PUBLICATION
Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio
- Authors
- Schutte, A., Lottaz, D., Sterchi, E.E., Stocker, W., and Becker-Pauly, C.
- ID
- ZDB-PUB-070523-27
- Date
- 2007
- Source
- Biological chemistry 388(5): 523-531 (Journal)
- Registered Authors
- Keywords
- astacin, metalloprotease, metzincin, zebrafish
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Catalysis
- Chromosomes/genetics
- Conserved Sequence
- Gene Expression Regulation
- Humans
- Metalloendopeptidases/chemistry
- Metalloendopeptidases/genetics
- Metalloendopeptidases/metabolism*
- Microscopy, Fluorescence
- Molecular Sequence Data
- Phylogeny
- Protein Structure, Tertiary
- Protein Subunits/chemistry
- Protein Subunits/genetics
- Protein Subunits/metabolism
- RNA, Messenger/genetics
- Sequence Alignment
- Structural Homology, Protein
- Zebrafish/genetics
- Zebrafish/metabolism*
- Zinc/metabolism*
- PubMed
- 17516848 Full text @ Biol. Chem.
Citation
Schutte, A., Lottaz, D., Sterchi, E.E., Stocker, W., and Becker-Pauly, C. (2007) Two alpha subunits and one beta subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio. Biological chemistry. 388(5):523-531.
Abstract
Meprins are members of the astacin family of metalloproteases expressed in epithelial tissues, intestinal leukocytes and certain cancer cells. In mammals, there are two homologous subunits, which form complex glycosylated disulfide-bonded homo- and heterooligomers. Both human meprin alpha and meprin beta cleave several basement membrane components, suggesting a role in epithelial differentiation and cell migration. There is also evidence that meprin beta is involved in immune defence owing to its capability of activating interleukin-1beta and the diminished mobility of intestinal leukocytes in meprin beta-knockout mice. Here we show for the first time by reverse transcription PCR, immunoblotting and immunofluorescence analyses that meprins are expressed not only in mammals, but also in the zebrafish Danio rerio. In contrast to the human, mouse and rat enzymes, zebrafish meprins are encoded by three genes, corresponding to two homologous alpha subunits and one beta subunit. Observations at both the mRNA and protein level indicate a broad distribution of meprins in zebrafish. However, there are strikingly different expression patterns of the three subunits, which is consistent with meprin expression in mammals. Hence, D. rerio appears to be a suitable model to gain insight into the basic physiological functions of meprin metalloproteases.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping