GRIFIN, a Novel Lens-specific Protein Related to the Galectin Family

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...

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Veröffentlicht in:The Journal of biological chemistry 1998-10, Vol.273 (44), p.28889-28896
Hauptverfasser: Ogden, Alfred T., Nunes, Irene, Ko, Kyung, Wu, Shengji, Hines, Christina S., Wang, Ai-Fei, Hegde, Rashmi S., Lang, Richard A.
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Sprache:eng
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Zusammenfassung: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 β-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-relatedinter-fiber protein) to reflect its exclusion from the galectin family given the lack of affinity for β-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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.44.28889