Bovine Lactoferrin (bLf) possessing an high homology of sequence with human Lf, is classified as Generally Recognized As Save and is used in vitro models and in clinical trials on humans. It is a multifunctional glycoprotein able i) to chelate two ferric ions/molecule, ii) to interact with cellular and molecular components due to its high pI >9 , iii) to enter inside the nucleus where, by binding to specific DNA sequences, inhibits pro-inflammatory cytokine synthesis and iv) to bind at high affinity to Lf receptor (LfR) and at low affinity to low density lipoprotein receptor related protein (LRP). We assumed that LfR or LRP could differently influence bLf internalization, localization into the nucleus, and consequently, anti-inflammatory activity and cell damage repair. As prolonged inflammation leads to non-repairing cell damages, the bLf anti-inflammatory activity could neutralize overabundant immune response and promote the cell damage repair. The cell damage repaired by bLf has been investigated only in intestinal cell model. Here, for the first time, bLf efficacy on cell damage repair, probably associated to LfR or LRP, has been studied in vitro on human cholangiocytes and in vivo on pregnant women with membrane premature rupture and in the patients affected from osteonecrosis. The preliminary positive results in healing both membrane premature ruptures and wounds following osteonecrosis treatments, respectively, have been obtained through intravaginal and oral bLf administration. A further deep study is required to unequivocally ascertain this new important bLf therapeutic potential in repairing cell damages promoted by severe and prolonged inflammations.
