Masaaki Sato
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Masaaki Sato has a total of 29 co-authors. Here are the top co-authors by number of shared publications:
- Kazuki Omoteyama
Clinical Proteomics and Molecular Medicine, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae, Kawasaki, Kanagawa, 216-8511, Japan
5 shared publications - Manae Suzuki Kurokawa
Clinical Proteomics and Molecular Medicine, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae, Kawasaki, Kanagawa, 216-8511, Japan
5 shared publications - Mitsumi Arito
Clinical Proteomics and Molecular Medicine, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae, Kawasaki, Kanagawa, 216-8511, Japan
5 shared publications - Tomohiro Kato
Department of Rheumatology and Allergology, St. Marianna University School of Medicine, 2-16-1, Sugao, Miyamae, Kawasaki, Kanagawa, 216-8511, Japan
5 shared publications - Atsuhiro Tsutiya
Clinical Proteomics and Molecular Medicine, St. Marianna University Graduate School of Medicine, 2-16-1 Sugao, Miyamae, Kawasaki 216-8511, Kanagawa, Japan
4 shared publications - Naoya Suematsu
Department of Biochemistry, St. Marianna University School of Medicine, Kanagawa, Japan
4 shared publications
Latest Publications
- 6 August 2025
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 779, 152458
Proximity-dependent biotin identification (BioID) screening identified novel layilin-proximal proteins
- 6 August 2025
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 779, 152458
Proximity-dependent biotin identification (BioID) screening identified novel layilin-proximal proteins
- 22 February 2025
- Published by Elsevier in Journal of Proteomics
- Vol. 315, 105412
Aberrant oxidative modifications of neutrophil myeloperoxidase in anti-neutrophil cytoplasmic antibody-associated vasculitis
- 22 February 2025
- Published by Elsevier in Journal of Proteomics
- Vol. 315, 105412
Aberrant oxidative modifications of neutrophil myeloperoxidase in anti-neutrophil cytoplasmic antibody-associated vasculitis
- 1 April 2021
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 549, 143-149
Layilin promotes mitochondrial fission by cyclin-dependent kinase 1 and dynamin-related protein 1 activation in HEK293T cells
- 1 April 2021
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 549, 143-149
Layilin promotes mitochondrial fission by cyclin-dependent kinase 1 and dynamin-related protein 1 activation in HEK293T cells
- 1 September 2019
- Published by Elsevier in Brain Research
- Vol. 1719, 140-147
Layilin enhances the invasive ability of malignant glioma cells via SNAI1 signaling
- 1 September 2019
- Published by Elsevier in Brain Research
- Vol. 1719, 140-147
Layilin enhances the invasive ability of malignant glioma cells via SNAI1 signaling
- Open Access
- 27 November 2018
- Published by Springer Nature in BMC Rheumatology
- Vol. 2 (1) , 35
A proteomic analysis of serum-derived exosomes in rheumatoid arthritis
To understand the roles of serum exosomes in rheumatoid arthritis (RA), we comprehensively investigated the protein profiles of serum exosomes in patients with RA. Exosomes were isolated from serum samples obtained from 33 patients (12 with active RA [aRA], 11 with inactive RA [iRA], 10 with osteoarthritis [OA]) and 10 healthy donors (HLs). Proteins extracted from the exosomes were separated by two-dimensional differential gel electrophoresis (2D-DIGE) and identified by mass spectrometry. In total, 204 protein spots were detected by 2D-DIGE. In the aRA, iRA, and OA groups, 24, 5, and 7 spots showed approximately ≥ ±1.3-fold intensity differences compared with the HL group, respectively. We were able to identify proteins in six protein spots. Among them, the protein spot identified as Toll-like receptor 3 (TLR3) showed approximately 6-fold higher intensity in the aRA group than in the other groups. Patients with active RA possessed considerably different protein profiles of serum exosomes from patients with iRA, patients with OA, and healthy donors. The unique protein profile of serum exosomes, such as the possession of abundant TLR3 fragments, may reflect the pathophysiology of active RA.
- 27 November 2018
- Published by Springer Nature in BMC Rheumatology
- Vol. 2 (1) , 35
Open AccessA proteomic analysis of serum-derived exosomes in rheumatoid arthritis
To understand the roles of serum exosomes in rheumatoid arthritis (RA), we comprehensively investigated the protein profiles of serum exosomes in patients with RA. Exosomes were isolated from serum samples obtained from 33 patients (12 with active RA [aRA], 11 with inactive RA [iRA], 10 with osteoarthritis [OA]) and 10 healthy donors (HLs). Proteins extracted from the exosomes were separated by two-dimensional differential gel electrophoresis (2D-DIGE) and identified by mass spectrometry. In total, 204 protein spots were detected by 2D-DIGE. In the aRA, iRA, and OA groups, 24, 5, and 7 spots showed approximately ≥ ±1.3-fold intensity differences compared with the HL group, respectively. We were able to identify proteins in six protein spots. Among them, the protein spot identified as Toll-like receptor 3 (TLR3) showed approximately 6-fold higher intensity in the aRA group than in the other groups. Patients with active RA possessed considerably different protein profiles of serum exosomes from patients with iRA, patients with OA, and healthy donors. The unique protein profile of serum exosomes, such as the possession of abundant TLR3 fragments, may reflect the pathophysiology of active RA.