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

  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},
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.



The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved.

The results indicate that the LBP, BPI, and PLTP genes, and probably the CETP gene, may have evolved from a common primordial gene and may share similar functional properties.

Expression of Antimicrobial Defensins in the Male Reproductive Tract of Rats, Mice, and Humans1

The male reproductive tract produces defensins that most probably assume an important, innate organ defense system against pathogens, and high salt concentration or dithiothreitol-sensitive cationic extracts from human seminal plasma were found to display antimicrobial activity.

The bactericidal/permeability‐increasing protein (BPI) in antibacterial host defense

  • P. Elsbach
  • Biology, Medicine
    Journal of leukocyte biology
  • 1998
Results suggest that BPI may have a place in the treatment of life‐threatening infections and conditions associated with bacteremia and endotoxemia and preliminary evidence points to overall benefit in BPI‐treated patients.

Four BPI (bactericidal/permeability-increasing protein)-like genes expressed in the mouse nasal, oral, airway and digestive epithelia.

A cluster of related genes whose products show structural identity with bactericidal permeability-increasing protein (BPI) has been identified in the genomes of both mice and humans and this mini-review addresses the tissue-specific expression of these genes in the mouse.

Novel Antimicrobial Peptide of Human Epididymal Duct Origin1

R reverse transcription-polymerase chain reaction analysis confirmed the occurrence of eight human HE2-derived transcripts, including minor mRNA variants, that had previously been shown only in animal species and suggested a proteolytic processing of these peptides by a furin-like proprotein convertase, which cleaves a propiece from the longer precursor peptides.

Lipid mediator-induced expression of bactericidal/ permeability-increasing protein (BPI) in human mucosal epithelia

  • G. CannyO. Levy S. Colgan
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 2002
This work demonstrates that human epithelial cells express bactericidal/permeability-increasing protein (BPI), an antibacterial and endotoxin-neutralizing molecule previously associated with neutrophils, and identifies a previously unappreciated "molecular shield" for protection of mucosal surfaces against Gram-negative bacteria and their endotoxin.

AML-1, PU.1, and Sp3 regulate expression of human bactericidal/permeability-increasing protein.

Role of the bactericidal/permeability-increasing protein in host defence.

The Human Cationic Antimicrobial Protein (hCAP-18) Is Expressed in the Epithelium of Human Epididymis, Is Present in Seminal Plasma at High Concentrations, and Is Attached to Spermatozoa

The results suggest a key role for hCAP-18 in the antibacterial integrity of the male reproductive system and the attachment of h CAP-18 to spermatozoa may implicate a role for the protein in conception in conception.

FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

In basal medium E, synthetic FALL-39 was highly active against Escherichia coli and Bacillus megaterium and CD spectra showed that medium E induced 30% helix formation in F Fall-39.