lactoferrin and Eosinophilia

The association of perennial allergic rhinitis (PAR) with recurrent sinusitis (RS) is well recognized. Anatomic abnormalities at the osteomeatal complex or ciliary dysfunction may play a significant role in some patients. However, for most patients with allergy, the determinants of RS are unknown.. To determine whether altered concentrations of antimicrobial peptides and proteins, such as lysozyme, lactoferrin, human beta-defensin-2 (HBD-2), and human neutrophil peptides 1 to 3 (HNP-1 to 3), contribute to the development of RS in patients with PAR.. Nasal secretions were collected by vacuum aspiration from 15 individuals with PAR+RS, 16 with PAR alone, and 16 controls. Lysozyme and lactoferrin levels were determined in nasal secretions by using quantitative enzyme-linked immunosorbent assay, and HBD-2 and HNP-1 to 3 levels were determined in nasal secretions by using semiquantitative Western blot analysis. Eosinophil-derived neurotoxin (EDN) levels were measured by using enzyme-linked immunosorbent assay as a marker of nasal eosinophilia in all 3 groups.. Levels of EDN were elevated significantly in patients with PAR+RS compared with controls. Lysozyme levels were decreased significantly in patients with PAR+RS compared with PAR alone or controls. Mean lysozyme levels were significantly lower in patients with EDN levels greater than 1,000 ng/mL vs those with levels of 1,000 ng/mL or less in the PAR+RS group. There were no statistically significant differences in lactoferrin, HBD-2, and HNP-1 to 3 levels among the 3 groups.. The presence of eosinophils and their products and reduced lysozyme concentrations may be critical factors that predispose the airways of patients with PAR to RS.

Topics: Adult; alpha-Defensins; beta-Defensins; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Eosinophil-Derived Neurotoxin; Eosinophilia; Female; Humans; Lactoferrin; Male; Muramidase; Nasal Lavage Fluid; Recurrence; Rhinitis, Allergic, Perennial; Ribonucleases; Sinusitis; Skin Tests

Mechanisms for degranulation in human eosinophils were evaluated. Release of eosinophil cationic protein (ECP), a unique eosinophil granule constituent, was measured upon exposure of purified eosinophils to a large surface consisting of Sephadex beads coated with serum, which leads to complement activation. Extracellular release of approximately 15% of the cellular ECP occurred both with eosinophils from patients with eosinophilia and normal people. Almost all eosinophils isolated from patients with eosinophilia and normal people adhered to serum-treated Sephadex. The data suggest that interaction through C3 receptors is a prerequisite for ECP release from eosinophils when exposed to serum-treated Sephadex. Both cytochalasin B, cytochalasin D and hydrocortisone reduced the release of ECP. Neither the cytochalasins nor hydrocortisone inhibited the adherence of eosinophils to the Sephadex beads. Thus the inhibitory effect of these agents on ECP release is a direct effect on the degranulation process. ECF-A, histamine and colchicine did not affect the release mechanism. No direct relationship was found between degranulation and oxidative burst inasmuch as some soluble mediators induced a high respiratory burst without a concomitant ECP release. Our data suggest that mechanisms for degranulation are not fully identical in eosinophils and neutrophils.

Topics: Antigen-Antibody Complex; Blood Proteins; Cell Adhesion; Concanavalin A; Cytochalasin B; Cytochalasin D; Cytochalasins; Cytoplasmic Granules; Eosinophil Granule Proteins; Eosinophilia; Eosinophils; Humans; Hydrocortisone; Lactoferrin; Neutrophils; Oxygen Consumption; Peroxidase; Ribonucleases

Several arginine-rich cationic proteins previously isolated from granules of leukemic myeloid cells have been found to reside primarily in human eosinophil leukocytes. The major component has a molecular weight of 21,000 and it contains approximately 2.6 moles of zinc per mole of protein. Velocity centrifugation of cytoplasm from leukocytes of patients with marked eosinophilia showed that this group of proteins is packaged in the crystalloid-containing large eosinophil granules. Approximately 30% of the protein content of eosinophil granules belonged to this group of cationic proteins. Bactericidal or esterolytic activities of the cationic proteins were not detected, nor did they inhibit guinea pig anaphylatoxin or histamine-induced contraction. The basic protein previously demonstrated in guinea pig eosinophils may be analogous to the group of basic proteins of human eosinophils but great differences are found for molecular weight and amino acid composition.

Topics: Acid Phosphatase; Adolescent; Arginine; Blood Bactericidal Activity; Blood Proteins; Child; Cytoplasmic Granules; Eosinophilia; Eosinophils; Female; Hodgkin Disease; Humans; Lactoferrin; Microbial Collagenase; Neutrophils; Pancreatic Elastase; Peroxidase; Peroxidases; Zinc