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Identification of a novel stress regulated FERM domain containing cytosolic protein having PTP activity in Setaria cervi, a bovine filarial parasite.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2015 Feb 27; Vol. 458 (1), pp. 194-200. Date of Electronic Publication: 2015 Jan 31. - Publication Year :
- 2015
-
Abstract
- A 67 kDa cytosolic FERM domain containing protein having significant protein tyrosine phosphatases activity (PTPL) has been purified to homogeneity from Setaria cervi, a bovine filarial parasite. The MALDI-MS/MS analysis of the purified protein revealed 16 peptide peaks showing nearest match to Brugia malayi Moesin/ezrin/radixin homolog 1 protein and one peptide showing significant similarity with a region lying in the catalytic domain of human PTPD1. PTPL showed significant cross reactivity with the human PTP1B antibody and colocalize with actin in the coelomyrian cells of hypodermis in the parasite. PTPL was stress regulated as it showed marked decrease in the expression when exposed to Aspirin, an antifilarial drug and Phenylarsine Oxide, PTP inhibitor.<br /> (Copyright © 2015 Elsevier Inc. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Arsenicals pharmacology
Aspirin pharmacology
Catalytic Domain
Cross Reactions
Female
Helminth Proteins isolation & purification
Humans
Molecular Sequence Data
Protein Structure, Tertiary
Protein Tyrosine Phosphatases chemistry
Sequence Homology, Amino Acid
Setaria Nematode drug effects
Setaria Nematode pathogenicity
Cytosol metabolism
Helminth Proteins chemistry
Helminth Proteins metabolism
Protein Tyrosine Phosphatases metabolism
Setaria Nematode chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 458
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 25645020
- Full Text :
- https://doi.org/10.1016/j.bbrc.2015.01.100