Leucine-rich alpha-2-glycoprotein (LRG) is a member of the leucine-rich repeat family. LRG is a plasma protein of approximately 50kD. LRG consists of 312aa. It has 1 galactosamine and 4 glucosamine oliogosacharides attached and has 2 intrachain disulfide bonds. Leucine comprises 66 of the 312aa, and LRG contains at least eight 24aa leucine-rich repeats. The consensus of these residues, termed leucine-rich repeats (LRR), has been identified as an LRR-containing domain. The primary function of LRRs is to provide versatile structural framework of the formation of protein-protein interactions. LRG is expressed during granulocyte differentiation. Although several family members of the leucine-rich repeat family have been shown to be involved in signal transduction, protein-protein interaction, or cell adhesion and development, a function for LRG remains elusive. LRG has been reported as a biomarker for certain diseases including microbial infections and cancer. LRG can be detected in human neutrophils and progenitor cells, but not in peripheral blood mononuclear cells.
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