title: Peptides bind to eosinophils in the rat stomach.
abstract: An immunological role for eosinophils has been well established. However, roles for eosinophils in the physiological functions of the organs they populate are little explored.
  
  
  
  Fixed, frozen, then vibratomed sections of rat stomach were exposed to biotinylated 1-17 gastrin (bG17), biotinylated gastrin-releasing peptide (bGRP), biotinylated neuromedin C (bNC), biotinylated vasoactive intestinal peptide (bVIP), and biotinylated substance P (bSP). Binding sites were identified using an avidin-biotin-glucose oxidase complex and tetranitroblue tetrazolium staining.
  
  
  
  bG17, bGRP, and bNC all bound to cells in the lamina propria and to a lesser extent in the submucosa. Neither bVIP nor bSP bound to cells in these sections. Stained cells were identified as eosinophils in the light microscope on the basis of their distribution and staining properties using the Luna stain for eosinophils and in the transmission electron microscope (TEM) on the basis of a light/TEM matching process. Plastic sections viewed in the light microscope showed that stain was localized to a granular component in the cytoplasm of the eosinophils. No other cell type, specifically neither mast cells nor plasma cells, stained. G17 competed for the bG17 binding site better than did NC. A competition study in which polyglutamic acid failed to compete with bG17 for the binding site, and the observation that bG17, bGRP, and bNC did not bind to other positively charged sites (e.g., collagen, red blood corpuscles), demonstrated that binding was not due to nonspecific electrostatic interactions alone. Binding of bG17 to a CCK(B)/gastrin-type receptor was ruled out when specific receptor antagonists failed to block binding.
  
  
  
  The particulate nature of the binding site suggests a secretory substance. If so, eosinophils might use that substance to destroy, neutralize, or control the activity of peptide hormones bound to it in the extracellular space.
authors.affiliation: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.
authors.forename: D H
authors.initials: DH
authors.lastname: Nichols
authors.forename: S
authors.initials: S
authors.lastname: Lovas
authors.forename: T E
authors.initials: TE
authors.lastname: Adrian
authors.forename: C A
authors.initials: CA
authors.lastname: Miller
authors.forename: R F
authors.initials: RF
authors.lastname: Murphy
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D019921:Biotinylation; D001839:Bombesin / Q000378:metabolism; D004396:Coloring Agents; D003594:Cytoplasmic Granules / Q000378:metabolism; D004804:Eosinophils / Q000378:metabolism* / Q000648:ultrastructure; D005629:Frozen Sections; D005753:Gastric Mucosa / Q000166:cytology* / Q000378:metabolism; D005755:Gastrins / Q000378:metabolism*; D008854:Microscopy, Electron; D009479:Neuropeptides / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D013373:Substance P / Q000378:metabolism; D016707:Tissue Fixation; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism
chemical_list: D004396:Coloring Agents; D005755:Gastrins; D009479:Neuropeptides; D010446:Peptide Fragments; D013373:Substance P; D014660:Vasoactive Intestinal Peptide; C013550:gastrin 17; C040794:neuromedin C; D001839:Bombesin