Chihao Zhang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Chihao Zhang has a total of 14 co-authors. Here are the top co-authors by number of shared publications:
- Changming Chen
Department of Laboratory Medicine, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publication Guoming Li
Department of Biochemistry and Molecular Cell Biology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publicationHaojie Jiang
Department of Biochemistry and Molecular Cell Biology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publication- Jing Dai
Department of Laboratory Medicine, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publication Junling Liu
Department of Biochemistry and Molecular Cell Biology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publicationKe Zhang
Department of Laboratory Medicine, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
1 shared publication
Latest Publications
- Open Access
- 13 October 2026
- Published by Springer Nature in EMBO Reports
- p. 1-24
G6PD suppresses thrombopoiesis via interfering with TMOD3-mediated actin dynamics
Glucose-6-phosphate dehydrogenase (G6PD), the committed enzyme of the pentose phosphate pathway, plays a pivotal role in glucose metabolism, which is integral to platelet biology. Although G6PD deficiency is a prevalent enzyme defect worldwide, the specific role of G6PD itself in platelets remains unclear. Herein, we discover a previously unrecognized phenotype in both human patients and murine models, demonstrating that G6PD deficiency leads to elevated platelet counts through enhanced proplatelet formation (PPF). Mechanistically, we reveal a non-canonical function of G6PD in regulating actin dynamics via its interaction with an actin-binding protein, tropomodulin-3 (TMOD3). The G6PD-TMOD3 interaction, which is concentration-dependently enhanced by nicotinamide adenine dinucleotide phosphate (NADP + ), can limit actin rearrangement, thereby inhibiting PPF. Furthermore, we develop a G6PD-derived peptide, GC2P2, which potentiates the G6PD-TMOD3 interaction and significantly suppresses thrombocytopoiesis both in vitro and in vivo. In conclusion, our findings suggest that G6PD deficiency facilitates platelet biogenesis by altering TMOD3-mediated actin dynamics. The study provides new insights into thrombopoiesis and offers potential strategies for modulating platelet production.
- 13 October 2026
- Published by Springer Nature in EMBO Reports
- p. 1-24
Open AccessG6PD suppresses thrombopoiesis via interfering with TMOD3-mediated actin dynamics
Glucose-6-phosphate dehydrogenase (G6PD), the committed enzyme of the pentose phosphate pathway, plays a pivotal role in glucose metabolism, which is integral to platelet biology. Although G6PD deficiency is a prevalent enzyme defect worldwide, the specific role of G6PD itself in platelets remains unclear. Herein, we discover a previously unrecognized phenotype in both human patients and murine models, demonstrating that G6PD deficiency leads to elevated platelet counts through enhanced proplatelet formation (PPF). Mechanistically, we reveal a non-canonical function of G6PD in regulating actin dynamics via its interaction with an actin-binding protein, tropomodulin-3 (TMOD3). The G6PD-TMOD3 interaction, which is concentration-dependently enhanced by nicotinamide adenine dinucleotide phosphate (NADP + ), can limit actin rearrangement, thereby inhibiting PPF. Furthermore, we develop a G6PD-derived peptide, GC2P2, which potentiates the G6PD-TMOD3 interaction and significantly suppresses thrombocytopoiesis both in vitro and in vivo. In conclusion, our findings suggest that G6PD deficiency facilitates platelet biogenesis by altering TMOD3-mediated actin dynamics. The study provides new insights into thrombopoiesis and offers potential strategies for modulating platelet production.