Identification of SLPI (Secretory Leukocyte Protease Inhibitor) in Human Mast Cells Using Immunohistochemistry and In Situ Hybridisation
-
U. Westin
Abstract
Recently interest has been focused on secretory leucocyte protease inhibitor (SLPI) and its role in immediate hypersensitive reactions, possibly by inhibiting mast cell chymase. The purpose of this investigation was to show whether or not SLPI is produced in mast cells.
Double-immunolabelling revealed that SLPI coexists with mast cell tryptase (60%) and chymase (37%). On the other hand, in situ hybridisation studies demonstrated the expression of SLPI mRNA in all mast cells. The differences in results can be attributed to the fact that in situ hybridisation is a more sensitive method than immunohistochemistry. Hence, we conclude that SLPI is produced in human tonsillar mast cells.
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
Articles in the same Issue
- Protein Kinase C-α Produces Reciprocal Effects on the Phorbol Ester Stimulated Tyrosine Phosphorylation of a 50 kDa Kinase in Jurkat Cells
- Growth- and Development-Dependent Expression of Gangliosides in Rat Hepatocytes and Liver Tissues
- Regulated Phosphorylation of the Gal4p Inhibitor Gal80p of <I>Kluyveromyces lactis</I> Revealed by Mutational Analysis
- The WW Domain of Dystrophin Requires EF-Hands Region to Interact with β-Dystroglycan
- Purification and MALDI-MS Characterization of Stressin, a Stress-Associated Glycoprotein
- Direct Selection of EGF Mutants Displayed on Filamentous Phage Using Cells Overexpressing EGF Receptor
- Refolding Studies on the Tetrameric Loop Deletion Mutant RM6 of ROP Protein
- Secretion of Protease Nexin-II/Amyloid β Protein Precursor by Human Colorectal Carcinoma Cells and Its Modulation by Cytokines/Growth Factors and Proteinase Inhibitors
- Isolation and Primary Structure of the CCI Papain-Like Cysteine Proteinases from the Latex of Carica candamarcensis Hook
- Identification of SLPI (Secretory Leukocyte Protease Inhibitor) in Human Mast Cells Using Immunohistochemistry and In Situ Hybridisation
- Stereochemistry of the Interaction between Methionine Sulfur and the Protein Core
- Trypsin from Pacifastacus leninsculus Hepatopancreas: Purification and cDNA Cloning of the Synthesized Zymogen
Articles in the same Issue
- Protein Kinase C-α Produces Reciprocal Effects on the Phorbol Ester Stimulated Tyrosine Phosphorylation of a 50 kDa Kinase in Jurkat Cells
- Growth- and Development-Dependent Expression of Gangliosides in Rat Hepatocytes and Liver Tissues
- Regulated Phosphorylation of the Gal4p Inhibitor Gal80p of <I>Kluyveromyces lactis</I> Revealed by Mutational Analysis
- The WW Domain of Dystrophin Requires EF-Hands Region to Interact with β-Dystroglycan
- Purification and MALDI-MS Characterization of Stressin, a Stress-Associated Glycoprotein
- Direct Selection of EGF Mutants Displayed on Filamentous Phage Using Cells Overexpressing EGF Receptor
- Refolding Studies on the Tetrameric Loop Deletion Mutant RM6 of ROP Protein
- Secretion of Protease Nexin-II/Amyloid β Protein Precursor by Human Colorectal Carcinoma Cells and Its Modulation by Cytokines/Growth Factors and Proteinase Inhibitors
- Isolation and Primary Structure of the CCI Papain-Like Cysteine Proteinases from the Latex of Carica candamarcensis Hook
- Identification of SLPI (Secretory Leukocyte Protease Inhibitor) in Human Mast Cells Using Immunohistochemistry and In Situ Hybridisation
- Stereochemistry of the Interaction between Methionine Sulfur and the Protein Core
- Trypsin from Pacifastacus leninsculus Hepatopancreas: Purification and cDNA Cloning of the Synthesized Zymogen