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Your search keyword '"Kitaura, Jiro"' showing total 12 results
Start Over Author "Kitaura, Jiro" Journal journal of biological chemistry
12 results on '"Kitaura, Jiro"'

1. Receptor-destroying enzyme (RDE) from Vibrio cholerae modulates IgE activity and reduces the initiation of anaphylaxis

Author

Yamazaki, Tatsuya, primary, Inui, Masanori, additional, Hiemori, Keiko, additional, Tomono, Susumu, additional, Itoh, Makoto, additional, Ichimonji, Isao, additional, Nakashima, Akina, additional, Takagi, Hidekazu, additional, Biswas, Mrityunjoy, additional, Izawa, Kumi, additional, Kitaura, Jiro, additional, Imai, Teruko, additional, Sugiura, Nobuo, additional, Tateno, Hiroaki, additional, and Akashi-Takamura, Sachiko, additional

Published
2019
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2. The CD300e molecule in mice is an immune-activating receptor

Author

Isobe, Masamichi, primary, Izawa, Kumi, additional, Sugiuchi, Masahiro, additional, Sakanishi, Tamami, additional, Kaitani, Ayako, additional, Takamori, Ayako, additional, Maehara, Akie, additional, Matsukawa, Toshihiro, additional, Takahashi, Mariko, additional, Yamanishi, Yoshinori, additional, Oki, Toshihiko, additional, Uchida, Shino, additional, Uchida, Koichiro, additional, Ando, Tomoaki, additional, Maeda, Keiko, additional, Nakano, Nobuhiro, additional, Yagita, Hideo, additional, Takai, Toshiyuki, additional, Ogawa, Hideoki, additional, Okumura, Ko, additional, Kitamura, Toshio, additional, and Kitaura, Jiro, additional

Published
2018
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3. Ceramide-CD300f Binding Inhibits Lipopolysaccharide-induced Skin Inflammation

Author

Shiba, Emiko, primary, Izawa, Kumi, additional, Kaitani, Ayako, additional, Isobe, Masamichi, additional, Maehara, Akie, additional, Uchida, Koichiro, additional, Maeda, Keiko, additional, Nakano, Nobuhiro, additional, Ogawa, Hideoki, additional, Okumura, Ko, additional, Kitamura, Toshio, additional, Shimizu, Toshiaki, additional, and Kitaura, Jiro, additional

Published
2017
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4. Human CD300C Delivers an Fc Receptor-γ-dependent Activating Signal in Mast Cells and Monocytes and Differs from CD300A in Ligand Recognition

Author

Takahashi, Mariko, primary, Izawa, Kumi, additional, Kashiwakura, Jun-ichi, additional, Yamanishi, Yoshinori, additional, Enomoto, Yutaka, additional, Kaitani, Ayako, additional, Maehara, Akie, additional, Isobe, Masamichi, additional, Ito, Shinichi, additional, Matsukawa, Toshihiro, additional, Nakahara, Fumio, additional, Oki, Toshihiko, additional, Kajikawa, Masunori, additional, Ra, Chisei, additional, Okayama, Yoshimichi, additional, Kitamura, Toshio, additional, and Kitaura, Jiro, additional

Published
2013
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5. Characterization of Leukocyte Mono-immunoglobulin-like Receptor 7 (LMIR7)/CLM-3 as an Activating Receptor

Author

Enomoto, Yutaka, primary, Yamanishi, Yoshinori, additional, Izawa, Kumi, additional, Kaitani, Ayako, additional, Takahashi, Mariko, additional, Maehara, Akie, additional, Oki, Toshihiko, additional, Takamatsu, Reiko, additional, Kajikawa, Masunori, additional, Takai, Toshiyuki, additional, Kitamura, Toshio, additional, and Kitaura, Jiro, additional

Published
2010
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7. Functional Analysis of Activating Receptor LMIR4 as a Counterpart of Inhibitory Receptor LMIR3

Author

Izawa, Kumi, primary, Kitaura, Jiro, additional, Yamanishi, Yoshinori, additional, Matsuoka, Takayuki, additional, Oki, Toshihiko, additional, Shibata, Fumi, additional, Kumagai, Hidetoshi, additional, Nakajima, Hideaki, additional, Maeda-Yamamoto, Mari, additional, Hauchins, Jeffrey P., additional, Tybulewicz, Victor L.J., additional, Takai, Toshiyuki, additional, and Kitamura, Toshio, additional

Published
2007
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11. Evidence That Integrin αllbβ3-dependent Interaction of Mast Cells with Fibrinogen Exacerbates Chronic lnflammation.

Author

Oki, Toshihiko, Eto, Koji, lzawa, Kumi, Yamanishi, Yoshinori, Inagaki, Naoki, Frampton, Jon, Kitamura, Toshio, and Kitaura, Jiro

Subjects
*MAST cells, *INTEGRINS, *MEGAKARYOCYTES, *BONE marrow cells, *CELL proliferation, *CYTOKINES, *IMMUNE response, *STAPHYLOCOCCUS aureus
Abstract

Integrin αIIbβ3 is expressed in mast cells as well as in megakaryocytes/platelets. A recent study has shown that surface expression levels of integrin αVβ3 are elevated in integrin αIIb-deficient bone marrow-derived mast cells (BMMCs) as compared with wild-type (WT) counterparts, but the underlying mechanism remains obscure. Here we demonstrate by transducing integrin αllb into integrin αIIb-deficient BMMCs that surface expression levels of integrin αVβ3 are inversely related to those of integrin αIIbβ3. Thus, competitive association of integrin β3 with integrin αllb or integrin αV determines surface expression levels of integrin αIIbβ3 or αVβ3 in mast cells. We compared WT and integrin αlIb-deficient BMMCs as well as integrin αlIb-deficient BMMCs transduced with integrin αIIb(WT) or non-functional αlIb(D163A) mutant and found that enhancement of proliferation, degranulation, cytokine production, and migration of BMMCs through interaction with fibrinogen (FB) depended on integrin αIIbβ3. In addition, elevated surface expression of integrin αVβ3 failed to compensate for loss of FB-associated functions in integrin αIIb-deficient BMMCs while enhancing adhesion to vitronectin or von Willebrand factor. Importantly, integrin αlIb deficiency strongly suppressed chronic inflammation with the remarkable increase of mast cells induced by continuous intraperitoneal administration of FB, although it did not affect acute allergic responses or mast cell numbers in tissues in steady states. Interestingly, soluble FB promoted cytokine production of BMMCs in response to Staphylococcus aureus with FB-binding capacity, through integrin αIIbβ3-dependent recognition of this pathogen. Collectively, integrin αIIbβ3 in mast cells plays an important part in FB-associated, chronic inflammation and innate immune responses. [ABSTRACT FROM AUTHOR]

Published
2009
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12. Protein kinase C betaII regulates Akt phosphorylation on Ser-473 in a cell type- and stimulus-specific fashion.

Author

Kawakami Y, Nishimoto H, Kitaura J, Maeda-Yamamoto M, Kato RM, Littman DR, Leitges M, Rawlings DJ, and Kawakami T

Subjects
Animals, Bone Marrow Cells cytology, Bone Marrow Cells physiology, Cells, Cultured, Enzyme Activation, Immunoglobulin E pharmacology, Interleukin-2 metabolism, Isoenzymes genetics, Mast Cells cytology, Mast Cells drug effects, Mast Cells physiology, Mice, Mice, Knockout, Phorbol Esters pharmacology, Phosphorylation, Protein Kinase C genetics, Protein Kinase C beta, Protein Serine-Threonine Kinases genetics, Proto-Oncogene Proteins genetics, Proto-Oncogene Proteins c-akt, Receptors, IgE metabolism, Isoenzymes metabolism, Protein Kinase C metabolism, Protein Serine-Threonine Kinases metabolism, Proto-Oncogene Proteins metabolism, Serine metabolism
Abstract

Akt (= protein kinase B), a subfamily of the AGC serine/threonine kinases, plays critical roles in survival, proliferation, glucose metabolism, and other cellular functions. Akt activation requires the recruitment of the enzyme to the plasma membrane by interacting with membrane-bound lipid products of phosphatidylinositol 3-kinase. Membrane-bound Akt is then phosphorylated at two sites for its full activation; Thr-308 in the activation loop of the kinase domain is phosphorylated by 3-phosphoinositide-dependent kinase-1 (PDK1) and Ser-473 in the C-terminal hydrophobic motif by a putative kinase PDK2. The identity of PDK2 has been elusive. Here we present evidence that conventional isoforms of protein kinase C (PKC), particularly PKCbetaII, can regulate Akt activity by directly phosphorylating Ser-473 in vitro and in IgE/antigen-stimulated mast cells. By contrast, PKCbeta is not required for Ser-473 phosphorylation in mast cells stimulated with stem cell factor or interleukin-3, in serum-stimulated fibroblasts, or in antigen receptor-stimulated T or B lymphocytes. Therefore, PKCbetaII appears to work as a cell type- and stimulus-specific PDK2.

Published
2004
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