Inflammasoma

Inflammasoma (-atis, n.) est complexus proteinorum oligomerorum responsa inflammatoria^[1] per varios adaptores^[2] excitatus. Adaptoribus incitatum his inflammasoma enzymum caspasem 1^[3] se immutare impellit ita, ut praecursor interleukini 1 beta macrophagocytis liberatus in formam activam interleukinumi 1 activi (IL-1β) et febrem generantis convertatur ideoque cataracta inflammationis biochemica continuetur.

Cave: notitiae huius paginae nec praescriptiones nec consilia medica sunt.

Inflammasomatum complexus, qui in textu myeloideo locati sunt ex enzymis caspasi 1 ac PYCARD et receptorio NALP et nonnumquam enzymo caspasi 5 compositi sunt. Variae formae receptoriorum NALP complexu ligatae notae sunt.

Natura inflammasomatum

Contextus

Sub inflammationem systema immunitatis innatum machinationem defensionis contestari oportet. Post stimulationem inflammasomate primum liberatio ex cellula cytokinorum conceditur, deinde extra cellulam pyroptosis (mors cellularum programmata) fit^[4].

Structura

Inflammasomata sunt complexus ex diversis proteinis compositi, ita ex enzymis caspasi 1 ac PYCARD et receptorio NALP et nonnumquam enzymo caspasi 5. Variae formae rececptoriorum NALP complexu ligatae notae sunt, quo inflammasomata NLRP1 et NLRP3^[5] et NLRC4 munerum singularium nominata sunt.

Physiologia

Quando infectio prodit cellulae systematis immunitatis, ut monocyti, macrophagocyti receptoria peculiaria, receptoria exempla cognoscendorum (Anglice Pattern Recognition Receptors, PRR) enim, exprimunt: et superficie membranae et intra cellulam.

Haec PRR′ia modo duo genera stimulorum cognoscunt: PAMP vel DAMP. PAMP est abbreviatura Anglica "pathogenis sociatorum exemplorum molecularis" (pathogen-associated molecular patterns), quae sunt partes corpori alienae, per exemplum lipopolysaccharidi bacteriorum. Pluribus exemplis alienis receptoria propria ex familia receptoriorum typi Toll instar (abbreviatura internationalis: TLR) superficie cellulae sunt; Exemplum flagella bacterialia per TLR 5 superficie membranae cellularum immunitatis recognoscuntur^[6]. DAMP sunt "vastitatibus sociata exempla molecularia" (damage-associated molecular patterns), quae sunt partes cellularum vulneratarum corporis poprii denaturatae: Quando damnum cellularum prodit, organella ex cellula liberata signum initii inflammationis fient^[7].

Inter cytokina et inflammasomata cellularum immunitatis mutuo signa dantur^[8].

Notae

↑ Martinon F., Burns K., Tschopp J. (2002). "The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta". Mol Cell 10 (2): 417-26 .
↑ Mariathasan S., Newton K., Monack D. M., Vucic D., French D. M., Lee W. P., Roose-Girma M., Erickson S., Dixit V. M. (2004). "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf". Nature 430 (6996): 213-8 .
↑ seu interleukini 1 beta convertasis
↑ Fink S. L., Cookson B. T. (2006). "Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages". Cell Microbiol 8 (11): 1812-25 .
↑ Lebeaupin C., Proics E., de Bieville C. H., Rousseau D., Bonnafous S., Patouraux S., Adam G., Lavallard V. J., Rovere C., Le Thuc O., Saint-Paul M. C., Anty R., Schneck AS., Iannelli A., Gugenheim J., Tran A., Gual P., Bailly-Maitre B. (2015). "ER stress induces NLRP3 inflammasome activation and hepatocyte death". Cell Death Dis 6: e1879
↑ Rumbo M., Nempont C., Kraehenbuhl J. P., Sirard J. C. (2006). "Mucosal interplay among commensal and pathogenic bacteria: lessons from flagellin and Toll-like receptor 5". FEBS Lett 580 (12): 2976-84 .
↑ Rubartelli A., Lotze M. T. (2007). "Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox". Curr Opin Immunol 23 (5): 591-7 .
↑ Barker B. R., Taxman D. J., Ting J. P. (2011). "Cross-regulation between the IL-1β/IL-18 processing inflammasome and other inflammatory cytokines". Curr Opin Immunol 23 (5): 591-7 .

Nexus interni

[TSCHOPP02-1] Martinon F., Burns K., Tschopp J. (2002). "The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta". Mol Cell 10 (2): 417-26 .

[2] Mariathasan S., Newton K., Monack D. M., Vucic D., French D. M., Lee W. P., Roose-Girma M., Erickson S., Dixit V. M. (2004). "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf". Nature 430 (6996): 213-8 .

[3] seu interleukini 1 beta convertasis

[4] Fink S. L., Cookson B. T. (2006). "Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages". Cell Microbiol 8 (11): 1812-25 .

[5] Lebeaupin C., Proics E., de Bieville C. H., Rousseau D., Bonnafous S., Patouraux S., Adam G., Lavallard V. J., Rovere C., Le Thuc O., Saint-Paul M. C., Anty R., Schneck AS., Iannelli A., Gugenheim J., Tran A., Gual P., Bailly-Maitre B. (2015). "ER stress induces NLRP3 inflammasome activation and hepatocyte death". Cell Death Dis 6: e1879

[6] Rumbo M., Nempont C., Kraehenbuhl J. P., Sirard J. C. (2006). "Mucosal interplay among commensal and pathogenic bacteria: lessons from flagellin and Toll-like receptor 5". FEBS Lett 580 (12): 2976-84 .

[7] Rubartelli A., Lotze M. T. (2007). "Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox". Curr Opin Immunol 23 (5): 591-7 .

[8] Barker B. R., Taxman D. J., Ting J. P. (2011). "Cross-regulation between the IL-1β/IL-18 processing inflammasome and other inflammatory cytokines". Curr Opin Immunol 23 (5): 591-7 .

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