Ultrastructural morphology and cytochemistry of iron-deficient polymorphonuclear leukocytes.
Previous studies have documented decreased activities of certain enzymes and altered function in polymorphonuclear leukocytes (PMN) during iron deficiency. The present study was undertaken to determine if the enzymatic abnormalities could be correlated with morphologic or quantitative change in PMN granules. Ultrastructural examination of primary and secondary granules and assessment of the secondary granule components alkaline phosphatase and vicinal glycol-containing glycoconjugates was performed in rabbit bone marrow, peripheral blood, and peritoneal heterophils. In addition, biochemical quantifications of the secondary granule component alkaline phosphatase and the primary granule marker beta-glucuronidase were performed. The results confirmed that a marked, significant decrease in alkaline phosphatase occurs in iron-deficient animals; however, no biochemical decrease in beta-glucuronidase activity was observed. Ultrastructurally, PMN secondary granules of iron-deficient rabbits tended to be more numerous than in controls when examined with morphometric and glycoconjugate staining methods, but lacked staining in alkaline phosphatase preparations. These results demonstrate that iron-deficient rabbits produce normal to increased quantities of primary and secondary granules, despite a uniform deficiency of alkaline phosphatase, a secondary granule marker.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D003594:Cytoplasmic Granules / Q000648:ultrastructure; D006801:Humans; D007501:Iron / Q000097:blood; D000090463:Iron Deficiencies; D008854:Microscopy, Electron; D009504:Neutrophils / Q000201:enzymology / Q000648:ultrastructure*; D011817:Rabbits
D007501:Iron; D000469:Alkaline Phosphatase