PUBLICATION
Nonspecific Cytotoxic Cell Antimicrobial Protein (NCAMP-1): A Novel Alarmin Ligand Identified in Zebrafish
- Authors
- Monette, M.M., Evans, D.L., Krunkosky, T., Camus, A., Jaso-Friedmann, L.
- ID
- ZDB-PUB-150218-1
- Date
- 2015
- Source
- PLoS One 10: e0116576 (Journal)
- Registered Authors
- Evans, Donald L., Jaso-Friedmann, Liliana
- Keywords
- none
- MeSH Terms
-
- Adenosine Triphosphate/pharmacology
- Alarmins/chemistry
- Alarmins/metabolism*
- Animals
- Antibodies/immunology
- Antimicrobial Cationic Peptides/immunology
- Antimicrobial Cationic Peptides/metabolism*
- Antimicrobial Cationic Peptides/toxicity
- Benzoxazoles/chemistry
- Benzoxazoles/metabolism
- Calcium/metabolism
- Cells, Cultured
- Epithelial Cells/cytology
- Epithelial Cells/drug effects
- Epithelial Cells/metabolism
- Female
- Immunohistochemistry
- Intestines/metabolism
- Intestines/pathology
- Kidney/metabolism
- Kidney/pathology
- Ligands
- Microscopy, Fluorescence
- Quinolinium Compounds/chemistry
- Quinolinium Compounds/metabolism
- Receptors, Purinergic P2X7/chemistry
- Receptors, Purinergic P2X7/metabolism
- Zebrafish
- PubMed
- 25689842 Full text @ PLoS One
Citation
Monette, M.M., Evans, D.L., Krunkosky, T., Camus, A., Jaso-Friedmann, L. (2015) Nonspecific Cytotoxic Cell Antimicrobial Protein (NCAMP-1): A Novel Alarmin Ligand Identified in Zebrafish. PLoS One. 10:e0116576.
Abstract
Cells from the coelomic cavity of adult zebrafish (zf) were used to study the alarmin-like activities of nonspecific cytotoxic cell antimicrobial protein-1 (NCAMP-1). Immunohistochemistry studies using polyclonal anti-NCAMP-1 identified constitutive NCAMP-1 in epithelial cells of the zf anterior kidney, in liver parenchyma and in the lamina propria of the intestine. NCAMP-1 was also located in the cytosol of mononuclear cells in these tissues. Cytosolic NCAMP-1 was detected in a diverse population of coelomic cells (CC) using confocal microscopy and polyclonal anti-NCAMP-1 staining. Large mononuclear and heterophil-like CC had intracellular NCAMP-1. These studies indicated that NCAMP-1 is constitutively found in epithelial cells and in ZFCC. To establish a relationship between NCAMP-1 and the alarmin functions of ATP, a stimulation-secretion model was initiated using zf coelomic cells (ZFCC). ZFCCs treated with the alarmin ATP secreted NCAMP-1 into culture supernatants. Treatment of ZFCC with either ATP or NCAMP-1 activated purinergic receptor induced pore formation detected by the ZFCC uptake of the dye YO-PRO-1. ATP induced YO-PRO-1 uptake was inhibited by antagonists oxidized-ATP, KN62, or CBB. These antagonists did not compete with NCAMP-1 induced YO-PRO-1 uptake. Binding of ZFCC by both ATP and NCAMP-1 produced an influx of Ca2+. Combined treatment of ZFCC with ATP and NCAMP-1 increased target cell cytotoxicity. Individually NCAMP-1 or ATP treatment did not produce target cell damage. Similar to ATP, NCAMP-1 activates cellular pore formation, calcium influx and cytotoxicity.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping