Hematology and serum chemistries of nestling bald eagles (Haliaeetus leucocephalus) in the lower peninsula of MI, USA.

Hematology constituents and serum biochemistries were determined in blood collected from 55 nestling bald eagles (Haliaeetus leucocephalus) from nest sites within the lower peninsula of Michigan in 1992. Hematological values were comparable to published ranges for birds for all but eosinophils, which were greater than normal. Serum chemistry values were similar to those of other birds for all but six parameters, uric acid, cholesterol, alkaline phosphatase, total protein, globulin, and urea nitrogen, which were greater and glucose which was less. Samples of blood collected from wild bald eagles can be used for hematologic parameters and serum chemistry. It is important for other studies of endangered species to obtain baseline data from healthy, wild animals in their natural environment, and for comparison of animals living in environments of greater exposure to those living in areas of lesser exposure to xenobiotics. We caution that arrangements for rapid analysis be done in advance of sample collection.

The neutrophil. Function, disorders, and testing.

Normal neutrophil function requires the cooperation and coordination of many cellular activities within the neutrophil and cells of the vascular system. The free flowing neutrophil begins the process by "rolling" along the vessel wall. This first step in migration is mediated by selectins on the surface of neutrophils, platelets, and endothelial cells. Subsequent firm adhesion requires the collaboration of neutrophil integrins and membrane-expressed cellular adhesion molecules. The activated neutrophil also changes shape from a sphere to an elongated motile cell by the assembly of actin filaments. At the inflammatory focus the neutrophil may encounter material to be ingested and killed. The ingestion process is mediated by the same receptors that stimulate firm adherence to the vessel wall. The ingestion process stimulates the formation of active NADPH oxidase, which is critical for the formation of superoxide and subsequent components of the killing mechanism. The process of normal neutrophil function is complex and multifaceted, but luckily, defects in this system are extremely rare. Patients with persistent and recurrent infections should be carefully evaluated for underlying disease before primary neutrophil dysfunction is pursued.

Adherence of neutrophils from dogs with diabetes mellitus.

Adherence of neutrophils from dogs with type I (insulin-dependent) diabetes mellitus controlled by insulin administration was compared with that from control dogs. Neutrophil adherence in whole blood decreased with increased serum glucose concentration, but was not different from normal cell adherence when isolated cells were examined. The decreased adherence in whole blood was considered to be the result of media factors and not dependent on altered neutrophil function.

Neutrophil function in the dog: shape change and response to a synthetic tripeptide.

Isolated dog neutrophils exposed to known chemotactic factors assumed a bipolar configuration in suspension. This response was initiated within 2 minutes with a gradual return to spherical shape. The rate of return to sphere was positively correlated with the dose of stimulant. Dog neutrophils exposed to N-formylmethionyl-leucyl-phenylalanine (fMLP) did not adapt to bipolar conformation and did not bind radiolabeled fMLP. These findings are consistent with other species (pig and cow) that also did not respond to fMLP.

Isoamylases in clinically normal dogs.

Isoenzymes of canine serum amylase were evaluated by electrophoresis on cellulose acetate membranes in a discontinuous buffer system. Two isoamylase groups were identified in the serum of clinically normal dogs. Most of the serum amylase activity was the more cathodal isoamylase. The anodal isoamylase was rarely observed in serum from normal dogs and, when present, accounted for little of the enzymatic activity. Amylase activities of various tissues were determined and isoenzymes were identified. The anodal isoenzyme was found in the pancreas and uterus. The cathodal isoamylase had its origin mainly from the intestinal tract. Activities of other tissues were not greater than was serum amylase activity. Effects of feeding upon total serum amylase activity and isoenzyme composition also were examined over a period of 5 minutes to 7 hours. Feeding did not markedly alter the serum amylase activity.