Article
Mild acidity likely accelerates the physiological matriptase autoactivation process: a comparative study between spontaneous and acid-induced matriptase zymogen activation.
Human cell - 1 Oct 2020
Jia Bailing, Thompson Hamishi A, Barndt Robert B, Chiu Yi-Lin, Lee Mon-Juan, Lee See-Chi, Wang Jehng-Kang, Tang Hung-Jen, Lin Chen-Yong, Johnson Michael D
Abstract excerpt
The pathophysiological functions of matriptase, a type 2 transmembrane serine protease, rely primarily on its enzymatic activity, which is under tight control through multiple mechanisms. Among those regulatory mechanisms, the control of zymogen activation is arguably the most important. Matriptase zymogen activation not only generates the mature active enzyme but also initiates suppressive mechanisms, such as...
Topics
- Acids
- Enzyme Activation
- Enzyme Precursors
- Humans
- Mutation
- Protein Domains
- Protein Processing, Post-Translational
- Proteinase Inhibitory Proteins, Secretory
- Serine Endopeptidases