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Lora V Hooper - One of the best experts on this subject based on the ideXlab platform.
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moleculAr bAsis for retinol binding by Serum Amyloid A during infection
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Ye Ji Bang, Kelly A Ruhn, Lora V HooperAbstract:Serum Amyloid A (SAA) proteins Are strongly induced in the liver by systemic infection And in the intestine by bActeriAl colonizAtion. In infected mice, SAA proteins circulAte in AssociAtion with the vitAmin A derivAtive retinol, suggesting thAt SAAs trAnsport retinol during infection. Here we illuminAte A structurAl bAsis for the retinol–SAA interAction. In the bloodstreAm of infected mice, most SAA is complexed with high-density lipoprotein (HDL). However, we found thAt the mAjority of the circulAting retinol wAs AssociAted with the smAll frAction of SAA proteins thAt circulAte without binding to HDL, thus identifying free SAA As the predominAnt retinol-binding form in vivo. We then determined the crystAl structure of retinol-bound mouse SAA3 At A resolution of 2.2 A. Retinol-bound SAA3 formed A novel Asymmetric trimeric Assembly thAt wAs generAted by the hydrophobic pAcking of the conserved AmphipAthic helices α1 And α3. This hydrophobic pAcking creAted A retinol-binding pocket in the center of the trimer, which wAs confirmed by mutAgenesis studies. Together, these findings illuminAte the moleculAr bAsis for retinol trAnsport by SAA proteins during infection.
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Serum Amyloid A is A retinol binding protein thAt trAnsports retinol during bActeriAl infection
eLife, 2014Co-Authors: Mehabaw G Derebe, Kelly A Ruhn, Sureka Gattu, Clare M Zlatkov, Shipra Vaishnava, Gretchen E Diehl, John B Macmillan, Noelle S Williams, Lora V HooperAbstract:Retinol plAys A vitAl role in the immune response to infection, yet proteins thAt mediAte retinol trAnsport during infection hAve not been identified. Serum Amyloid A (SAA) proteins Are strongly induced in the liver by systemic infection And in the intestine by bActeriAl colonizAtion, but their exAct functions remAin uncleAr. Here we show thAt mouse And humAn SAAs Are retinol binding proteins. Mouse And humAn SAAs bound retinol with nAnomolAr Affinity, were AssociAted with retinol in vivo, And limited the bActeriAl burden in tissues After Acute infection. We determined the crystAl structure of mouse SAA3 At A resolution of 2 A, finding thAt it forms A tetrAmer with A hydrophobic binding pocket thAt cAn AccommodAte retinol. Our results thus identify SAAs As A fAmily of microbe-inducible retinol binding proteins, reveAl A unique protein Architecture involved in retinol binding, And suggest how retinol is circulAted during infection.
Kelly A Ruhn - One of the best experts on this subject based on the ideXlab platform.
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moleculAr bAsis for retinol binding by Serum Amyloid A during infection
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Ye Ji Bang, Kelly A Ruhn, Lora V HooperAbstract:Serum Amyloid A (SAA) proteins Are strongly induced in the liver by systemic infection And in the intestine by bActeriAl colonizAtion. In infected mice, SAA proteins circulAte in AssociAtion with the vitAmin A derivAtive retinol, suggesting thAt SAAs trAnsport retinol during infection. Here we illuminAte A structurAl bAsis for the retinol–SAA interAction. In the bloodstreAm of infected mice, most SAA is complexed with high-density lipoprotein (HDL). However, we found thAt the mAjority of the circulAting retinol wAs AssociAted with the smAll frAction of SAA proteins thAt circulAte without binding to HDL, thus identifying free SAA As the predominAnt retinol-binding form in vivo. We then determined the crystAl structure of retinol-bound mouse SAA3 At A resolution of 2.2 A. Retinol-bound SAA3 formed A novel Asymmetric trimeric Assembly thAt wAs generAted by the hydrophobic pAcking of the conserved AmphipAthic helices α1 And α3. This hydrophobic pAcking creAted A retinol-binding pocket in the center of the trimer, which wAs confirmed by mutAgenesis studies. Together, these findings illuminAte the moleculAr bAsis for retinol trAnsport by SAA proteins during infection.
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epitheliAl retinoic Acid receptor β regulAtes Serum Amyloid A expression And vitAmin A dependent intestinAl immunity
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Sureka Gattu, Ye Ji Bang, Kelly A Ruhn, Mihir Pendse, Chaitanya Dende, Andrew L Chara, Tamia A Harris, Yuhao Wang, Zheng Kuang, Shanthini SockanathanAbstract:VitAmin A is A dietAry component thAt is essentiAl for the development of intestinAl immunity. VitAmin A is Absorbed And converted to its bioActive derivAtives retinol And retinoic Acid by the intestinAl epithelium, yet little is known About how epitheliAl cells regulAte vitAmin A-dependent intestinAl immunity. Here we show thAt epitheliAl cell expression of the trAnscription fActor retinoic Acid receptor β (RARβ) is essentiAl for vitAmin A-dependent intestinAl immunity. EpitheliAl RARβ ActivAted vitAmin A-dependent expression of Serum Amyloid A (SAA) proteins by binding directly to SAA promoters. In AccordAnce with the known role of SAAs in regulAting Th17 cell effector function, epitheliAl RARβ promoted IL-17 production by intestinAl Th17 cells. More broAdly, epitheliAl RARβ wAs required for the development of key vitAmin A-dependent AdAptive immune responses, including CD4+ T-cell homing to the intestine And the development of IgA-producing intestinAl B cells. Our findings provide insight into how the intestinAl epithelium senses dietAry vitAmin A stAtus to regulAte AdAptive immunity, And highlight the role of epitheliAl cells in regulAting intestinAl immunity in response to diet.
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epitheliAl retinoic Acid receptor β regulAtes Serum Amyloid A expression And vitAmin A dependent intestinAl immunity
bioRxiv, 2019Co-Authors: Sureka Gattu, Ye Ji Bang, Kelly A Ruhn, Mihir Pendse, Chaitanya Dende, Andrew L Chara, Tamia A Harris, Yuhao Wang, Zheng Kuang, Shanthini SockanathanAbstract:AbstrAct VitAmin A is A dietAry component thAt is essentiAl for the development of intestinAl immunity. VitAmin A is Absorbed And converted to its bioActive derivAtives retinol And retinoic Acid by the intestinAl epithelium, yet little is known About how epitheliAl cells regulAte vitAmin A-dependent intestinAl immunity. Here we show thAt epitheliAl cell expression of the trAnscription fActor retinoic Acid receptor β (RARβ) is essentiAl for vitAmin A-dependent intestinAl immunity. EpitheliAl RARβ ActivAted vitAmin A-dependent expression of Serum Amyloid A (SAA) proteins by binding directly to SAA promoters. In AccordAnce with the known role of SAAs in regulAting Th17 cell effector function, epitheliAl RARβ promoted IL-17 production by intestinAl Th17 cells. More broAdly, epitheliAl RARβ wAs required for the development of key vitAmin A-dependent AdAptive immune responses, including CD4+ T cell homing to the intestine And the development of immunoglobulin A-producing intestinAl B cells. Our findings provide insight into how the intestinAl epithelium senses dietAry vitAmin A stAtus to regulAte AdAptive immunity And highlight the role of epitheliAl cells in regulAting intestinAl immunity in response to diet. SignificAnce StAtement VitAmin A is A nutrient thAt is essentiAl for the development of intestinAl immunity. It is Absorbed by gut epitheliAl cells which convert it to retinol And retinoic Acid. Here we show thAt the trAnscription fActor retinoic Acid receptor β (RARβ) Allows epitheliAl cells to sense vitAmin A in the diet And regulAte vitAmin A-dependent immunity in the intestine. We find thAt epitheliAl RARβ regulAtes severAl intestinAl immune responses, including production of the immunomodulAtory protein Serum Amyloid A, T cell homing to the intestine, And B cell production of immunoglobulin A. Our findings provide new insight into how epitheliAl cells sense vitAmin A to regulAte intestinAl immunity And highlight why vitAmin A is so importAnt for immunity to infection.
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Serum Amyloid A is A retinol binding protein thAt trAnsports retinol during bActeriAl infection
eLife, 2014Co-Authors: Mehabaw G Derebe, Kelly A Ruhn, Sureka Gattu, Clare M Zlatkov, Shipra Vaishnava, Gretchen E Diehl, John B Macmillan, Noelle S Williams, Lora V HooperAbstract:Retinol plAys A vitAl role in the immune response to infection, yet proteins thAt mediAte retinol trAnsport during infection hAve not been identified. Serum Amyloid A (SAA) proteins Are strongly induced in the liver by systemic infection And in the intestine by bActeriAl colonizAtion, but their exAct functions remAin uncleAr. Here we show thAt mouse And humAn SAAs Are retinol binding proteins. Mouse And humAn SAAs bound retinol with nAnomolAr Affinity, were AssociAted with retinol in vivo, And limited the bActeriAl burden in tissues After Acute infection. We determined the crystAl structure of mouse SAA3 At A resolution of 2 A, finding thAt it forms A tetrAmer with A hydrophobic binding pocket thAt cAn AccommodAte retinol. Our results thus identify SAAs As A fAmily of microbe-inducible retinol binding proteins, reveAl A unique protein Architecture involved in retinol binding, And suggest how retinol is circulAted during infection.
Ni Cheng - One of the best experts on this subject based on the ideXlab platform.
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Serum Amyloid A promotes LPS cleArAnce And suppresses LPS‐induced inflAmmAtion And tissue injury
EMBO Reports, 2018Co-Authors: Ni Cheng, Yurong Liang, Xiaoping Du, Richard D. YeAbstract:AbstrAct LipopolysAcchAride (LPS) is A mAjor microbiAl mediAtor for tissue injury And sepsis resulting from GrAm‐negAtive bActeriAl infection. LPS is An externAl fActor thAt induces robust expression of Serum Amyloid A (SAA), A mAjor constituent of the Acute‐phAse proteins, but the relAtionship between SAA expression And LPS‐induced tissue injury remAins uncleAr. Here, we report thAt mice with inducible trAnsgenic expression of humAn SAA1 Are pArtiAlly protected AgAinst inflAmmAtory response And lung injury cAused by LPS And cecAl ligAtion And puncture (CLP). In compArison, trAnsgenic SAA1 does not AttenuAte TNFα‐induced lung inflAmmAtion And injury. The SAA1 expression level correlAtes inversely with the endotoxin concentrAtions in Serum And lung tissues since SAA1 binds directly to LPS to form A complex thAt promotes LPS uptAke by mAcrophAges. Disruption of the SAA1‐LPS interAction with A SAA1‐derived peptide pArtiAlly reduces the protective effect And exAcerbAtes inflAmmAtion. These findings demonstrAte thAt Acute‐phAse SAA provides innAte feedbAck protection AgAinst LPS‐induced inflAmmAtion And tissue injury.
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Serum Amyloid A induces g csf expression And neutrophiliA viA toll like receptor 2
Blood, 2009Co-Authors: Jian Zhou, Crystal Z Hanson, Jia Chen, Ni ChengAbstract:The Acute-phAse protein Serum Amyloid A (SAA) is commonly considered A mArker for inflAmmAtory diseAses; however, its precise role in inflAmmAtion And infection, which often result in neutrophiliA, remAins Ambiguous. In this study, we demonstrAte thAt SAA is A potent endogenous stimulAtor of grAnulocyte colony-stimulAted fActor (G-CSF), A principAl cytokine-regulAting grAnulocytosis. This effect of SAA is dependent on Toll-like receptor 2 (TLR2). Our dAtA demonstrAte thAt, in mouse mAcrophAges, both G-CSF mRNA And protein were significAntly increAsed After SAA stimulAtion. The induction of G-CSF wAs blocked by An Anti-TLR2 Antibody And mArkedly decreAsed in the TLR2-deficient mAcrophAges. SAA stimulAtion results in the ActivAtion of nucleAr fActor–κB And binding Activity to the CK-1 element of the G-CSF promoter region. In vitro reconstitution experiments Also support thAt TLR2 mediAtes SAA-induced G-CSF expression. In Addition, SAA-induced secretion of G-CSF wAs sensitive to heAt And proteinAse K treAtment, yet insensitive to polymyxin B treAtment, indicAting thAt the induction is A direct effect of SAA. FinAlly, our in vivo studies confirmed thAt SAA treAtment results in A significAnt increAse in plAsmA G-CSF And neutrophiliA, whereAs these responses Are AblAted in G-CSF– or TLR2-deficient mice.
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cutting edge tlr2 is A functionAl receptor for Acute phAse Serum Amyloid A
Journal of Immunology, 2008Co-Authors: Ni Cheng, Jun TianAbstract:Induced secretion of Acute-phAse Serum Amyloid A (SAA) is A host response to dAnger signAls And A clinicAl indicAtion of inflAmmAtion. The biologicAl functions of SAA in inflAmmAtion hAve not been fully defined, Although recent reports indicAte thAt SAA induces proinflAmmAtory cytokine expression. We now show thAt TLR2 is A functionAl receptor for SAA. HeLA cells expressing TLR2 responded to SAA with potent ActivAtion of NF-κB, which wAs enhAnced by TLR1 expression And blocked by the Toll/IL-1 receptor/resistAnce (TIR) deletion mutAnts of TLR1, TLR2, And TLR6. SAA stimulAtion led to increAsed phosphorylAtion of MAPKs And AccelerAted IκBα degrAdAtion in TLR2-HeLA cells, And results from A solid-phAse binding AssAy showed SAA interAction with the ectodomAin of TLR2. Selective reduction of SAA-induced gene expression wAs observed in tlr2 −/− mouse mAcrophAges compAred with wild-type cells. These results suggest A potentiAl role for SAA in inflAmmAtory diseAses through ActivAtion of TLR2.
Ye Ji Bang - One of the best experts on this subject based on the ideXlab platform.
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moleculAr bAsis for retinol binding by Serum Amyloid A during infection
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Ye Ji Bang, Kelly A Ruhn, Lora V HooperAbstract:Serum Amyloid A (SAA) proteins Are strongly induced in the liver by systemic infection And in the intestine by bActeriAl colonizAtion. In infected mice, SAA proteins circulAte in AssociAtion with the vitAmin A derivAtive retinol, suggesting thAt SAAs trAnsport retinol during infection. Here we illuminAte A structurAl bAsis for the retinol–SAA interAction. In the bloodstreAm of infected mice, most SAA is complexed with high-density lipoprotein (HDL). However, we found thAt the mAjority of the circulAting retinol wAs AssociAted with the smAll frAction of SAA proteins thAt circulAte without binding to HDL, thus identifying free SAA As the predominAnt retinol-binding form in vivo. We then determined the crystAl structure of retinol-bound mouse SAA3 At A resolution of 2.2 A. Retinol-bound SAA3 formed A novel Asymmetric trimeric Assembly thAt wAs generAted by the hydrophobic pAcking of the conserved AmphipAthic helices α1 And α3. This hydrophobic pAcking creAted A retinol-binding pocket in the center of the trimer, which wAs confirmed by mutAgenesis studies. Together, these findings illuminAte the moleculAr bAsis for retinol trAnsport by SAA proteins during infection.
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epitheliAl retinoic Acid receptor β regulAtes Serum Amyloid A expression And vitAmin A dependent intestinAl immunity
Proceedings of the National Academy of Sciences of the United States of America, 2019Co-Authors: Sureka Gattu, Ye Ji Bang, Kelly A Ruhn, Mihir Pendse, Chaitanya Dende, Andrew L Chara, Tamia A Harris, Yuhao Wang, Zheng Kuang, Shanthini SockanathanAbstract:VitAmin A is A dietAry component thAt is essentiAl for the development of intestinAl immunity. VitAmin A is Absorbed And converted to its bioActive derivAtives retinol And retinoic Acid by the intestinAl epithelium, yet little is known About how epitheliAl cells regulAte vitAmin A-dependent intestinAl immunity. Here we show thAt epitheliAl cell expression of the trAnscription fActor retinoic Acid receptor β (RARβ) is essentiAl for vitAmin A-dependent intestinAl immunity. EpitheliAl RARβ ActivAted vitAmin A-dependent expression of Serum Amyloid A (SAA) proteins by binding directly to SAA promoters. In AccordAnce with the known role of SAAs in regulAting Th17 cell effector function, epitheliAl RARβ promoted IL-17 production by intestinAl Th17 cells. More broAdly, epitheliAl RARβ wAs required for the development of key vitAmin A-dependent AdAptive immune responses, including CD4+ T-cell homing to the intestine And the development of IgA-producing intestinAl B cells. Our findings provide insight into how the intestinAl epithelium senses dietAry vitAmin A stAtus to regulAte AdAptive immunity, And highlight the role of epitheliAl cells in regulAting intestinAl immunity in response to diet.
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epitheliAl retinoic Acid receptor β regulAtes Serum Amyloid A expression And vitAmin A dependent intestinAl immunity
bioRxiv, 2019Co-Authors: Sureka Gattu, Ye Ji Bang, Kelly A Ruhn, Mihir Pendse, Chaitanya Dende, Andrew L Chara, Tamia A Harris, Yuhao Wang, Zheng Kuang, Shanthini SockanathanAbstract:AbstrAct VitAmin A is A dietAry component thAt is essentiAl for the development of intestinAl immunity. VitAmin A is Absorbed And converted to its bioActive derivAtives retinol And retinoic Acid by the intestinAl epithelium, yet little is known About how epitheliAl cells regulAte vitAmin A-dependent intestinAl immunity. Here we show thAt epitheliAl cell expression of the trAnscription fActor retinoic Acid receptor β (RARβ) is essentiAl for vitAmin A-dependent intestinAl immunity. EpitheliAl RARβ ActivAted vitAmin A-dependent expression of Serum Amyloid A (SAA) proteins by binding directly to SAA promoters. In AccordAnce with the known role of SAAs in regulAting Th17 cell effector function, epitheliAl RARβ promoted IL-17 production by intestinAl Th17 cells. More broAdly, epitheliAl RARβ wAs required for the development of key vitAmin A-dependent AdAptive immune responses, including CD4+ T cell homing to the intestine And the development of immunoglobulin A-producing intestinAl B cells. Our findings provide insight into how the intestinAl epithelium senses dietAry vitAmin A stAtus to regulAte AdAptive immunity And highlight the role of epitheliAl cells in regulAting intestinAl immunity in response to diet. SignificAnce StAtement VitAmin A is A nutrient thAt is essentiAl for the development of intestinAl immunity. It is Absorbed by gut epitheliAl cells which convert it to retinol And retinoic Acid. Here we show thAt the trAnscription fActor retinoic Acid receptor β (RARβ) Allows epitheliAl cells to sense vitAmin A in the diet And regulAte vitAmin A-dependent immunity in the intestine. We find thAt epitheliAl RARβ regulAtes severAl intestinAl immune responses, including production of the immunomodulAtory protein Serum Amyloid A, T cell homing to the intestine, And B cell production of immunoglobulin A. Our findings provide new insight into how epitheliAl cells sense vitAmin A to regulAte intestinAl immunity And highlight why vitAmin A is so importAnt for immunity to infection.
Alexander S. Whitehead - One of the best experts on this subject based on the ideXlab platform.
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Serum Amyloid A the mAjor vertebrAte Acute phAse reActAnt
FEBS Journal, 1999Co-Authors: Clarissa M Uhlar, Alexander S. WhiteheadAbstract:The Serum Amyloid A (SAA) fAmily comprises A number of differentiAlly expressed Apolipoproteins, Acute-phAse SAAs (A-SAAs) And constitutive SAAs (C-SAAs). A-SAAs Are mAjor Acute-phAse reActAnts, the in vivo concentrAtions of which increAse by As much As 1000-fold during inflAmmAtion. A-SAA mRNAs or proteins hAve been identified in All vertebrAtes investigAted to dAte And Are highly conserved. In contrAst, C-SAAs Are induced minimAlly, if At All, during the Acute-phAse response And hAve only been found in humAn And mouse. Although the liver is the primAry site of synthesis of both A-SAA And C-SAA, extrAhepAtic production hAs been reported for most fAmily members in most of the mAmmAliAn species studied. In vitro, the drAmAtic induction of A-SAA mRNA in response to pro-inflAmmAtory stimuli is due lArgely to the synergistic effects of cytokine signAling pAthwAys, principAlly those of the interleukin-1 And interleukin-6 type cytokines. This induction cAn be enhAnced by glucocorticoids. Studies of the A-SAA promoters in severAl mAmmAliAn species hAve identified A rAnge of trAnscription fActors thAt Are vAriously involved in defining both cytokine responsiveness And cell specificity. These include NF-κB, C/EBP, YY1, AP-2, SAF And Sp1. A-SAA is Also post-trAnscriptionAlly regulAted. Although the precise role of A-SAA in host defense during inflAmmAtion hAs not been defined, mAny potentiAl clinicAlly importAnt functions hAve been proposed for individuAl SAA fAmily members. These include involvement in lipid metAbolism/trAnsport, induction of extrAcellulAr-mAtrix-degrAding enzymes, And chemotActic recruitment of inflAmmAtory cells to sites of inflAmmAtion. A-SAA is potentiAlly involved in the pAthogenesis of severAl chronic inflAmmAtory diseAses: it is the precursor of the Amyloid A protein deposited in Amyloid A Amyloidosis, And it hAs Also been implicAted in the pAthogenesis of Atheroscelerosis And rheumAtoid Arthritis.
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regulAtion of Serum Amyloid A protein expression during the Acute phAse response
Biochemical Journal, 1998Co-Authors: Liselotte E Jensen, Alexander S. WhiteheadAbstract:The Acute-phAse (AP) Serum Amyloid A proteins (A-SAA) Are multifunctionAl Apolipoproteins which Are involved in cholesterol trAnsport And metAbolism, And in modulAting numerous immunologicAl responses during inflAmmAtion And the AP response to infection, trAumA or stress. During the AP response the hepAtic biosynthesis of A-SAA is up-regulAted by pro-inflAmmAtory cytokines, And circulAting concentrAtions cAn increAse by up to 1000-fold. ChronicAlly elevAted A-SAA concentrAtions Are A prerequisite for the pAthogenesis of secondAry Amyloidosis, A progressive And fAtAl diseAse chArActerized by the deposition in mAjor orgAns of insoluble plAques composed principAlly of proteolyticAlly cleAved A-SAA, And mAy Also contribute to physiologicAl processes thAt leAd to Atherosclerosis. There is therefore A requirement for both positive And negAtive control mechAnisms thAt permit the rApid induction of A-SAA expression until it hAs fulfilled its host-protective function(s) And subsequently ensure thAt its expression cAn be rApidly returned to bAseline. These mechAnisms include modulAtion of promoter Activity involving, for exAmple, the inducer nucleAr fActor kAppAB (NF-kAppAB) And its inhibitor IkAppAB, up-regulAtory trAnscription fActors of the nucleAr fActor for interleukin-6 (NF-IL6) fAmily And trAnscriptionAl repressors such As yin And yAng 1 (YY1). Post-trAnscriptionAl modulAtion involving chAnges in mRNA stAbility And trAnslAtion efficiency permit further up- And down-regulAtory control of A-SAA protein synthesis to be Achieved. In the lAter stAges of the AP response, A-SAA expression is effectively down-regulAted viA the increAsed production of cytokine AntAgonists such As the interleukin-1 receptor AntAgonist (IL-1RA) And of soluble cytokine receptors, resulting in less signAl trAnsduction driven by pro-inflAmmAtory cytokines.
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locAlizAtion of four humAn Serum Amyloid A sAA protein superfAmily genes to chromosome 11p chArActerizAtion of A fifth sAA relAted gene sequence
Genomics, 1993Co-Authors: Grant C Sellar, Alexander S. WhiteheadAbstract:AbstrAct The Serum Amyloid A proteins (SAAs) Are heterogeneous differentiAlly expressed Apolipoproteins of M r 12-19 kDA. Four SAA loci hAve been described. Two of the loci ( SAA1 And SAA2 ) encode Acute-phAse SAAs (ASAAs), which exhibit A drAmAtic trAnsient increAse in Serum concentrAtion in response to inflAmmAtory stimuli; A third locus ( SAA3 ) defines A pseudogene; And A fourth locus ( SAA4 ) encodes A constitutively expressed SAA (C-SAA). Using locus-specific polymerAse chAin reAction, we hAve definitively Assigned All four well-chArActerized SAA loci, SAA1, -2, -3 , And -4 , to chromosome 11p. In Addition, we hAve more fully chArActerized An ill-defined sequence previously misidentified by others As SAA4 , which Also mAps to chromosome 11p And mAy represent A fifth SAA locus.
