Depression increases the length of hospitalization for patients undergoing thoracic surgery: a preliminary study.

OBJECTIVE: Surgical treatment, especially thoracic surgery, is a burdensome prospect for many patients. Depression-related anxiety, insomnia, and stress are common complaints in preoperative patients. Such depressive complaints are currently thought to affect the patients' physiological status. We examined the effect of mental status on the length of hospitalization following thoracic surgery. METHODS: The study population was comprised of 52 patients (lung cancer 88%) who underwent operative treatment for thoracic disease. Patient depressive status was evaluated using the Self-Rating Depression Scale (SDS) at admission and again at discharge. Demographic data were collected retrospectively and included age, thoracotomy, and number of days in the hospital. RESULTS: SDS scores did not differ between admission and discharge (37.7 ± 9.9 vs. 40.4 ± 8.9, respectively; ns). The length of hospitalization in patients with depression (SDS score > 40) was significantly greater than for those without depression (P < 0.05). The length of hospitalization significantly correlated with the SDS score at admission (r = 0.492, P < 0.001). Multiple regression analyses revealed that the length of hospitalization correlated with the SDS score at admission (P < 0.01) and with endoscopic surgery (P < 0.05). CONCLUSION: This study suggests that depression increases the length of hospitalization for malignancy patients undergoing thoracic surgery; early intervention or treatment for depression may be required for these patients to improve outcomes.

Compensatory binding of an asparagine residue to the coordination-unsaturated type I Cu center in bilirubin oxidase mutants.

Met467, the axial ligand to type I Cu in a multicopper oxidase, Myrothecium verrucaria bilirubin oxidase was substituted with a non-coordinating Phe and Leu to transform the spectral and magnetic properties and oxidase activities of the enzyme into those of fungal laccases, but the mutated type I Cu center showed properties characteristic of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459 as evidenced by a double mutation.

Aortic valve replacement in a patient with myelodysplastic syndrome and interstitial pneumonia.

There are a few reports of cardiac surgery in patients with myelodysplastic syndrome (MDS). It is difficult to control bleeding and prevent infection in the presence of pancytopenia. Interstitial pneumonia, which is treated by steroid medication, is also a risk factor in cardiac surgery. Aortic valve replacement was successfully performed in a patient with severe thrombocytopenia associated with MDS, interstitial pneumonia and scleroderma.

Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen.

The type I Cu site in the Cys457Ser mutant of Myrothecium verrucaria bilirubin oxidase was vacant, but the trinuclear center composed of a type II Cu and a pair of type III Cu's was fully occupied by three Cu ions. Cys457Ser could react with dioxygen, affording reaction intermediate I with absorption maxima at 340, 470, and 675 nm. This intermediate corresponds to that obtained from laccase, whose type I Cu is cupric and type II and III Cu's are cuprous [Zoppellaro, G., Sakurai, T., and Huang, H. (2001) J. Biochem. 129, 949-953] or whose type I Cu is substituted with Hg [Palmer, A. E., Lee, S. K., and Solomon, E. I. (2001) J. Am. Chem. Soc. 123, 6591-6599]. Another type I Cu mutant, Met467Gln, with modified spectroscopic properties and redox potential, afforded reaction intermediate II with absorption maxima at 355 and 450 nm. This intermediate corresponds to that obtained during the reaction of laccase [Sundaram, U. M., Zhang, H. H., Hedman, B., Hodgson, K. O., and Solomon, E. I. (1997) J. Am. Chem. Soc. 119, 12525-12540; Huang, H., Zoppellaro, G., and Sakurai, T. (1999) J. Biol. Chem. 274, 32718-32724]. According to a three-dimensional model of bilirubin oxidase, Asp105 is positioned near the trinuclear center. Asp105Glu and Asp105Ala exhibited 46 and 7.5% bilirubin oxidase activity compared to the wild-type enzyme, respectively, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II. In addition, this amino acid might be involved in the formation of the trinuclear center and in the binding of dioxygen based on the difficulties in incorporating four Cu ions in Asp105Ala and Asp105Asn and their reactions with dioxygen.