PUBLICATION
Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydrate-binding galectin
- Authors
- Ahmed, H., and Vasta, G.R.
- ID
- ZDB-PUB-080506-2
- Date
- 2008
- Source
- Biochemical and Biophysical Research Communications 371(3): 350-355 (Journal)
- Registered Authors
- Keywords
- Galectin, GRIFIN, Zebrafish, Danio rerio, Carbohydrate-recognition domain, Lens crystallin
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Carbohydrate Metabolism
- Embryo, Nonmammalian/metabolism
- Evolution, Molecular
- Galectin 1/chemistry
- Galectin 1/genetics
- Galectin 1/metabolism
- Galectins/chemistry
- Galectins/genetics*
- Galectins/metabolism*
- Humans
- Lens, Crystalline/embryology
- Lens, Crystalline/metabolism
- Mice
- Molecular Sequence Data
- Protein Conformation
- Rats
- Sequence Homology, Amino Acid
- Tissue Distribution
- Zebrafish/embryology
- Zebrafish/genetics
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics*
- Zebrafish Proteins/metabolism*
- PubMed
- 18448074 Full text @ Biochem. Biophys. Res. Commun.
Citation
Ahmed, H., and Vasta, G.R. (2008) Unlike mammalian GRIFIN, the zebrafish homologue (DrGRIFIN) represents a functional carbohydrate-binding galectin. Biochemical and Biophysical Research Communications. 371(3):350-355.
Abstract
Galectins, a family of beta-galactoside-binding proteins, participate in a variety of biological processes, such as early development, tissue organization, immune regulation, and tumor evasion and metastasis. Although as many as fifteen bona fide galectins have been identified in mammals, but the detailed mechanisms of their biological roles still remain unclear for most. This fragmentary knowledge extends to galectin-like proteins such as the rat lens crystallin protein GRIFIN (Galectin-related inter fiber protein) and the galectin-related protein GRP (previously HSPC159; hematopoietic stem cell precursor) that lack carbohydrate-binding activity. Their inclusion in the galectin family has been debated, as they are considered products of evolutionary co-option. We have identified a homologue of the GRIFIN in zebrafish (Danio rerio) (designated DrGRIFIN), which like the mammalian equivalent is expressed in the lens, particularly in the fiber cells, as revealed by whole mount in situ hybridization and immunostaining of 2 dpf (days post fertilization) embryos. As evidenced by RT-PCR, it is weakly expressed in the embryos as early as 21 hpf (hour post fertilization) but strongly at all later stages tested (30 hpf and 3, 4, 6, and 7 dpf). In adult zebrafish tissues, however, DrGRIFIN is also expressed in oocytes, brain, and intestine. Unlike the mammalian homologue, DrGRIFIN contains all amino acids critical for binding to carbohydrate ligands and its activity was confirmed as the recombinant DrGRIFIN could be purified to homogeneity by affinity chromatography on a lactosyl-Sepharose column. Therefore, DrGRIFIN is a bona fide galectin family member that in addition to its carbohydrate-binding properties, may also function as a crystallin.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping