Volar plate fixation of AO type C2 and C3 distal radius fractures, a single-center study of 55 patients.

OBJECTIVES: We hypothesized that volar locked plate fixation of AO type C2 or C3 fractures could effectively maintain radiographic reduction as shown by comparison of immediate postoperative alignment and that seen after more than 12 months' follow-up. DESIGN: Prospective cohort study. SETTING: Level II trauma center located in a suburban area. PATIENTS: Fifty-five adult patients with intra-articular fractures of the distal radius. INTERVENTION: Open reduction and internal fixation with a locked volar plate and screws. MAIN OUTCOME MEASUREMENTS: Volar tilt, radial inclination, radial length, and articular incongruity were radiologically assessed immediately postoperatively and at the time of final follow-up (mean follow-up: 29 +/- 7 months). RESULTS: At final radiographic examination, the average loss of volar tilt was 1.9 +/- 3.3 degrees (P < 0.001) and the average loss of radial inclination was 1.4 +/- 2.8 degrees (P < 0.001). Four patients had more than 5 degrees loss of radial inclination (7.8%), and 22 patients (43.1%) had more than 5 degrees loss of volar tilt. Radial shortening was not statistically significant (P > 0.05). CONCLUSIONS: The treatment of intra-articular fractures of the distal radius with a volar locked plating system is associated with a small but statistically significant loss of volar tilt and radial inclination upon comparison of immediate postoperative alignment with that seen after more than 12 months' follow-up.

SARS-CoV-2 Entry Protein TMPRSS2 and Its Homologue, TMPRSS4 Adopts Structural Fold Similar to Blood Coagulation and Complement Pathway Related Proteins

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) utilizes TMPRSS2 receptor to enter target human cells and subsequently causes coronavirus disease 19 (COVID-19). TMPRSS2 belongs to the type II serine proteases of subfamily TMPRSS, which is characterized by the presence of the serine-protease domain. TMPRSS4 is another TMPRSS member, which has a domain architecture similar to TMPRSS2. TMPRSS2 and TMPRSS4 have been shown to be involved in SARS-CoV-2 infection. However, their normal physiological roles have not been explored in detail. In this study, we analyzed the amino acid sequences and predicted 3D structures of TMPRSS2 and TMPRSS4 to understand their functional aspects at the protein domain level. Our results suggest that these proteins are likely to have common functions based on their conserved domain organization. Furthermore, we show that the predicted 3D structure of their serine protease domain has significant similarity to that of plasminogen which dissolves blood clot, and of other blood coagulation related proteins. Additionally, molecular docking analyses of inhibitors of four blood coagulation and anticoagulation factors show the same high specificity to TMPRSS2 and TMPRSS4 3D structures. Hence, our observations are consistent with the blood coagulopathy observed in COVID-19 patients and their predicted functions based on the sequence and structural analyses offer avenues to understand better and explore therapeutic approaches for this disease.