| First Author | Ogden AT | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 44 | Pages | 28889-96 |
| PubMed ID | 9786891 | Mgi Jnum | J:71329 |
| Mgi Id | MGI:2149661 | Doi | 10.1074/jbc.273.44.28889 |
| Citation | Ogden AT, et al. (1998) GRIFIN, a novel lens-specific protein related to the galectin family. J Biol Chem 273(44):28889-96 |
| abstractText | The vertebrate lens is a relatively simple cellular structure that has evolved to refract light. The ability of the lens to focus light on the retina derives from a number of properties including the expression at high levels of a selection of soluble proteins referred to as the crystallins. In the present study, we have used differential cDNA display techniques to identify a novel, highly abundant and soluble lens protein. Though related to the family of soluble lectins called galectins, it does not bind beta-galactoside sugars and has atypical sequences at normally conserved regions of the carbohydrate-binding domain. Like some galectin family members, it can form a stable dimer. It is expressed only in the lens and is located at the interface between lens fiber cells despite the apparent lack of any membrane-targeting motifs. This protein is designated GRIFIN (galectin-related inter-fiber protein) to reflect its exclusion from the galectin family given the lack of affinity for beta-galactosides. Although the abundance, solubility, and lens-specific expression of GRIFIN would argue that it represents a new crystallin, its location at the fiber cell interface might suggest that its primary function is executed at the membrane. |
