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In vivo imaging of advanced glycation end products (AGEs) of albumin: first observations of significantly reduced clearance and liver deposition properties in mice.
Tsutsui, Ayumi; Ogura, Akihiro; Tahara, Tsuyoshi; Nozaki, Satoshi; Urano, Sayaka; Hara, Mitsuko; Kojima, Soichi; Kurbangalieva, Almira; Onoe, Hirotaka; Watanabe, Yasuyoshi; Taniguchi, Naoyuki; Tanaka, Katsunori.
Affiliation
  • Tsutsui A; Biofunctional Synthetic Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. kotzenori@riken.jp.
  • Ogura A; Biofunctional Synthetic Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. kotzenori@riken.jp.
  • Tahara T; RIKEN Center for Life Science Technologies, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.
  • Nozaki S; RIKEN Center for Life Science Technologies, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.
  • Urano S; Biofunctional Synthetic Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. kotzenori@riken.jp.
  • Hara M; Micro-Signaling Regulation Technology Unit, RIKEN Center for Life Science Technologies, Wako-shi, Saitama 351-0198, Japan.
  • Kojima S; Micro-Signaling Regulation Technology Unit, RIKEN Center for Life Science Technologies, Wako-shi, Saitama 351-0198, Japan.
  • Kurbangalieva A; Biofunctional Chemistry Laboratory, A. Butlerov Institute of Chemistry, Kazan Federal University, 18 Kremlyovskaya Street, Kazan 420008, Russia.
  • Onoe H; RIKEN Center for Life Science Technologies, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.
  • Watanabe Y; RIKEN Center for Life Science Technologies, 6-7-3 Minatojima-minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.
  • Taniguchi N; Disease Glycomics Team, Global Research Cluster, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
  • Tanaka K; Biofunctional Synthetic Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. kotzenori@riken.jp and Biofunctional Chemistry Laboratory, A. Butlerov Institute of Chemistry, Kazan Federal University, 18 Kremlyovskaya Street, Kazan 420008, Russia and Japan Science and Technolog
Org Biomol Chem ; 14(24): 5755-60, 2016 Jun 15.
Article in En | MEDLINE | ID: mdl-26932508
Advanced glycation end products (AGEs) are associated with various diseases, especially during aging and the development of diabetes and uremia. To better understand these biological processes, investigation of the in vivo kinetics of AGEs, i.e., analysis of trafficking and clearance properties, was carried out by molecular imaging. Following the preparation of Cy7.5-labeled AGE-albumin and intravenous injection in BALB/cA-nu/nu mice, noninvasive fluorescence kinetics analysis was performed. In vivo imaging and fluorescence microscopy analysis revealed that non-enzymatic AGEs were smoothly captured by scavenger cells in the liver, i.e., Kupffer and other sinusoidal cells, but were unable to be properly cleared from the body. Overall, these results highlight an important link between AGEs and various disorders associated with them, which may serve as a platform for future research to better understand the processes and mechanisms of these disorders.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glycation End Products, Advanced / Albumins / Molecular Imaging / Liver Limits: Animals Language: En Journal: Org Biomol Chem Journal subject: BIOQUIMICA / QUIMICA Year: 2016 Document type: Article Affiliation country: Japan Country of publication: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glycation End Products, Advanced / Albumins / Molecular Imaging / Liver Limits: Animals Language: En Journal: Org Biomol Chem Journal subject: BIOQUIMICA / QUIMICA Year: 2016 Document type: Article Affiliation country: Japan Country of publication: United kingdom