The quality of the coronary arteries influences the outcome of bypass surgery [6] (multiple letters)

10.1016/j.athoracsur.2003.08.078Annals of Thoracic Surgery7841515-1517ATHS

Strong crossreaction of human anti-aprotinin antibodies from heart transplant patient with [Arg(15)]aprotinin

Brinkmann T, Korfer R, Wenzel H, Tschesche H, Kleesiek K. Strong crossreaction of human anti-aprotinin antibodies from heart transplant patient with [Arg(15)]aprotinin. IMMUNOPHARMACOLOGY. 1997;35(3):221-228.We detected anti-aprotinin antibodies by an enzyme immunoassay in serum of a 33 year old man who showed anaphylactic reactions during heart transplantation under aprotinin reexposition. The antibodies were isolated by affinity chromatography by aprotinin immobilized on CNBr activated Sepharose. The crossreactivity was tested by a competitive enzyme immunoassay (50% inhibition) against different aprotinin homologues and two human Kunitz-type protease inhibitors, bikunin and TFPI. In comparison with native aprotinin (immunoreactivity = 100%) the crossreaction of the homologue [Arg(15)]aprotinin was 76%, of [Val(15)]aprotinin 15% and of isoaprotinin 1, [Ala(14,38)]aprotinin and [seco15/16]aprotinin less than 10%. An immunoreactivity with bikunin and TFPI was not detected, Similar results were obtained with polyclonal anti-aprotinin antibodies from rabbit. Our results show that human anti-aprotinin antibodies are mainly directed against the reactive site of aprotinin, From this we conclude that the reactive site exposes the major epitope resulting in a major target site for antibodies in a species independent way, and therefore, it is obvious that the recombinant aprotinin homologue [Arg(15)]aprotinin, which is scheduled for therapy in open-heart surgery, will have similar immunogenic effects as native aprotinin

Coexpression of alpha and beta myosin heavy-chain isoforms in atria of neonates and infants with congenital heart disease.

Milting H, Thies WR, Breymann T, et al. Coexpression of alpha and beta myosin heavy-chain isoforms in atria of neonates and infants with congenital heart disease. Basic Res Cardiol. 1993;88(4):371-377.The relative amounts of cardiac myosin heavy-chain isoforms (MyHC) in right atrial tissue (RA) of 16 neonates and children suffering from congenital heart disease have been investigated. Quantification of MyHC was based on one-dimensional gel electrophoresis and on histometrical evaluation of cyro-sections stained with monoclonal antibodies against alpha- and beta-MyHC. The mean right atrial pressures ranged from 2 to 14 Hg. The RA load was normal in eight patients (5.1 +/- 1.3 mm Hg) and overloaded in eight cases (10 +/- 2.5 mm Hg). The arterial oxygen saturation was normal in 12 and ranged between 85% and 89% in four cases. In all patients a large proportion of atrial myocytes coexpressed alpha- and beta-MyHC. However, in the cases with pressure overloaded RA the amount of beta-MyHC was found to be 1.6 times higher than in the cases with normal pressure. This indicates an adaptational response to overload, as was previously described for the adult human heart. In light of this finding, it seems important to conserve as much as possible of the trained right atrial wall during a Fontan type of operation

Effects of temperature and sodium on myocardial and hepatocellular fatty acid uptake

Fatty acid influx into human myocardium was studied in 15 patients during the cooling phase of cardiopulmonary bypass at myocardial temperatures of 37 degrees to 25 degrees C. The fitting of the data to a functional relation, developed in this study, revealed fatty acid influx to be a temperature-dependent saturable process corresponding to a Michaelis-Menten constant (Km) at 37 degrees C of 0.26 +/- 0.084 mumol/g, a maximal fatty acid influx velocity (Vmax) at 37 degrees C of 0.28 +/- 0.045 mumol/g per minute, activation energy for fatty acid binding to the putative carrier (E) of 23.8 +/- 5.6 kcal/mol, and a free energy for conformational change of the carrier (U) of 10.9 +/- 8.0 kcal/mol. In short-term cultured hepatocytes, Km increased in the absence of Na+ from 171 +/- 48 to 301 +/- 71 nmol/L, and Vmax of [3H]oleate decreased from 1063 +/- 69 to 847 +/- 68 pmol/min per milligram protein. The fitting of these data to a functional relation revealed a transmembrane potential-dependent component of parameters E and U to be -0.479 and -0.374 kcal/mol, respectively. It is proposed that for fatty acid influx a protonated fatty acid form is preferred that consists of a Na+ complex with the mesomeric form of nondissociated fatty acid from which Na+ and H+ are released during collision with the carrier

Antimicrobial resistance of Escherichia coli isolated from freshwaters and hospital effluents in Belgium

The purpose of this work was to evaluate the level of antimicrobial resistant Escherichia coli isolates in freshwaters and hospital effluents in Belgium. The samples were collected from 24 locations along the Ourthe, Vesdre, Ambl eve and Meuse rivers and in the wastewater effluents of several hospitals. The sampling stations in rivers were classified according to the dominant land covers of the rivers (rural, urban and forest areas). Two sampling campaigns were organized in May and October 2019 to highlight a possible seasonal effect. A total of 938 E. coli strains were isolated on Chromogenic Selective Tryptone Bile X-glucuronide (TBX) and TBX supplemented with amoxicillin (TBX+AMX) media. Disk diffusion assays were performed following the EUCAST’s recommendations to assess the antimicrobial resistance against 12 antibiotics. A total of 32 7% of strains were at least resistant to one antibiotic and 24 6% were multiple antimicrobial resistant strains on TBX. The highest resistance rates were found for ampicillin (AMP), amoxicillin coupled with clavulanic acid (AMC) and sulfamethoxazole/trimethoprim (SXT). The lowest resistance rates were observed for meropenem (MEM) and ertapenem (ETP), which are last resort antibiotics. No significant difference was observed between both campaigns for the resistance rate to antibiotics