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Predictive factors for hyperglycaemic progression in patients with schizophrenia or bipolar disorder
- Ichiro Kusumi, Yuki Arai, Ryo Okubo, Minoru Honda, Yasuhiro Matsuda, Yukihiko Matsuda, Akihiko Tochigi, Yoshiteru Takekita, Hiroyoshi Yamanaka, Keiichi Uemura, Koichi Ito, Kiyoshi Tsuchiya, Jun Yamada, Bunta Yoshimura, Nobuyuki Mitsui, Sigehiro Matsubara, Takayuki Segawa, Nobuyuki Nishi, Yasufumi Sugawara, Yuki Kako, Ikuta Shinkawa, Kaoru Shinohara, Akiko Konishi, Junichi Iga, Naoki Hashimoto, Shinsaku Inomata, Noriko Tsukamoto, Hiroto Ito, Yoichi M. Ito, Norihiro Sato
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- Journal:
- BJPsych Open / Volume 4 / Issue 6 / November 2018
- Published online by Cambridge University Press:
- 30 October 2018, pp. 454-460
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Background
Patients with schizophrenia or bipolar disorder have a high risk of developing type 2 diabetes.
AimsTo identify predictive factors for hyperglycaemic progression in individuals with schizophrenia or bipolar disorder and to determine whether hyperglycaemic progression rates differ among antipsychotics in regular clinical practice.
MethodWe recruited 1166 patients who initially had normal or prediabetic glucose levels for a nationwide, multisite, l-year prospective cohort study to determine predictive factors for hyperglycaemic progression. We also examined whether hyperglycaemic progression varied among patients receiving monotherapy with the six most frequently used antipsychotics.
ResultsHigh baseline serum triglycerides and coexisting hypertension significantly predicted hyperglycaemic progression. The six most frequently used antipsychotics did not significantly differ in their associated hyperglycaemic progression rates over the 1-year observation period.
ConclusionsClinicians should carefully evaluate baseline serum triglycerides and coexisting hypertension and perform strict longitudinal monitoring irrespective of the antipsychotic used.
Declaration of interestThe authors report no financial or other relationship that is relevant to the subject of this article. Relevant financial activities outside the submitted work are as follows. I.K. has received honoraria from Astellas, Chugai Pharmaceutical, Daiichi Sankyo, Dainippon Sumitomo Pharma, Eisai, Eli Lilly, Janssen Pharmaceutical, Kyowa Hakko Kirin, Meiji Seika Pharma, MSD, Nippon Chemiphar, Novartis Pharma, Ono Pharmaceutical, Otsuka Pharmaceutical, Pfizer, Tanabe Mitsubishi Pharma, Shionogi and Yoshitomiyakuhin; has received research/grant support from AbbVie GK, Asahi Kasei Pharma, Astellas, Boehringer Ingelheim, Chugai Pharmaceutical, Daiichi Sankyo, Dainippon Sumitomo Pharma, Eisai, Eli Lilly, GlaxoSmithKline, Kyowa Hakko Kirin, Meiji Seika Pharma, MSD, Novartis Pharma, Ono Pharmaceutical, Otsuka Pharmaceutical, Pfizer, Takeda Pharmaceutical, Tanabe Mitsubishi Pharma, Shionogi and Yoshitomiyakuhin; and is a member of the advisory boards of Dainippon Sumitomo Pharma and Tanabe Mitsubishi Pharma. Y.T. has received speaker's honoraria from Dainippon-Sumitomo Pharma, Otsuka, Meiji-Seika Pharma, Janssen Pharmaceutical, Daiichi-Sankyo Company, UCB Japan and Ono Pharmaceutical. K.U. has received honoraria from Dainippon Sumitomo Pharma, Eisai, Eli Lilly, Janssen Pharmaceutical, Kyowa Hakko Kirin, Meiji Seika Pharma, MSD, Takeda Pharmaceutical, Hisamitsu Pharmaceutical, Otsuka Pharmaceutical, Pfizer, Tanabe Mitsubishi Pharma, Shionogi and Yoshitomiyakuhin. B.Y. has received speaker's honoraria from Otsuka Pharmaceutical and Janssen Pharmaceutical. J. I. has received honoraria from Dainippon Sumitomo Pharma, Eli Lilly, Janssen Pharmaceutical, Meiji Seika Pharma, MSD, Novartis Pharma, Otsuka Pharmaceutical and Mochida Pharma.
Protein histidine phosphorylation: Increased stability of thiophosphohistidine
- MICHAEL LASKER, CUONG D. BUI, PAUL G. BESANT, KIYOSHI SUGAWARA, PHILIP THAI, GERGELY MEDZIHRADSZKY, CHRISTOPH W. TURCK
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- Journal:
- Protein Science / Volume 8 / Issue 10 / October 1999
- Published online by Cambridge University Press:
- 01 October 1999, pp. 2177-2185
- Print publication:
- October 1999
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Posttranslational phosphorylation of proteins is an important event in many cellular processes. Whereas phosphoesters of serine, threonine and tyrosine have been extensively studied, only limited information is available for other amino acids modified by a phosphate group. The formation of phosphohistidine residues in proteins has been discovered in prokaryotic organisms as well as in eukaryotic cells. The ability to biochemically analyze phosphohistidine residues in proteins, however, is severely hampered by its extreme lability under acidic conditions. In our studies we have found that by replacing the phosphate linked to the histidine residue with a thiophosphate, a phosphohistidine derivative with increased stability is formed. This allows the analysis of phosphohistidine-containing proteins by established biochemical techniques and will greatly aid in the investigation of the role of this posttranslational modification in cellular processes.