PUBLICATION
Characterization of prominin-2, a new member of the prominin family of pentaspan membrane glycoproteins
- Authors
- Fargeas, C.A., Florek, M., Huttner, W.B., and Corbeil, D.
- ID
- ZDB-PUB-031003-1
- Date
- 2003
- Source
- The Journal of biological chemistry 278(10): 8586-8596 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Cloning, Molecular
- DNA, Complementary
- Expressed Sequence Tags
- Eye/metabolism
- Humans
- Membrane Glycoproteins/chemistry
- Membrane Glycoproteins/genetics
- Membrane Glycoproteins/metabolism*
- Mice
- Microscopy, Fluorescence
- Molecular Sequence Data
- RNA, Messenger/genetics
- Rats
- Sequence Homology, Amino Acid
- PubMed
- 12514187 Full text @ J. Biol. Chem.
Citation
Fargeas, C.A., Florek, M., Huttner, W.B., and Corbeil, D. (2003) Characterization of prominin-2, a new member of the prominin family of pentaspan membrane glycoproteins. The Journal of biological chemistry. 278(10):8586-8596.
Abstract
Prominin/CD133 is a 115/120-kDa integral membrane glycoprotein specifically associated with plasma membrane protrusions in epithelial and non-epithelial cells including neuroepithelial and hematopoietic stem cells. Here we report the identification as well as molecular and cell biological characterization of mouse, rat, and human prominin-2, a 112-kDa glycoprotein structurally related to prominin (referred to as prominin-1). Although the amino acid identity between prominin-2 and prominin-1 is low (<30%), their genomic organization is strikingly similar, suggesting an early gene duplication event. Like prominin-1, prominin-2 exhibits a characteristic membrane topology with five transmembrane segments and two large glycosylated extracellular loops. Upon its ectopic expression in Chinese hamster ovary cells as a green fluorescent protein fusion chimera, prominin-2 was also found to be associated with plasma membrane protrusions, as revealed by its co-localization with prominin-1, suggesting a related role. Consistent with this, prominin-2 shows a similar tissue distribution to prominin-1, being highly expressed in the adult kidney and detected all along the digestive tract as well as in various other epithelial tissues. However, in contrast to prominin-1, prominin-2 was not detected in the eye, which perhaps explains why a loss-of function mutation in the human prominin-1 gene causes retinal degeneration but no other obvious pathological signs. Finally, we present evidence for the existence of a family of pentaspan membrane proteins, the prominins, which are conserved in evolution.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping