Short exposure of intestinal epithelial cells to TNF-alpha and histamine induces Mac-1-mediated neutrophil adhesion independent of protein synthesis.
Neutrophils play an important role in intestinal inflammation by interacting with intestinal epithelial cells. In this study, we evaluated neutrophil adhesion to intestinal epithelial cells using intestinal epithelial cell line HT29 stimulated with tumor necrosis factor alpha (TNF-alpha) and histamine for a short time (30 min). The TNF-alpha and histamine stimulation markedly increased neutrophil adhesion. The increased adhesion was inhibited by anti-CD11b and anti-CD18 monoclonal antibodies (mAbs), but not by anti-CD11a and anti-CD54 (ICAM-1) mAbs. It is interesting that flow cytometric analysis revealed that ICAM-1 expression on HT29 cells was not changed by TNF-alpha and histamine stimulation. Moreover, the increased adhesion was inhibited by proteinase K treatment but not cycloheximide treatment of HT29 cells. Together these observations suggest that short exposure of HT29 cells to TNF-alpha and histamine induces CD11b/CD18 (Mac-1)-dependent but CD11a/CD18 (LFA-1)-independent neutrophil adhesion to intestinal epithelial cells, and ICAM-1 is not likely to be involved in the interactions. Furthermore, epithelial cell ligand(s) for neutrophils is likely protein molecule(s) that is expressed on the cell by stimulation independent protein synthesis. However, it is also possible that neutrophil activating factor(s), which stimulates neutrophils to bind with epithelial ligands via Mac-1, is expressed by epithelial cells during stimulation.
Miyata
R
R
Department of Biochemistry, Juntendo University, School of Medicine, Tokyo, Japan.
Iwabuchi
K
K
Watanabe
S
S
Sato
N
N
Nagaoka
I
I
D000230:Adenocarcinoma / Q000473:pathology; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D000963:Antimetabolites / Q000494:pharmacology; D018821:CD18 Antigens / Q000502:physiology; D002413:Cations, Divalent / Q000494:pharmacology; D002448:Cell Adhesion / Q000187:drug effects; D016764:Cell Polarity; D003110:Colonic Neoplasms / Q000473:pathology; D003513:Cycloheximide / Q000494:pharmacology; D019286:Endopeptidase K / Q000494:pharmacology; D004847:Epithelial Cells / Q000187:drug effects; D006596:Hexosaminidases / Q000494:pharmacology; D006632:Histamine / Q000494:pharmacology*; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000502:physiology; D007413:Intestinal Mucosa / Q000166:cytology / Q000187:drug effects*; D016169:Lymphocyte Function-Associated Antigen-1 / Q000502:physiology; D016177:Macrophage-1 Antigen / Q000502:physiology*; D009363:Neoplasm Proteins / Q000502:physiology; D009439:Neuraminidase / Q000494:pharmacology; D009504:Neutrophils / Q000166:cytology / Q000187:drug effects*; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D011994:Recombinant Proteins / Q000494:pharmacology; D013268:Stimulation, Chemical; D014407:Tumor Cells, Cultured / Q000187:drug effects / Q000378:metabolism; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology*; D014415:Tunicamycin / Q000494:pharmacology; D010738:Type C Phospholipases / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000963:Antimetabolites; D018821:CD18 Antigens; D002413:Cations, Divalent; D016169:Lymphocyte Function-Associated Antigen-1; D016177:Macrophage-1 Antigen; D009363:Neoplasm Proteins; D011994:Recombinant Proteins; D014409:Tumor Necrosis Factor-alpha; D014415:Tunicamycin; D018799:Intercellular Adhesion Molecule-1; D006632:Histamine; D003513:Cycloheximide; D010738:Type C Phospholipases; D006596:Hexosaminidases; D009439:Neuraminidase; D019286:Endopeptidase K; D043265:Phosphatidylinositol Diacylglycerol-Lyase