Faculty Bibliography

Granulocytes from patients with chronic myelogenous leukemia (CML) were studied for their ability to regenerate surface sialic acid following treatment with Vibrio cholera neuraminidase (VCN) in vitro. Immediately after neuraminidase treatment, CML and normal granulocytes showed similar incorporation of radioactivity after surface labelling with sodium periodate/potassium-H3-borohydride (PI/BH3(4)). CML granulocytes treated with neuraminidase then incubated for 18 h in nutrient medium showed strikingly increased PI/BH3(4) labelling, usually greater than initial pretreatment values, consistent with a rapid reappearance of sialic acid in the cell membrane. This pattern was not seen in normal granulocytes. The aberrant regeneration of sialic acid in CML granulocytes in vitro could be inhibited by addition of 3 X 10(-6) M retinoic acid, suggesting either a direct effect on membrane glycoconjugate synthesis or an association with granulocyte differentiation.

Peripheral blood granulocytes from patients with chronic myelogenous leukemia (CML) were studied for accessibility of membrane sialic acid and galactose residues to sodium borohydride-3H radiolabeling after oxidation with sodium metaperiodate (PI/B3H4) or with galactose oxidase (GO/B3H4). Granulocytes from untreated patients with chronic myelogenous leukemia showed increased radiolabeling with PI/B3H4, and decreased labeling with GO/B3H4 when compared to normal granulocytes. Granulocytes from leukemic patients receiving chemotherapy showed normal labeling patterns. Gel electrophoresis of membrane extracts showed that the changes in PI/B3H4 and GO/B3H4 reactivity of CML cells were distributed over all membrane protein bands. Our data suggest that CML granulocyte membrane proteins are aberrantly sialylated, with decreased accessibility of galactose residues, and that these changes may be reversed by clinical drug treatment.

Two structurally distinct forms of eggwhite lysozyme (EC 3.2.1.17) are known. The egg white of some species contains both of these forms, while the egg white of other species appears to contain only one or the other of them. We have immunological and electrophoretic evidence that the chicken, which has only one lysozyme type in its egg white, contains both types in its polymorphonuclear leukocytes. Experiments on Embden goose bone marrow showed that this tissue also contains both lysozymes, even though the egg white of this species contains only one of them. Our studies suggest that many avian species have the genetic loci that code for both forms of lysozyme, but that a species-specific regulatory mechanism controls whether one or the other or both of them are expressed during egg white production. The fact that two distinct lysozymes are present in chicken leukocytes may be of significance to the antibacterial mechanism of these cells, especially in light of the fact that they lack myeloperoxidase, an important leukocyte enzyme in mammals.