MCP did not alter galectin-3 initially, but the latter effects were associated with significantly decreased galectin-3 levels, with no change in other renal galectins. This data raises the possibility that modulation of galectin-3 may be a novel strategy to reduce acute renal injury. Indeed, Fernandes Bertocchi and colleagues demonstrated acute kidney damage induced by ischemia reperfusion was attenuated in mice lacking galectin-3 with an improvement in blood urea nitrogen 6 and 24 hours after the initial insult, but no difference at later timepoints. Structurally, the knock-out animals presented with less acute tubular necrosis and a more prominent tubular regeneration when compared with controls and an improvement in inflammation. MCP is a derivative of pectin; a soluble dietary fibre found in the peel and pulp of citrus fruits, and has inhibitory effects on the progression of several animal models of cancer. MCP is rich in b-galactoside residues and binds to the carbohydrate recognition domain of galectin-3 thereby impairing the lectin��s carbohydrate binding-related functions. Therefore, it could be postulated that if MCP acted only through galectin-3 in FA nephropathy it would not have any effect on intracellular actions including proliferation and apoptosis, while modulating extracellular functions such as inflammation. This proved not the case; MCP treatment Ro 19-4603 reduced tubular proliferation two days following FA administration with no differences in galectin-3 expression. Most studies have only considered the effects of MCP in relation to galectin-3, but many other pathways could modulate proliferation here, such as MAP kinase activation. One could speculate that an alternative explanation is that it is not just galectin-3 levels but also bioavailability that should be considered. It is possible that similar levels of galectin-3 have less biological effects when MCP is present because its carbohydrate binding roles will be abrogated. This cannot be measured in-vivo at present, but in-vitro studies have shown that both cell migration and agglutination are diminished in the presence of MCP when induced with similar concentrations of galectin-3. The reduced proliferation could also suggest renal recovery is slower in MCP-treated mice or alternatively that MCP may protect the kidney against structural injury. This second explanation is supported by the fact MCP mice have preserved body weight and their kidneys did not exhibit such acute gross swelling as those exposed to FA but maintained on water alone. MCP decreased renal mRNA and protein levels of galectin-3 at 14 days after FA injection, in concert with significantly improved renal RHPS 4 methosulfate fibrosis as assessed by reduced expression of multiple fibrotic genes. MCP had no effect on galectin-1 and galectin-9, which are also expressed in the kidney, suggesting these effects do not result from MCP interactions with other galectins.