Human RegIV Protein Adopts a Typical C-Type Lectin Fold but Binds Mannan with Two Calcium-Independent Sites

Regenerating islet‐derived family member, 4 modulates multiple receptor tyrosine kinases and mediators of drug resistance in cancer

“…6b); while we did not further characterize the nature of the Reg IV doublet, we speculate that this is likely due to glycosylation, as has been previously reported. 7 Lysates were then probed to reveal phosphotyrosine bands. On the basis of the phosphotryosine blot, Reg IV knockdown precluded the ability of each ligand to fully induce tyrosine phosphorylation on distinct protein bands.…”

“…However, unlike other C-type lectins, Reg IV can bind polysaccharides in the absence of calcium. 7 The Reg family of proteins have been reported to play a role in pancreatic, gastric, liver and intestinal growth or differentiation. 8 Upregulation of Reg IV has been reported in colorectal, prostate, gallbladder, salivary, gastric and pancreatic cancers [9][10][11][12][13][14][15][16][17][18][19] ; additionally, it is amplified in pancreatic cancer.…”

Recombinant Human REG I<i>α</i> Aggregates <i>Staphylococcus aureus</i>—Exhibits a Lectin-Like Function

“…Previously, lectin activity has been reported in other Reg proteins such as recombinant human REG III and REG IV that were expressed in E. coli [24] [31]. Therefore, we assumed that compromising glycosylation on REG Iα will not affect its lectin activity.…”

The Role of Reg Proteins, a Family of Secreted C-Type Lectins, in Islet Regeneration and as Autoantigens in Type 1 Diabetes

“…It should also be noted that RegIV, which has a blocked tryptic cleavage site and can therefore not undergo the unblocking process leading to an active bactericidal Reg member and has a deleted EPN motif nevertheless does bind carbohydrates (Ho, Lou et al 2010). Perhaps the carbohydrate-binding step is common to all Reg members, with effector mechanisms diverging downstream of this event.…”