Crystallin lambda 1 (CRYL1)

Crystallin lambda 1 (CRYL1) is a human metabolic enzyme that catalyzes the oxidation of L-gulonate to dehydro-L-gulonate in the uronate cycle, an alternative glucose catabolism pathway accounting for about 5% of daily glucose metabolism[1][2][3][5]. It requires NAD(H) as a coenzyme and is inhibited by inorganic phosphate. CRYL1 is highly expressed in liver and kidney and is evolutionarily related to proteins serving a structural function in the lens of the eye in other species (such as rabbit), but not in humans[1][3]. CRYL1 also acts as a tumor suppressor: its expression is frequently reduced in hepatocellular carcinoma, and its loss correlates with larger tumor size, higher stage, and reduced disease-free survival; restoring its expression suppresses tumor cell proliferation, prolongs cell cycle, and induces apoptosis[1][3]. Rarely, gene fusion events (e.g., CRYL1-IFT88) have been implicated in tumorigenesis[1]. Deficiency or alteration in CRYL1 has been associated with metabolic disorders such as pentosuria. No drugs are known to target CRYL1 directly, nor are safety concerns with targeting CRYL1 documented in the literature.

Other names

Lambda-crystallin homologL-gulonate 3-dehydrogenaseL-3-aldonate dehydrogenaseGDHgul3DHlambda-CRYHEL30crystallin, lamda 1epididymis luminal protein 30testicular tissue protein Li 44