Lambda-crystallin homolog

Lambda-crystallin homolog (CRYL1) is a NAD-dependent dehydrogenase that catalyzes the conversion of L-gulonate to 3-dehydro-L-gulonate, with secondary activity toward L-3-hydroxybutyrate and L-threonate (UniProt: Q9Y2S2). The protein is a 319-residue enzyme with a molecular mass of approximately 35 kDa.

CRYL1 is expressed in human tissues and localizes to multiple subcellular compartments. UniProt records no canonical disease associations for this protein.

CRYL1 shows elevated expression in Alzheimer's Disease brain tissue. Analysis of post-mortem AD brain compared to age-matched controls across four subcellular fractions (P2, P3, S2, S3) using TMT-labeled proteomics detected upregulation with a mean log2 fold-change of 0.85 (Chaparral AD proteomics). This increase suggests altered metabolic or oxidative stress-response pathways in AD pathology, though the functional significance of CRYL1 elevation in disease progression remains to be determined.