 337,131-139 (2004)

Hitomi, K., Ikeda, N., and Maki, M.
Immunological detection of proteolytically activated epidermal-type transglutaminase (TGase 3) using cleavage site specific antibody.
Biosci. Biotechnol. Biochem. 67, 2492-2494 (2003)

Hitomi, K., Nakayama T., Presland, R.B., Fleckman, P. Dale, B. A., and Maki M.
Analysis of epidermal-type transglutaminase in human stratified epithelia and cultured keratinocytes using monospecific antibodies.
J. Dermatol. Sci. 32, 905-103 (2003)

Wada F., Nakamura, A., Masutani, T., Ikura, K., Maki, M., and Hitomi, K.
Identification of Mammalian-type Transglutaminase in Physarum polycephalum: Evidence from cDNA sequence and involvement of GTP in the regulation of transamidating activity.
Eur. J. Biochem. 269, 3451-3460 (2002)

Ohkouchi, S., Nishio K., Maeda M., Hitomi K., Adachi H., and Maki M.
Identification and characterization of two penta-EF-Hand Ca2+-binding proteins in Dictyostelium discoideum. 
J. Biochem (Tokyo) 130, 207-215 (2001)

Hitomi, K., Horio, Y., Ikura K., Yamanishi K., and Maki M.
Analysis of epidermal transglutaminase (TGase 3) expression in mouse tissues and cell lines.
Int. J. Biochem. Cell Biol. 33, 491-498 (2001)

Kitaura, Y., Matsumoto, S., Satoh, H., Hitomi, K., and Maki M.
Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner.
J. Biol. Chem. 276,14503-14508 (2001)

Hitomi, K., Yamagiwa, Y., Ikura, K., Yamanishi, K., and Maki, M.
Characterization of human recombinant transglutaminase 1 purified from baculovirus-infected insect cells.
Biosci. Biotechnol. Biochem. 64, 2128-2137 (2000)

Takano J., Watanabe M., Hitomi K., and Maki M.
Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues.
J. Biochem. (Tokyo), 128, 83-92 (2000)

Hitomi K., Murase M., Kawamura T., and Maki M.
Constant expression of mouse calpastatin isoforms during differentiation in myoblast cell line, C2C12.
Cytotechnology 33, 63-70 (2000)

Hitomi K., Ikura K., and Maki M.
GTP, an inhibitor of transglutaminases, is hydrolyzed by tissue-type transglutaminase (TGase 2) but not by epidermal-type transglutaminase (TGase 3).
Biosci. Biotechnol. Biochem. 64, 657-659 (2000)

Hitomi K., Kanehiro S., Ikura K., and Maki M.
Characterization of recombinant mouse epidermal-type transglutaminase (TGase 3):regulation of its activity by proteolysis and guanine nucleotides.
J. Biochem.(Tokyo) , 125, 1048-1054 (1999)

Takano J., Kawamura T., Murase M., Hitomi K., and Maki M.
Structure of mouse calpastatin isoforms:Implication of species-common and species-specific alternative splicing.
Biochem. Biophys. Res. Commun. 260, 339-345 (1999)

Kitaura Y., Sato H., Watanabe M., Kawai T., Hitomi K., and Maki M.
Peflin, a novel member of the five-EF-hand-protein family, is similar to the apoptosis-linked-gene 2 (ALG-2) protein but possesses nonapeptide repeats in the N-terminal hydrophobic region.
Biochem. Biophys. Res. Commun. 263, 68-75 (1999)

Hitomi K. , Yokoyama A., and Maki M.
Expression of biologically active human calpastatin in baculovirus-infected insect cells and in Escherichia coli.
Biosci. Biotechnol. Biochem. 62,136-141 (1998)

Hitomi K., Uchiyama Y., Ohkubo I., Kunimatsu M., Sasaki M., and Maki M.
Purification and characterization of the active-site-mutated recombinant human mu-calpain in baculovirus-infected insect cells.
Biochem. Biophys. Res. Commun. 246, 681-685 (1998)

Maki M., Yamaguchi K., Kitaura Y., Sato H., and Hitomi K.
Calcium-induced exposure of hydrophobic surface on mouse ALG-2 which is a member of the penta-EF-hand protein family.
J. Biochem. 124, 1170-1177 (1998)

Takahashi C., Sheng Z., Horan T.P., Kitayama H., Maki M., Hitomi K., Kitaura Y., Takai S., Sasahara R.M., Horimoto R., Ikawa Y., Ratzkin B., Arakawa T., and Noda M.
Regulation of matrix metalloprotease-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK.
Proc. Natl. Acad. Sci. U.S.A. 95, 13221-13226 (1998)

Mizutani A., Maki H., Torii Y., Hitomi K., and Tsukagoshi N.,
Ascorbate-dependent enhancement of nitric oxide formation in activated macrophages.
Nitric Oxide 2, 235-241 (1998)

Edy M. Vilei, E.M., Calderara, S., Anagli, J., Berardi S., Hitomi K., Maki M., and Carafoli E.,
Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit.
J. Biol. Chem. 272, 25802-25906 (1997)

Mizutani A., Nakagawa N., Hitomi K., and Tsukagoshi N.
Ascorbate-dependent expression of ubiquitin genes in guinea pigs.
Int. J. Biochem. Cell. Biol. 29, 575-582 (1997)

Maki, M., Narayam, A.V.L., and Hitomi, K.
A growing family of the calcium-binding proteins with five EF-hand motifs.
Biochem. J. 328, 718-720 (1997).

Fukuda A., Osawa T., Hitomi K., and Uchida K.
4-hydroxy-2-nonenal cytotoxitciy in renal proximal tubular cells: Protein modification and redox alteration.
Arch. Biochem. Biophys. 333, 419-426 (1996)

Torii Y., Hitomi K., Yamagishi Y., and Tsukagoshi N.
Demonstration of alkaline phosphatase participation in the mineralization of osteoblasts by antisense RNA approach.
Cell Biol. Int. 20, 459-464 (1996)

Torii Y., Hitomi K., and Tsukagoshi N.
Synergistic effect of BMP-2 and ascorbate on the phenotypic expression of osteoblastic MC3T3- E1.
Mol. Cell. Biochem. 165, 25-29 (1996)

Torii Y., Hitomi K., and Tsukagoshi N.
L-Ascorbic acid 2-phosphate promotes osteoblastic differentiation of MC3T3-E1 mediated by type I collagen.
J. Nutr. Sci. Vitaminol. 40, 229-238 (1994)

Hitomi K. and Tsukagoshi N.
cDNA sequence for rkST1, a novel member of the sodium ion-dependent glucose cotransporter family.
Biochim. Biophys. Acta. 1190, 469-472 (1994)

Suzuki H., Torii Y., Hitomi K., and Tsukagoshi N.
Ascorbate-dependent elevation of mRNA levels for cytochrome P450s induced by polychlorinated biphenyls.
Biochem. Pharmacology 46, 186-189 (1993)

Hitomi K., Torii Y., and Tsukagoshi N.
Increase in the activity of alkaline phosphatase by l-ascorbic acid 2-phosphate in a human osteoblast cell line.
J. Nutr. Sci. Vitaminol. 38, 535-544 (1992)

Okuno Y., Suzuki A., Ichiba S., Takahashi T., Nakamura K., Hitomi K., Sasaki R., Tada K., and Imura H.
Establishment of an erythroid cell line (JK-1) that spontaneously differentiation to red cells.
Cancer 66, 1544-1551 (1990)

Okuno Y., Takahashi T., Ichiba S., Suzuki A., Nakamura K., Hitomi K., and Sasaki R.
Expression of erythropoietin receptor on a human myeloma cell line.
Biochem. Biophys. Res. Commun. 170, 1128-1148 (1990)

Hitomi K., Masuda S., Itoh H., Ueda M., and Sasaki R.
Solubilization and characterization of erythropoietin receptor from transplantable mouse erythroblastic leukemic cell line.
Biochem. Biophys. Res. Commun. 160, 1140-1148 (1989)

Shirai Y., Hashimoto K., Kawahara H., Sasaki R., Hitomi K., and Chiba H.
Production of erythropoietin by BHK cells growing on the microcarriers trapped in alginate cells.
Cytotechnology 2, 141-145 (1988)

Shirai Y., Sasaki R., Hashimoto K., Kawahara H., Hitomi K., and Chiba H.
Continuous production of erythropoietin with immobilized animal cells.
Appl. Microbial. Biotechnol. 29, 544-549 (1988)

Itoh K., Sasaki R., Ono K., Tezuka H., Sakoda H., Sawada H., Hitomi K., Nakane H.,Uchiyama T., Uchino H., and Mori K.
Stromal cell-dependent growth of leukemic cells from murine erythroblastic leukemia.
Jpn. J. Cancer Res. (Gann) 79, 931-937 (1988)

Hitomi K., Fujita K., Sasaki R., Chiba H., Okuno Y., Ichiba S., Takahashi T., and Imura H.
Erythropoietin receptor of a leukemic cell line with erythroid characteristics.
Biochem. Biophys. Res. Commun. 154, 902-909 (1988)

Sasaki R., Yanagawa S., Hitomi K., and Chiba H.
Characterization of erythropoietin receptor of murine erythroid cells.
Eur. J. Biochem. 168, 43-48 (1987)

Yanagawa S., Hitomi K., Sasaki R., and Chiba H.
Isolation and characterization of cDNA encoding rabbit reticulocyte 2,3-bisphosphoglycerate synthase.
Gene, 44, 185-191 (1986)


総説・著書 など


辰川英樹、人見清隆(5. 細胞外マトリクス 項目の執筆分担)
実験医学別冊 もっとよくわかる!シリーズ「もっとよくわかる!線維化と疾患」-炎症・慢性疾患の初期からはじまるダイナミックな過程をたどる-
羊土社 2023年09月20日発行 B5判 172ページ ISBN 978-4-7581-2213-9. Web link


辰川英樹、人見清隆
臓器の線維化を誘導するタンパク質架橋酵素の網羅的な分子標的解析
B&I バイオサイエンスとインダストリー 第80巻2号 113-117 (2021). Web link

Tatsukawa H, Hitomi K.
Role of Transglutaminase 2 in Cell Death, Survival, and Fibrosis.
Cells. 2021 Jul 20;10(7):1842. doi: 10.3390/cells10071842. PMID: 34360011

辰川英樹、篠田祥希、竹内大修、人見清隆
タンパク質架橋酵素を介した上皮細胞の間葉転換機構の解析
日本応用酵素協会誌 No. 55 1-9 (2020).

Tatsukawa H, Takeuchi T, Shinoda Y, Hitomi K.
Identification and characterization of substrates crosslinked by transglutaminases in liver and kidney fibrosis.
Anal Biochem. 2020 Sep 1;604:113629. doi: 10.1016/j.ab.2020.113629. Online ahead of print. PMID: 32061735

Meng Q, Watanabe Y, Suzuki R, Oguri R, Tatsukawa H, Hitomi K.
Transglutaminase orthologues for medaka fish research model- biochemical characterization and establishment of gene-deficient mutants.
Anal Biochem. 2020 Sep 1;604:113610. doi: 10.1016/j.ab.2020.113610. Online ahead of print. PMID: 32014415

Teshima H, Kato M, Tatsukawa H, Hitomi K.
Analysis of the expression of transglutaminases in the reconstructed human epidermis using three-dimensional cell culture.
Anal Biochem. 2020 Aug 15;603:113606. doi: 10.1016/j.ab.2020.113606. Online ahead of print. PMID: 32004543

手島裕文, 加藤まなみ, 辰川英樹, 人見清隆
皮膚表皮形成を司るタンパク質架橋化酵素・トランスグルタミナーゼ 
シーエムシー出版 食品・バイオにおける最新の酵素利用 井上國世 監修 分担執筆 第14章 (2019)

鈴木里沙、Qi Meng, 渡辺優子、人見清隆
血液凝固のメカニズムと病態について魚類を用いて解析する 
化学と生物 57, 359-365 (2019)

渡邊優子,人見清隆
生命に内在するタンパク質接着酵素をメダカで研究する 
生化学 第90巻第4号 491-494(2018)

辰川英樹、人見清隆
組織の線維化に伴い架橋される基質タンパク質群の網羅的同定・解析 
日本応用酵素協会誌 No. 52 1-10(2017)

人見清隆
トランスグルタミナーゼとポリアミン 
ポリアミン(日本ポリアミン学会) vol. 3 1号 8-13(2016)

Tatsukawa H, Furutani Y, Hitomi K, Kojima S.
Transglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and death.
Cell Death Dis. 7(6), e2244 (2016). doi: 10.1038/cddis.2016.150.

Hitomi K., Kojima S., Fesus L. Edited.
Transglutaminase: Multiple functional Modifiers and Targets for New Drug Delivery(Springer) 

人見清隆
タンパク質架橋化酵素の高反応性基質の探索と活用 
バイオサイエンスとバイオインダストリー vol. 70 11月号 6号 442-447(2012)

人見清隆
タンパク質架橋化酵素に対する高反応性基質配列の探索と活用
生化学、8月号、708-711(2009)

Sugimura Y., Kitamura M., Hosono H., Shibata, H., Maki M. and Hitomi K.
Characterization of highly reactive sequences for transglutaminase 2 and factor XIIIa.
Animal Cell technology vol. 15, 339-346 (2008)

Hitomi, K., Yamamoto, K., Nishi, K., Sugimura , Y., and MAki, M.
Immunological analysis of epidermal-type transglutaminase (TGase 3) in epithelium.
Animal Cell Technolgy vol. 14. (Iijima S. edt.) 339-345 (2006)

和田文孝、人見清隆
トランスグルタミナーゼによる低分子量Gタンパク質の機能制御
化学と生物 43、630-632(2005) 

Hitomi, K.
Transglutaminases in skin epidermis
Eur. J. Dermatol. 15, 313-319 (2005)

人見清隆
トランスグルタミナーゼによるタンパク質修飾
生化学 77, 552-558(2005)

人見清隆、和田文孝
トランスグルタミナーゼの分子進化と多様性 
化学と生物 12月号 41 782-784(2003) 

Hitomi, K.
Molecular Evolution of Transglutaminase: from bacteria to animal
Recent Research Developmemts in Biophysics and Biochemistry (Research Signpost) 3, 223-234 (2003)

Hitomi, K., Ikura, K., and Maki, M.
Characterization of recombinant transglutaminase 1 and 3 expressed in baculovirus system.
Animal Cell Technology (Editors: Shirahata S. et al.) 12, 167-172 (2002)

人見清隆
皮膚表皮に存在するカルシウム依存性タンパク質架橋酵素の発現と活性調節に関する研究
日本農芸化学会誌 第77巻 第2号 114-119(2003)

Hitomi K. and Maki M.
Expression and characterization of mouse epidermal transglutaminase in baculovirus-infected insect cells.
Animal Cell Technology (Editors: Ikura K. et al.) 295-300 (1999)

Maki M. and Hitomi K.
Purification of recombinant calpastatin in Escherichia coli.
Methods in Molecular Biology 144, 85-94 (1999) Human Press Totowa NJ.

Maki M. and Hitomi K.
Preparation of calpastatin Samples for Western blotting.
Methods in Molecular Biology 144, 95-98 (1999) Human Press Totowa NJ.

Hitomi K. and Maki M.
Expression and characterization of human calpain and calpastatin using baculovirus system.
Animal Cell Technology (Editors: Kitagawa Y. et al.) 10, 265-270 (1998)

Maki M., Narayam A.V.L., and Hitomi K.
A growing family of the calcium-binding proteins with five EF-hand motifs.
Biochem. J. 328, 718-720 (1997)

Hitomi, K. and Tsukagoshi N.
Role of Ascorbic Acid on Modulation of Gene Expression.
Subcellular Biochemistry (Plenum Publishing Co) vol. 25, 41-56 (1996)

Sasaki R., Hitomi K., Masuda S., Ueda M., and Kawanishi G.
Recombinant human erythropoietin and its receptor
Trends in animal cell culture technology, (Kodansha) 155-160 (1990)

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