Description
The 111-amino acid FIZZ2 protein, which shows 59% sequence identity to mouse Fizz2 and 47% identity to human FIZZ3, shares an N-terminal signal peptide and a C-terminal stretch of 10 cysteine residues with identical spacing with other FIZZ family members. Strong expression of mouse Fizz2 mRNA was found in the adult colon in the mucosal crypt epithelial cells. Increases in circulating resistin or RELMB levels markedly stimulated hepatic glucose production despite the presence of fixed physiologic insulin levels. This enhanced rate of glucose output was due to increased flux through glucose-6-phosphatase. The results supported the notion that a novel family of fat- and gut-derived circulating proteins modulates hepatic insulin action