Jack D. A. Sharpen
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Jack D. A. Sharpen has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Beatriz Martinez-Abad
Department of Medical Biochemistry, University of Gothenburg, Gothenburg, Sweden
2 shared publications - Christian V. Recktenwald
Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden
2 shared publications - George M. H. Birchenough
Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden
2 shared publications - Gunnar C. Hansson
University of Gothenburg
2 shared publications - Malin E. V. Johansson
Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden
2 shared publications Brendan Dolan
University of Gothenburg
1 shared publication
Latest Publications
- Open Access
- 11 January 2022
- Published by Springer Nature in Nature Communications
- Vol. 13 (1) , 1-12
Transglutaminase 3 crosslinks the secreted gel-forming mucus component Mucin-2 and stabilizes the colonic mucus layer
The colonic mucus layer is organized as a two-layered system providing a physical barrier against pathogens and simultaneously harboring the commensal flora. The factors contributing to the organization of this gel network are not well understood. In this study, the impact of transglutaminase activity on this architecture was analyzed. Here, we show that transglutaminase TGM3 is the major transglutaminase-isoform expressed and synthesized in the colon. Furthermore, intrinsic extracellular transglutaminase activity in the secreted mucus was demonstrated in vitro and ex vivo. Absence of this acyl-transferase activity resulted in faster degradation of the major mucus component the MUC2 mucin and changed the biochemical properties of mucus. Finally, TGM3-deficient mice showed an early increased susceptibility to Dextran Sodium Sulfate-induced colitis. Here, we report that natural isopeptide cross-linking by TGM3 is important for mucus homeostasis and protection of the colon from inflammation, reducing the risk of colitis.
- 11 January 2022
- Published by Springer Nature in Nature Communications
- Vol. 13 (1) , 1-12
Open AccessTransglutaminase 3 crosslinks the secreted gel-forming mucus component Mucin-2 and stabilizes the colonic mucus layer
The colonic mucus layer is organized as a two-layered system providing a physical barrier against pathogens and simultaneously harboring the commensal flora. The factors contributing to the organization of this gel network are not well understood. In this study, the impact of transglutaminase activity on this architecture was analyzed. Here, we show that transglutaminase TGM3 is the major transglutaminase-isoform expressed and synthesized in the colon. Furthermore, intrinsic extracellular transglutaminase activity in the secreted mucus was demonstrated in vitro and ex vivo. Absence of this acyl-transferase activity resulted in faster degradation of the major mucus component the MUC2 mucin and changed the biochemical properties of mucus. Finally, TGM3-deficient mice showed an early increased susceptibility to Dextran Sodium Sulfate-induced colitis. Here, we report that natural isopeptide cross-linking by TGM3 is important for mucus homeostasis and protection of the colon from inflammation, reducing the risk of colitis.
- Open Access
- 21 June 2021
- Published by Springer Nature in Research Square
Transglutaminase 3 crosslinks secreted MUC2 and stabilizes the colonic mucus layer
The colonic mucus layer is organized as a two-layered system providing a physical barrier against pathogens and simultaneously harboring the commensal flora. The factors contributing to the organization of this gel network are not well understood. In this study, the impact of transglutaminase activity on this architecture was analyzed. Here, we show that transglutaminase TGM3 is the major TGM isoform expressed and synthesized in the colon. Furthermore, intrinsic extracellular TGM activity in the secreted mucus was demonstrated in vitro and ex vivo. Absence of this acyl-transferase activity resulted in faster degradation of the major mucus component the MUC2 mucin and changed the biochemical properties of mucus. Finally, TGM3-deficient mice showed an early increased susceptibility to DSS-induced colitis. Thus, these observations suggest that natural isopeptide cross-linking by TGM3 is important for mucus homeostasis and protection of the colon from inflammation, a suggested pre-stage of colon carcinoma.
- 21 June 2021
- Published by Springer Nature in Research Square
Open AccessTransglutaminase 3 crosslinks secreted MUC2 and stabilizes the colonic mucus layer
The colonic mucus layer is organized as a two-layered system providing a physical barrier against pathogens and simultaneously harboring the commensal flora. The factors contributing to the organization of this gel network are not well understood. In this study, the impact of transglutaminase activity on this architecture was analyzed. Here, we show that transglutaminase TGM3 is the major TGM isoform expressed and synthesized in the colon. Furthermore, intrinsic extracellular TGM activity in the secreted mucus was demonstrated in vitro and ex vivo. Absence of this acyl-transferase activity resulted in faster degradation of the major mucus component the MUC2 mucin and changed the biochemical properties of mucus. Finally, TGM3-deficient mice showed an early increased susceptibility to DSS-induced colitis. Thus, these observations suggest that natural isopeptide cross-linking by TGM3 is important for mucus homeostasis and protection of the colon from inflammation, a suggested pre-stage of colon carcinoma.