◀ Back to IRF6

BPI — IRF6

Text-mined interactions from Literome

Hubacek et al., Clin Chem Lab Med 2002 (Myocardial Infarction) : BPI is cytotoxic for Gram negative bacteria and BPI-LPS complexes do not activate monocytes
Eckert et al., J Immunol 2006 (Salmonella Infections) : Mouse BPI is most strongly induced by bacterial LPS through a signaling pathway that is completely dependent on TLR4-Toll/IL-1R domain containing adaptor inducing IFN-beta
Azuma et al., Biochem Biophys Res Commun 2007 : Although the functional mechanism whereby extra-cellular BPI modulates the intra-cellular signal pathways selected by the TLR adaptors, MyD88 and TICAM-1 ( TRIF ), remains unknown, we infer that the lipid A portion of LPS participates in LBP amplified IFN-beta induction and that BPI binding to LPS leads to inhibition of the activation of NF-kappaB and IFN-beta by LPS or agonistic lipid A via TLR4 in an extrinsic mode
Luo et al., Zhongguo Shi Yan Xue Ye Xue Za Zhi 2012 (Inflammation) : PRP were stimulated by LPS ( 10 µg/ml ) in the presence and absence of BPI ( 100 µg/ml ) or BPI alone
Revelo et al., J Dairy Sci 2012 : In addition, LPS augmented the expression of TNF, BPI , and CYBA ( 2,908, 59, and 158 % compared with controls, respectively ) only in PMNL from mid lactation cows
Marra et al., J Immunol 1990 : Since LPS is a structure common to all gram negative bacteria, we investigated whether the microbicidal protein BPI affects biologic activity of LPS in vitro
Weiss et al., J Immunol 1984 : BPI causes extracellular release of LPS , but only at supra saturating doses ... BPI markedly ( approximately 50 % ) and selectively stimulates biosynthesis of LPS , suggesting an attempt by BPI -killed bacteria to repair outer membrane damage ... The removal of surface bound BPI by 40 mM Mg2+ initiates time- and temperature dependent repair of the outer membrane permeability barrier and a further increase ( approximately 170 % of control ) in LPS synthesis, even though the bacteria are no longer viable ... These findings indicate that the repair of the permeability barrier after the removal of BPI from the surface requires newly made LPS, but apparently no biosynthesis of other outer membrane constituents, which strongly suggests that the effects of BPI on LPS are mainly responsible for the break-down of the outer membrane permeability barrier
Calvano et al., Arch Surg 1994 (Gram-Negative Bacterial Infections...) : Circulating polymorphonuclear leukocytes increase expression of BPI in response to LPS or gram negative sepsis
Vandermeer et al., J Appl Physiol 1994 (Lung Diseases...) : The salutory effects of BPI23 on acute lung injury in endotoxemic pigs may be mediated , at least in part, by inhibition of direct activation of phagocytes by LPS
Elsbach et al., Immunobiology 1993 (Gram-Negative Bacterial Infections) : BPI also binds with high affinity ( apparent Kd 2-5 nM ) to a broad range of LPS species and potently inhibits the biologic activities of LPS in vitro
Dentener et al., J Immunol 1993 : LPS prevented binding of BPI to anti-BPI mAb, whereas preincubation of LPS with LBP prevented the LPS induced inhibition ... Also, it was observed that both BPI and LBP inhibited LPS activity in the chromogenic LAL assay
Dentener et al., J Infect Dis 1996 : However, cell surface BPI did not quantitatively contribute to the interaction of LPS with the monocyte cell membrane, since preincubation of cells with 4E3 did not block binding of LPS-fluorescein isothiocyanate to monocytes
Dentener et al., J Infect Dis 1997 : Of the microbial products tested, lipopolysaccharide (LPS) most potently induced BPI release ; FMLP, serum treated zymosan (STZ), and lipoteichoic acid (LTA) also induced BPI release