In addition to the monomeric mammalian progelatinase, two additional forms of progelatinase have been identified. The shorter of these additional forms is a covalently linked, disulfide-bridged protein that heterodimerizes with a short protein; an α2-Microglobulin-related protein known as neutrophil gelatinase-associated lipocalin (NGAL), which is moderately expressed in breast and lung tissues. NGAL belongs to the lipocalin family and has a high degree of similarity with rat α2-Microglobulin-related protein and mouse protein 24p3. NGAL is able to bind a derivative of the bacterial chemotactic peptide, suggesting that it has important immuno-modulatory functions. NGAL has been described as an inflammatory protein; it is released into the circulation as a result of the inflammatory activation of leukocytes initiated by the extra-corporeal circulation. In addition, NGAL synthesis is induced in epithelial cells in inflammatory and neoplastic colorectal diseases. In conclusion, NGAL may serve as a scavenger of bacterial products to function in the anti-inflammatory process.