A murine antibacterial ortholog to human bactericidal/permeability‐increasing protein (BPI) is expressed in testis, epididymis, and bone marrow

@article{Lennartsson2005AMA,
  title={A murine antibacterial ortholog to human bactericidal/permeability‐increasing protein (BPI) is expressed in testis, epididymis, and bone marrow},
  author={Andreas Lennartsson and Katrien Pieters and Karina Vidovic and Urban Gullberg},
  journal={Journal of Leukocyte Biology},
  year={2005},
  volume={77}
}
The bactericidal/permeability‐increasing protein (BPI), stored in human neutrophil granulocytes, is cytotoxic against Gram‐negative bacteria. Several genes related to BPI cluster on human chromosome 20 and on mouse chromosome 2, but expression and characterization of a BPI ortholog in the mouse have not been reported. We asked whether BPI is structurally and functionally conserved between humans and mice and whether murine BPI might be synthesized in neutrophils as well as in other tissues. We… 

All‐trans retinoic acid‐induced expression of bactericidal/permeability‐increasing protein (BPI) in human myeloid cells correlates to binding of C/EBPβ and C/EBPε to the BPI promoter

It is shown that treatment of NB4 cells with all‐trans retinoic acid (ATRA) induces BPI expression at mRNA and at protein level, and the dependency on C/EBPβ and C/ EBPε provides an explanation for delayed BPI mRNA expression, as compared with mRNA of other azurophil granule proteins.

Bactericidal/permeability-increasing protein in the reproductive system of male mice may be involved in the sperm-oocyte fusion.

The results suggest that BPI may take part in the process of sperm-oocyte fusion and play a unique and significant role in reproduction.

Endotoxin-Induced Expression of Murine Bactericidal Permeability/Increasing Protein Is Mediated Exclusively by Toll/IL-1 Receptor Domain-Containing Adaptor Inducing IFN-β-Dependent Pathways1

Functional studies revealed that mouse BPI does have the potential to neutralize LPS and inhibits bacterial growth, and the transcriptional activation is controlled by TLRs.

Expression of Bactericidal/Permeability-Increasing Protein Requires C/EBPɛ

The requirement for a myeloid-specific transcription factor, CCAAT/enhancer binding protein ɛ (C/EBPɛ), in mediating BPI gene expression in myeloids cells in vitro and in vivo is demonstrated.

Bactericidal/permeability-increasing protein originates in both the testis and the epididymis and localizes in mouse spermatozoa

A dual origin of the BPI that generated both in the testis and epididymis, and associated with mouse spermatozoa is suggested, which might be involved in the dynamics modification of the sperm plasma membrane and also the fertilization process.

Functional and biochemical characterization of epithelial bactericidal/permeability-increasing protein.

It is demonstrated that, whereas epithelia express markedly less BPI protein than neutrophils, epithelial BPI contributes significantly to bacterial killing and attenuating bacterial-elicted proinflammatory signals and provides insight into the relevance of BPI as an anti-infective molecule at intestinal surfaces.

Bactericidal/Permeability-increasing protein is associated with the acrosome region of rodent epididymal spermatozoa.

Data suggested that BPI, which is synthesized in caput epididymis and secreted into the lumen, is associated with not only the granulelike structures, but also the sperm surface covering the acrosome region, and that B PI bound to the acosome region is extinguished by acrosomes reaction.

Bactericidal Permeability Increasing Protein Deficiency Aggravates Acute Colitis in Mice by Increasing the Serum Levels of Lipopolysaccharide

The BPI KO mice developed worse colitis than WT mice by increased colitis symptoms and colonic mucosal damage, elevated levels of serum LPS, and a disrupted microbiome, suggesting BPI could be a potential target for treatment of ulcerative colitis in humans.

Murine Bactericidal/Permeability-Increasing Protein Inhibits the Endotoxic Activity of Lipopolysaccharide and Gram-Negative Bacteria1

Recombinant expression and functional characterization of the mouse homolog of human bactericidal/permeability-increasing protein BPI are reported, demonstrating that murine BPI is a potent LPS-neutralizing protein that may limit innate immune responses during Gram-negative infections.

Long‐term anti‐endotoxin/E. coli efficacy in mice transfected with AAV2/1‐muBPI25‐muFcγ1

  • Z. LvYiqiang Fan Y. An
  • Biology
    APMIS : acta pathologica, microbiologica, et immunologica Scandinavica
  • 2016
An adeno‐associated virus‐containing mouse BPI and Fc fragment genes are established and AAV‐muBPI‐Fc has potential long‐term efficacy as an anti‐endotoxin and has anti‐bacterial activity in mice, suggesting the potential clinical application of AAV-hBPI-Fc, such as in endotoxin shock.

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