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Postoperative pulmonary complications are a common cause of postoperative morbidity in patients undergoing hepatectomy. This study aimed to identify risk factors, define severity, and evaluate the impact of postoperative pulmonary complications on postoperative morbidity after hepatectomy.We used a prospective database in identifying all hepatectomies from 2013 to 2018. The database was then augmented using extensive review of medical records. The Strasburg system was used in categorizing resections per complexity: major hepatic resection and minor hepatic resection, whereas the Clavien-Dindo system was used in defining postoperative pulmonary complications per severity. Potential confounders were controlled for on multiple regression models.A total of 702 cases were identified: major hepatic resection 413 (60%) and minor hepatic resection 289 (40%). Patients demonstrated comparable characteristics, but the postoperative pulmonary complications group was more likely to have chronic obstructive pulmonary disease (10% vs 5%; P = .02). Severe postoperative pulmonary complications among major hepatectomy was observed in 38 patients (13%). Predictors for severe postoperative pulmonary complications requiring intervention included postoperative liver failure (odds ratio = 2.8; P = .002) and biliary fistula (odds ratio = 3.5; P = .001). In addition, the occurrence of severe postoperative pulmonary complications markedly hindered recovery, increasing length of stay by 4.4-fold and readmission rates by 3-fold (P.001). On multivariable analysis, postoperative pulmonary complications significantly increase postoperative length of stay (8 vs 5 days; P.001) and readmission (odds ratio = 3.2; P = .001). Mortality was similar (1% vs 4%; P = .066).Postoperative pulmonary complications are a major cause of delayed recovery and worse outcomes after hepatectomy. Further, postoperative liver failure and biliary fistula can predict the occurrence of severe postoperative pulmonary complications among major hepatic resection and the associated need for readmission with these complications.

Aggregation is a characteristic of extensively oxidized (ox-) LDL. We wished to determine whether this structural change contributed even more to the documented poor degradation in macrophages of ox-LDL than the chemical changes. When protein degradation of the soluble and insoluble portions of extensively ox-LDL was compared to that of acetyl LDL in mouse peritoneal macrophages (MPM), we found that the percent of internalized LDL that was degraded was lowest for the insoluble portion (insol. ox-LDL), intermediate for the soluble portion (sol. ox-LDL), and highest for the acetyl LDL, regardless of whether the binding and uptake mechanisms had been excluded, e.g., by performing appropriate pulse-chase studies. As the same order of degradation was found after long-term degradation under cell-free conditions by a mixture of cathepsin B and D, it is likely that poor degradation of ox-LDL by lysosomal proteases is partially responsible for the deficient processing of ox-LDL in MPM. However, when MPM were incubated in a pulse-chase design with LDL that was induced to aggregate by vortexing without oxidizing (vx-LDL), degradation over an 18-h interval of accumulated vx-LDL was almost as low (25%) as that of insol. ox-LDL (18%), in contrast to sol. ox-LDL (60%). Yet, in a cell-free system cathepsin degradation of vx-LDL was as efficient as that of acetyl LDL and LDL. Also, the differences in degradation between sol. and insol. ox-LDL were smaller than in MPM. Thus, it appears that alternative mechanisms to poor proteolysis of substrate were responsible for poor intracellular processing of such aggregated lipoproteins. These results suggest that, although the poorer processing of insol. ox-LDL than sol. ox-LDL may be due, in part, to more deficient proteolytic degradation, particle aggregation per se may play at least as important a role in such deficiencies. This may occur by such mechanisms as altered intracellular trafficking leading to poorer fusion in macrophages of phagosomes containing aggregated lipoproteins with lysosomes.