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- W2791520301 abstract "Coagulation factor XIII (FXIII) is a precursor of the active transglutaminase (FXIIIa) that catalyzes covalent cross-linking within polymeric fibrin to increase mechanical and proteolytic stability of blood clots and thrombi. Inactive FXIII is a heterotetramer (A2B2) with two catalytic A-subunits and two inhibitory B-subunits, which are dissociated upon thrombin-induced conversion of FXIII to the enzymatically active dimeric (A2) form FXIIIa. FXIII-A2 has been characterized crystallographically, while the atomic structures of the FXIII-A2B2 complex and B-subunits remain unknown. Our goal was to visualize and characterize the molecular structure of FXIII-A2B2, FXIIIa-A2, and individual B-subunits using high-resolution atomic force microscopy (AFM). Commercially available FXIII and FXIIIa (Enzyme Research Laboratories, USA) were adsorbed on the surface of freshly cleaved graphite rendered hydrophilic with an amphiphilic hydrocarbon-glycine modifier followed by high-resolution single-molecule AFM imaging in air. FXIII was visualized as a globule with two filamentous extensions, while in FXIIIa the protruded elongated portions were separated from the globule, suggesting that the globular structure represented a compact A2-dimer and the extensions comprised individual B-subunits. The contour length of the B-subunits increased from 21±6 nm in FXIII to 36±6 nm in FXIIIa after their dissociation from the globular part of the protein, implying that ∼40% of each B-subunit was invisible due to tight association with the globular A2-dimer. These observations strongly suggest that two B subunits are partially wrapped around the A-subunits, probably through their N-terminal portions. The dimensions (height) of the globular part decreased upon activation from 3.5±0.6 nm in FXIII to 2.6±0.6 nm in FXIIIa as a result of B-subunits separation and conformational changes in FXIII-A2. These results provide molecular structural characteristics of FXIII and FXIIIa molecules as well as individual A and B subunits and their interactions within FXIII." @default.
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- W2791520301 date "2018-02-01" @default.
- W2791520301 modified "2023-09-25" @default.
- W2791520301 title "Single-Molecule Atomic Force Microscopy of Blood Coagulation Factor XIII and its Subunits" @default.
- W2791520301 doi "https://doi.org/10.1016/j.bpj.2017.11.3114" @default.
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