Bactericidal/permeability-increasing protein: Difference between revisions
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'''Bactericidal/permeability-increasing protein''' (BPI) is a 456-[[residue (chemistry)|residue]] (~50k[[atomic mass unit|Da]]) [[protein]] that is part of the [[innate immune system]].<ref name = "elsbach">{{cite journal | '''Bactericidal/permeability-increasing protein''' (BPI) is a 456-[[residue (chemistry)|residue]] (~50k[[atomic mass unit|Da]]) [[protein]] that is part of the [[innate immune system]].<ref name = "elsbach">{{cite journal | vauthors = Elsbach P | title = The bactericidal/permeability-increasing protein (BPI) in antibacterial host defense | journal = Journal of Leukocyte Biology | volume = 64 | issue = 1 | pages = 14–8 | date = July 1998 | pmid = 9665269 | url = http://www.jleukbio.org/cgi/reprint/64/1/14 | publisher = Wiley-Liss | format = pdf }}</ref> It belongs to family of [[lipid-binding serum glycoprotein]]s. | ||
==Distribution and function== | ==Distribution and function== | ||
BPI was initially identified in [[neutrophil]]s, but is found in other [[tissue (biology)|tissues]] including the [[epithelium|epithelial]] lining of [[mucous membrane]]s.<ref>{{cite journal | BPI was initially identified in [[neutrophil]]s, but is found in other [[tissue (biology)|tissues]] including the [[epithelium|epithelial]] lining of [[mucous membrane]]s.<ref>{{cite journal | vauthors = Canny G, Levy O, Furuta GT, Narravula-Alipati S, Sisson RB, Serhan CN, Colgan SP | title = Lipid mediator-induced expression of bactericidal/ permeability-increasing protein (BPI) in human mucosal epithelia | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 6 | pages = 3902–7 | date = March 2002 | pmid = 11891303 | pmc = 122621 | doi = 10.1073/pnas.052533799 | url = http://www.pnas.org/cgi/content/full/99/6/3902 | publisher = National Academy of Sciences }}</ref> | ||
It is an endogenous antibiotic protein with potent killing activity against [[Gram-negative bacteria]]. It binds to compounds called [[lipopolysaccharide]]s produced by Gram-negative bacteria. Lipolysaccharides are potent activators of the [[immune system]]; however, BPI at certain concentrations can prevent this activation. | It is an endogenous antibiotic protein with potent killing activity against [[Gram-negative bacteria]]. It binds to compounds called [[lipopolysaccharide]]s produced by Gram-negative bacteria. Lipolysaccharides are potent activators of the [[immune system]]; however, BPI at certain concentrations can prevent this activation. | ||
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==rBPI<sub>21</sub>== | ==rBPI<sub>21</sub>== | ||
Because lipopolysaccharides are potent [[inflammation|inflammatory]] agents, and the action of antibiotics can result in the release of these compounds, the binding capacity of BPI was explored as a possible means of reducing injury. [[Xoma|Xoma Ltd.]] developed a [[Recombinant DNA|recombinant]] 21kDa portion of the BPI molecule called rBPI<sub>21</sub>, NEUPREX, or opebecan. In a trial, it was found to decrease the mortality of Gram-negative bacterial-induced sepsis.<ref>{{cite journal | Because lipopolysaccharides are potent [[inflammation|inflammatory]] agents, and the action of antibiotics can result in the release of these compounds, the binding capacity of BPI was explored as a possible means of reducing injury. [[Xoma|Xoma Ltd.]] developed a [[Recombinant DNA|recombinant]] 21kDa portion of the BPI molecule called rBPI<sub>21</sub>, NEUPREX, or opebecan. In a trial, it was found to decrease the mortality of Gram-negative bacterial-induced sepsis.<ref>{{cite journal | vauthors = Levin M, Quint PA, Goldstein B, Barton P, Bradley JS, Shemie SD, Yeh T, Kim SS, Cafaro DP, Scannon PJ, Giroir BP | title = Recombinant bactericidal/permeability-increasing protein (rBPI21) as adjunctive treatment for children with severe meningococcal sepsis: a randomised trial. rBPI21 Meningococcal Sepsis Study Group | journal = Lancet | volume = 356 | issue = 9234 | pages = 961–7 | date = September 2000 | pmid = 11041396 | doi = 10.1016/S0140-6736(00)02712-4 | url = http://www.thelancet.com/journals/lancet/article/PIIS0140673600027124/abstract | publisher = Lancet Publishing Group | laydate = 2000-09-14 | laysource = Business Wire | laysummary = http://findarticles.com/p/articles/mi_m0EIN/is_2000_Sept_14/ai_65253242 }}</ref> Studies suggest that its binding activity is not the means by which it mediates its protective effect.<ref>{{cite journal | vauthors = Schlag G, Redl H, Davies J, Scannon P | title = Protective effect of bactericidal/permeability-increasing protein (rBPI21) in baboon sepsis is related to its antibacterial, not antiendotoxin, properties | journal = Annals of Surgery | volume = 229 | issue = 2 | pages = 262–71 | date = February 1999 | pmid = 10024109 | pmc = 1191640 | doi = 10.1097/00000658-199902000-00015 | publisher = Lippincott Williams & Wilkins }}</ref> Studies show biological effects with [[Gram-positive bacteria]]<ref>{{cite journal | vauthors = Srivastava A, Casey H, Johnson N, Levy O, Malley R | title = Recombinant bactericidal/permeability-increasing protein rBPI21 protects against pneumococcal disease | journal = Infection and Immunity | volume = 75 | issue = 1 | pages = 342–9 | date = January 2007 | pmid = 17101667 | pmc = 1828387 | doi = 10.1128/IAI.01089-06 | publisher = American Society for Microbiology }}</ref> and even in infection by the [[protozoa]]n, ''[[Toxoplasma gondii]]''.<ref>{{cite journal | vauthors = Khan AA, Lambert LH, Remington JS, Araujo FG | title = Recombinant bactericidal/permeability-increasing protein (rBPI21) in combination with sulfadiazine is active against Toxoplasma gondii | journal = Antimicrobial Agents and Chemotherapy | volume = 43 | issue = 4 | pages = 758–62 | date = April 1999 | pmid = 10103177 | pmc = 89203 | url = http://aac.asm.org/cgi/content/abstract/43/4/758 | publisher = American Society for Microbiology | quotes = }}</ref> | ||
==References== | == References == | ||
{{Reflist|2}} | {{Reflist|2}} | ||
==External links== | == External links == | ||
* {{MeshName|bactericidal+permeability+increasing+protein}} | * {{MeshName|bactericidal+permeability+increasing+protein}} | ||
{{Granule contents}} | {{Granule contents}} | ||
{{gene-20-stub}} | {{gene-20-stub}} | ||
Latest revision as of 07:08, 10 January 2019
| bactericidal/permeability-increasing protein | |
|---|---|
| Identifiers | |
| Symbol | BPI |
| Entrez | 671 |
| HUGO | 1095 |
| OMIM | 109195 |
| RefSeq | NM_001725 |
| UniProt | P17213 |
| Other data | |
| Locus | Chr. 20 q11.23 |
Bactericidal/permeability-increasing protein (BPI) is a 456-residue (~50kDa) protein that is part of the innate immune system.[1] It belongs to family of lipid-binding serum glycoproteins.
Distribution and function
BPI was initially identified in neutrophils, but is found in other tissues including the epithelial lining of mucous membranes.[2] It is an endogenous antibiotic protein with potent killing activity against Gram-negative bacteria. It binds to compounds called lipopolysaccharides produced by Gram-negative bacteria. Lipolysaccharides are potent activators of the immune system; however, BPI at certain concentrations can prevent this activation.
BPI was discovered by Jerrold Weiss and Peter Elsbach at New York University Medical School.
rBPI21
Because lipopolysaccharides are potent inflammatory agents, and the action of antibiotics can result in the release of these compounds, the binding capacity of BPI was explored as a possible means of reducing injury. Xoma Ltd. developed a recombinant 21kDa portion of the BPI molecule called rBPI21, NEUPREX, or opebecan. In a trial, it was found to decrease the mortality of Gram-negative bacterial-induced sepsis.[3] Studies suggest that its binding activity is not the means by which it mediates its protective effect.[4] Studies show biological effects with Gram-positive bacteria[5] and even in infection by the protozoan, Toxoplasma gondii.[6]
References
- ↑ Elsbach P (July 1998). "The bactericidal/permeability-increasing protein (BPI) in antibacterial host defense" (pdf). Journal of Leukocyte Biology. Wiley-Liss. 64 (1): 14–8. PMID 9665269.
- ↑ Canny G, Levy O, Furuta GT, Narravula-Alipati S, Sisson RB, Serhan CN, Colgan SP (March 2002). "Lipid mediator-induced expression of bactericidal/ permeability-increasing protein (BPI) in human mucosal epithelia". Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences. 99 (6): 3902–7. doi:10.1073/pnas.052533799. PMC 122621. PMID 11891303.
- ↑ Levin M, Quint PA, Goldstein B, Barton P, Bradley JS, Shemie SD, Yeh T, Kim SS, Cafaro DP, Scannon PJ, Giroir BP (September 2000). "Recombinant bactericidal/permeability-increasing protein (rBPI21) as adjunctive treatment for children with severe meningococcal sepsis: a randomised trial. rBPI21 Meningococcal Sepsis Study Group". Lancet. Lancet Publishing Group. 356 (9234): 961–7. doi:10.1016/S0140-6736(00)02712-4. PMID 11041396. Lay summary – Business Wire (2000-09-14).
- ↑ Schlag G, Redl H, Davies J, Scannon P (February 1999). "Protective effect of bactericidal/permeability-increasing protein (rBPI21) in baboon sepsis is related to its antibacterial, not antiendotoxin, properties". Annals of Surgery. Lippincott Williams & Wilkins. 229 (2): 262–71. doi:10.1097/00000658-199902000-00015. PMC 1191640. PMID 10024109.
- ↑ Srivastava A, Casey H, Johnson N, Levy O, Malley R (January 2007). "Recombinant bactericidal/permeability-increasing protein rBPI21 protects against pneumococcal disease". Infection and Immunity. American Society for Microbiology. 75 (1): 342–9. doi:10.1128/IAI.01089-06. PMC 1828387. PMID 17101667.
- ↑ Khan AA, Lambert LH, Remington JS, Araujo FG (April 1999). "Recombinant bactericidal/permeability-increasing protein (rBPI21) in combination with sulfadiazine is active against Toxoplasma gondii". Antimicrobial Agents and Chemotherapy. American Society for Microbiology. 43 (4): 758–62. PMC 89203. PMID 10103177.
External links
- bactericidal+permeability+increasing+protein at the US National Library of Medicine Medical Subject Headings (MeSH)
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