A murine antibacterial orthologue to human bactericidal/permeability-increasing protein (BPI) is expressed in testis, epididymis, and bone marrow.
(2005) In Journal of Leukocyte Biology 77(3). p.369-377- Abstract
- 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 report the isolation of a murine full-length cDNA encoding a 54-kDa protein, showing 53% amino acid identity and 71% similarity, to human BPI. The murine BPI and human BPI genes show a similar exon-intron organization. Murine BPI mRNA was detected in... (More)
- 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 report the isolation of a murine full-length cDNA encoding a 54-kDa protein, showing 53% amino acid identity and 71% similarity, to human BPI. The murine BPI and human BPI genes show a similar exon-intron organization. Murine BPI mRNA was detected in testis, epididymis, and bone marrow, as well as in Sertoli and promyelocytic cell lines. Although levels of BPI mRNA in human and murine testis were comparable, expression in murine bone marrow cells was low as compared with that in human bone marrow. BPI protein showed a cytoplasmic, granular localization in mature neutrophils. BPI gene expression in Sertoli and promyelocytic cells was enhanced several-fold by all-trans retinoic acid. Overexpression of murine BPI in human embryonic kidney 293 cells resulted in antibacterial activity against Escherichia coli, comparable with that obtained with human BPI. In conclusion, it was demonstrated that mouse neutrophils store BPI with antibacterial activity and that murine BPI is also expressed in testis and epididymis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/132056
- author
- Lennartsson, Andreas LU ; Pieters, Katrien LU ; Vidovic, Karina LU and Gullberg, Urban LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- granulopoiesis, leukocyte, innate, immunity, azurophil, neutrophil, antimicrobial
- in
- Journal of Leukocyte Biology
- volume
- 77
- issue
- 3
- pages
- 369 - 377
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:15590754
- wos:000227488600012
- scopus:14244250585
- ISSN
- 1938-3673
- DOI
- 10.1189/jlb.0304159
- language
- English
- LU publication?
- yes
- id
- a54f6286-54e9-4d07-82bc-05f53b75ce55 (old id 132056)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15590754&dopt=Abstract
- date added to LUP
- 2016-04-01 11:57:35
- date last changed
- 2022-02-10 23:58:32
@article{a54f6286-54e9-4d07-82bc-05f53b75ce55, abstract = {{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 report the isolation of a murine full-length cDNA encoding a 54-kDa protein, showing 53% amino acid identity and 71% similarity, to human BPI. The murine BPI and human BPI genes show a similar exon-intron organization. Murine BPI mRNA was detected in testis, epididymis, and bone marrow, as well as in Sertoli and promyelocytic cell lines. Although levels of BPI mRNA in human and murine testis were comparable, expression in murine bone marrow cells was low as compared with that in human bone marrow. BPI protein showed a cytoplasmic, granular localization in mature neutrophils. BPI gene expression in Sertoli and promyelocytic cells was enhanced several-fold by all-trans retinoic acid. Overexpression of murine BPI in human embryonic kidney 293 cells resulted in antibacterial activity against Escherichia coli, comparable with that obtained with human BPI. In conclusion, it was demonstrated that mouse neutrophils store BPI with antibacterial activity and that murine BPI is also expressed in testis and epididymis.}}, author = {{Lennartsson, Andreas and Pieters, Katrien and Vidovic, Karina and Gullberg, Urban}}, issn = {{1938-3673}}, keywords = {{granulopoiesis; leukocyte; innate; immunity; azurophil; neutrophil; antimicrobial}}, language = {{eng}}, number = {{3}}, pages = {{369--377}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Journal of Leukocyte Biology}}, title = {{A murine antibacterial orthologue to human bactericidal/permeability-increasing protein (BPI) is expressed in testis, epididymis, and bone marrow.}}, url = {{http://dx.doi.org/10.1189/jlb.0304159}}, doi = {{10.1189/jlb.0304159}}, volume = {{77}}, year = {{2005}}, }