Background Babesia canis infection induces a marked acute phase response (APR) that might be associated with alteration in lipid and lipoprotein metabolism and disease prognosis. Hypothesis Dogs with B. canis ‐induced APR develop dyslipidemia with altered lipoprotein concentration and morphology. Animals Twenty‐nine client‐owned dogs with acute B. canis infection and 10 clinically healthy control dogs. Methods Observational cross‐sectional study. Serum amyloid A (SAA) was measured using ELISA. Cholesterol, phospholipids, and triglycerides were determined biochemically. Lipoproteins were separated using agarose gel electrophoresis. Lipoprotein diameter was assessed by polyacrylamide gradient gel electrophoresis; correlation with ApoA‐1 (radioimmunoassay) and SAA was determined. Results Dogs with B. canis infection had a marked APR (median SAA, 168.3 μg/mL; range, 98.1‐716.2 μg/mL) compared with controls (3.2 μg/mL, 2.0‐4.2 μg/mL) ( P < .001). Dogs with B. canis infection had significantly lower median cholesterol (4.79 mmol/L, 1.89‐7.64 mmol/L versus 6.15 mmol/L, 4.2‐7.4 mmol/L) ( P = .02), phospholipid (4.64 mmol/L, 2.6‐6.6 mmol/L versus 5.72 mmol/L, 4.68‐7.0 mmol/L) ( P = .02), and α‐lipoproteins (77.5%, 27.7%‐93.5% versus 89.2%, 75.1%‐93.5%) ( P = .04), and higher ApoA‐1 (1.36 U, 0.8‐2.56 U versus 0.95 U, 0.73‐1.54 U) concentrations ( P = .02). Serum amyloid A correlated with high‐density lipoproteins (HDLs) diameter (rho = .43; P = .03) and ApoA‐1 (rho = .63, P < .001). Conclusions and Clinical Importance Major changes associated with B. canis ‐induced APR in dogs are related to concentration, composition, and morphology of HDL particles pointing to an altered reverse cholesterol transport. Parallel ApoA‐1 and SAA concentration increase is a unique still unexplained pathophysiological finding.

Adequate acrosome reaction is one of the essential events that has to occur in successful mammalian fertilization. The purpose of the present study was to assess the acrosome reaction in human spermatozoa by means of iodine-labelled lectins concanavalin A and peanut agglutinin ([125I]Con A and [125I]PNA). Six sperm samples in the control (fertile) group were compared with 24 samples obtained from infertile patients. The acrosome reaction in both groups was induced in vitro by adding follicular fluid. Iodine-labelled lectins were bound to the sperm surface, and alteration in the binding capacity for [125I]PNA and [125I]Con A after induced acrosomal reaction was the main parameter for the prediction of acrosome reaction and fertilizing ability. It is hoped that with the availability of this test, in-vivo data may be accumulated.

Lectins extracted from com (Zea mays L.) kernel with Tris-HCI buffer pH 7.5 were isolated from the crude extract by affinity chromatography on Sepharose 6B-N-acetyl-D-galactosamine and Sepharose 6B-methyla-D-mannoside, and also by lectin affinity chromatography using concanavalin A and Lens culinaris lectin as ligands. According to preferential monosaccharide specificity, salt-soluble lectins of com seed comprise at least two distinct types: N-acetyl-D-galactosamine-interactive and mannose-interactive lectins. The extracted lectins are unstable, with a tendency to form aggregates during storage.

No abstract

No abstract