In vivo delivery of heat shock protein 70 accelerates wound healing by up-regulating macrophage-mediated phagocytosis
ABSTRACT Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are well‐established activators of the immune system and include heat shock proteins (HSPs), uric acid, nucleotides, High Mobility Group Box‐1 prot...
Saved in:
| Published in | Wound repair and regeneration Vol. 14; no. 2; pp. 129 - 137 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Malden, USA
Blackwell Publishing Inc
01.03.2006
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | ABSTRACT
Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are well‐established activators of the immune system and include heat shock proteins (HSPs), uric acid, nucleotides, High Mobility Group Box‐1 protein (HMGB‐1), and DNA. Here, we show that in vivo delivery of HSPs into BALB/cJ mice with full‐thickness wounds accelerates the rate of wound closure by 60% as compared with control‐treated mice. The onset is rapid and the effect is sustained, dose dependent, and protein specific. Adoptive transfer of RAW264 macrophages pretreated with HSP70 into naïve recipients with a wound transfers the HSP‐mediated effect on the rate of wound closure. Further, we demonstrate that part of the mechanism by which HSP70 accelerates wound closure is through the stimulation of macrophage‐mediated phagocytosis of wound debris. Disabling the HSP70‐mediated enhancement of phagocytosis abrogates the HSP‐mediated acceleration of the healing process. These findings create two opportunities: one, therapeutic, wherein HSP70 could be used in the clinical management of wounds; and two, pathophysiologic, to decode signals by which the host defenses recognize and respond to injury. |
|---|---|
| AbstractList | ABSTRACT
Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are well‐established activators of the immune system and include heat shock proteins (HSPs), uric acid, nucleotides, High Mobility Group Box‐1 protein (HMGB‐1), and DNA. Here, we show that in vivo delivery of HSPs into BALB/cJ mice with full‐thickness wounds accelerates the rate of wound closure by 60% as compared with control‐treated mice. The onset is rapid and the effect is sustained, dose dependent, and protein specific. Adoptive transfer of RAW264 macrophages pretreated with HSP70 into naïve recipients with a wound transfers the HSP‐mediated effect on the rate of wound closure. Further, we demonstrate that part of the mechanism by which HSP70 accelerates wound closure is through the stimulation of macrophage‐mediated phagocytosis of wound debris. Disabling the HSP70‐mediated enhancement of phagocytosis abrogates the HSP‐mediated acceleration of the healing process. These findings create two opportunities: one, therapeutic, wherein HSP70 could be used in the clinical management of wounds; and two, pathophysiologic, to decode signals by which the host defenses recognize and respond to injury. Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are well-established activators of the immune system and include heat shock proteins (HSPs), uric acid, nucleotides, High Mobility Group Box-1 protein (HMGB-1), and DNA. Here, we show that in vivo delivery of HSPs into BALB/cJ mice with full-thickness wounds accelerates the rate of wound closure by 60% as compared with control-treated mice. The onset is rapid and the effect is sustained, dose dependent, and protein specific. Adoptive transfer of RAW264 macrophages pretreated with HSP70 into naïve recipients with a wound transfers the HSP-mediated effect on the rate of wound closure. Further, we demonstrate that part of the mechanism by which HSP70 accelerates wound closure is through the stimulation of macrophage-mediated phagocytosis of wound debris. Disabling the HSP70-mediated enhancement of phagocytosis abrogates the HSP-mediated acceleration of the healing process. These findings create two opportunities: one, therapeutic, wherein HSP70 could be used in the clinical management of wounds; and two, pathophysiologic, to decode signals by which the host defenses recognize and respond to injury. Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are well-established activators of the immune system and include heat shock proteins (HSPs), uric acid, nucleotides, High Mobility Group Box-1 protein (HMGB-1), and DNA. Here, we show that in vivo delivery of HSPs into BALB-cJ mice with full-thickness wounds accelerates the rate of wound closure by 60% as compared with control-treated mice. The onset is rapid and the effect is sustained, dose dependent, and protein specific. Adoptive transfer of RAW264 macrophages pretreated with HSP70 into naive recipients with a wound transfers the HSP-mediated effect on the rate of wound closure. Further, we demonstrate that part of the mechanism by which HSP70 accelerates wound closure is through the stimulation of macrophage-mediated phagocytosis of wound debris. Disabling the HSP70-mediated enhancement of phagocytosis abrogates the HSP-mediated acceleration of the healing process. These findings create two opportunities: one, therapeutic, wherein HSP70 could be used in the clinical management of wounds; and two, pathophysiologic, to decode signals by which the host defenses recognize and respond to injury. |
| Author | Kovalchin, PhD, Joseph T. Wang, MD, PhD, Ruibo Sanders, MD, Melinda Chandawarkar, Rajiv Y. Wagh, MD, Mihir S. Azoulay, BS, Jason |
| Author_xml | – sequence: 1 givenname: Joseph T. surname: Kovalchin, PhD fullname: Kovalchin, PhD, Joseph T. organization: Center for Immunotherapy – sequence: 2 givenname: Ruibo surname: Wang, MD, PhD fullname: Wang, MD, PhD, Ruibo organization: Center for Immunotherapy – sequence: 3 givenname: Mihir S. surname: Wagh, MD fullname: Wagh, MD, Mihir S. organization: Center for Immunotherapy – sequence: 4 givenname: Jason surname: Azoulay, BS fullname: Azoulay, BS, Jason organization: Center for Immunotherapy – sequence: 5 givenname: Melinda surname: Sanders, MD fullname: Sanders, MD, Melinda organization: Department of Pathology, and – sequence: 6 givenname: Rajiv Y. surname: Chandawarkar fullname: Chandawarkar, Rajiv Y. organization: Center for Immunotherapy |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16630101$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNkUtv1DAUhS1URB_wF5BX7JJev2OJDaqYtlJbpApUxMZyHGfG00wyxMl08u9xmBEswRtfX53vWueec3TSdq1HCBPISTqX65wozjJJQOcUQOYABGi-f4XOiKA840p8P0k1SJURTdUpOo9xDQBC6OINOiVSskSQMzTetngXdh2ufBN2vp9wV-OVtwOOq849423fDT60WAG2zvnG93bwEb90Y1vNuia0S1xOeNxmvV-OjR3mxsa6vtuu7NJnG1-FhFR4fnZuGroY4lv0urZN9O-O9wX6tvj89eomu_tyfXv16S5zggHNFOOKgrSS15Y7S6i2nkldi5oqKWrgUPjKKVc6WvraQVkJ7nTBCktcpS2wC_ThMDfZ-Dn6OJhNiMlFY1vfjdFIVWhg5N9CojmXAnQSFgdhMhhj72uz7cPG9pMhYOZszNrM2Zg5GzNnY35nY_YJfX_8YyzTVv6CxzCS4ONB8BIaP_33YPP0-JiKhGcHPMTB7__gtn9OPpkS5unh2iwWmvy4p8zcsF-8nK97 |
| CitedBy_id | crossref_primary_10_1007_s12033_021_00430_8 crossref_primary_10_1016_j_jss_2006_06_003 crossref_primary_10_1097_00029330_200807020_00004 crossref_primary_10_1002_lsm_20713 crossref_primary_10_1055_s_0042_1757758 crossref_primary_10_1016_j_jaad_2009_10_048 crossref_primary_10_1016_j_biomaterials_2021_121164 crossref_primary_10_3390_ijms20030636 crossref_primary_10_1007_s12192_008_0059_8 crossref_primary_10_1016_j_aquaculture_2024_740972 crossref_primary_10_1016_j_fsi_2014_11_010 crossref_primary_10_1016_j_jinsphys_2016_10_013 crossref_primary_10_1038_s41598_020_76796_7 crossref_primary_10_1152_ajpcell_00345_2008 crossref_primary_10_1590_1981_863720210005420200017 crossref_primary_10_1007_s10620_007_9795_3 crossref_primary_10_1016_j_actbio_2017_01_056 crossref_primary_10_1152_ajpregu_00624_2007 crossref_primary_10_1189_jlb_1209779 crossref_primary_10_1007_s10522_015_9607_7 crossref_primary_10_1186_1742_2094_11_64 crossref_primary_10_3390_molecules23112846 crossref_primary_10_1016_j_jid_2023_05_002 crossref_primary_10_3390_cancers16030505 crossref_primary_10_1002_lsm_20983 crossref_primary_10_1007_s00423_008_0286_6 crossref_primary_10_1097_PRS_0b013e318199f01d crossref_primary_10_1186_1472_6882_14_136 crossref_primary_10_1371_journal_pone_0062687 crossref_primary_10_1002_wnan_1638 crossref_primary_10_1002_cbf_1739 crossref_primary_10_1016_j_yacs_2022_02_004 crossref_primary_10_1016_j_zool_2015_07_001 crossref_primary_10_1007_s12192_010_0244_4 crossref_primary_10_3390_ijms18050946 crossref_primary_10_1016_j_actbio_2021_05_043 crossref_primary_10_1042_BJ20081847 crossref_primary_10_1177_1721727X0900700201 crossref_primary_10_1016_j_placenta_2023_08_074 crossref_primary_10_1002_jcp_27397 crossref_primary_10_1111_j_1524_4725_2011_02136_x crossref_primary_10_1016_j_fsc_2020_03_006 crossref_primary_10_1016_j_vetimm_2012_07_001 crossref_primary_10_1115_1_3143030 crossref_primary_10_1111_j_1600_0846_2010_00441_x crossref_primary_10_1007_s12192_019_01001_2 crossref_primary_10_1055_s_0043_1777409 crossref_primary_10_1098_rstb_2016_0528 crossref_primary_10_1007_s12192_010_0236_4 crossref_primary_10_1016_j_mtadv_2019_100049 crossref_primary_10_1038_ni_1801 crossref_primary_10_1038_s41598_023_33799_4 crossref_primary_10_1093_hmg_ddy071 crossref_primary_10_1379_CSC_237R_1 crossref_primary_10_1111_j_1600_0846_2010_00473_x crossref_primary_10_1021_la103542y crossref_primary_10_1111_j_1742_481X_2012_01052_x crossref_primary_10_1186_1746_160X_7_22 crossref_primary_10_1002_jcp_24354 crossref_primary_10_1016_j_jphotobiol_2012_10_014 crossref_primary_10_1186_1479_5876_5_11 crossref_primary_10_1016_j_taap_2011_03_015 crossref_primary_10_1055_s_0040_1714119 crossref_primary_10_1007_s12192_015_0608_x crossref_primary_10_2353_ajpath_2008_071027 crossref_primary_10_1016_j_fsi_2017_03_024 crossref_primary_10_1111_1440_1681_12477 crossref_primary_10_3390_ijms19092795 crossref_primary_10_1111_j_1600_0765_2009_01239_x crossref_primary_10_1016_j_fsi_2023_109323 crossref_primary_10_1080_15368378_2020_1830796 crossref_primary_10_1097_ALN_0000000000000235 crossref_primary_10_2334_josnusd_52_623 |
| Cites_doi | 10.1016/S0002-9440(10)61717-8 10.1006/bbrc.1998.8216 10.1182/blood.V92.2.520 10.1182/blood.V99.10.3676 10.1177/002215549804601109 10.1128/IAI.72.5.2956-2963.2004 10.1038/355033a0 10.1016/0007-1226(95)90001-2 10.1016/S0014-2999(98)00388-4 10.1189/jlb.0802397 10.1152/physrev.1999.79.2.425 10.1292/jvms.67.111 10.1006/bbrc.1995.2386 10.1016/S1091-255X(99)80072-9 10.4049/jimmunol.160.1.361 10.1093/emboj/cdg572 10.1046/j.1432-1327.1999.00078.x 10.1016/j.cbpb.2004.04.001 10.1046/j.1524-475x.2000.00547.x 10.1038/nm1165 10.1093/emboj/cdf528 10.1002/1521-4141(200201)32:1<155::AID-IMMU155>3.0.CO;2-P 10.1089/ars.2005.7.465 10.1038/nature01991 10.1111/j.1443-9573.2004.00154.x 10.1016/S0021-9258(18)54216-2 10.1093/intimm/12.11.1539 10.1161/hc0602.103617 10.1016/S1074-7613(01)00111-X 10.1006/bbrc.1998.8286 10.1038/nri749 10.1042/bj3150497 10.1182/blood-2002-07-2261 10.1016/0955-0674(91)90125-I 10.1038/scientificamerican0593-56 10.1006/meth.1997.0464 10.1128/IAI.70.7.3759-3767.2002 10.1046/j.1524-475x.2001.00378.x 10.1038/74697 10.1016/S0165-2478(00)00294-7 10.1023/A:1008931725401 10.1007/978-3-642-59430-4_11 10.4049/jimmunol.168.6.2997 10.1096/fj.01-0776com 10.1073/pnas.260497597 10.1016/S1074-7613(02)00388-6 10.1111/j.1527-3466.2001.tb00182.x |
| ContentType | Journal Article |
| DBID | BSCLL CGR CUY CVF ECM EIF NPM AAYXX CITATION 7T5 H94 7X8 |
| DOI | 10.1111/j.1743-6109.2006.00102.x |
| DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Immunology Abstracts AIDS and Cancer Research Abstracts MEDLINE - Academic |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef AIDS and Cancer Research Abstracts Immunology Abstracts MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic CrossRef AIDS and Cancer Research Abstracts MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| EISSN | 1524-475X |
| EndPage | 137 |
| ExternalDocumentID | 10_1111_j_1743_6109_2006_00102_x 16630101 WRR102 ark_67375_WNG_FF91ZM23_H |
| Genre | article Journal Article |
| GroupedDBID | --- .3N .GA .Y3 04C 05W 0R~ 10A 123 1OB 1OC 29R 31~ 33P 36B 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52R 52S 52T 52U 52V 52W 52X 53G 5HH 5LA 5VS 66C 6PF 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A01 A03 AAESR AAEVG AAHHS AANLZ AAONW AASGY AAVGM AAWTL AAXRX AAZKR ABCQN ABCUV ABDBF ABEML ABHUG ABJNI ABPTK ABPVW ABQWH ABXGK ACAHQ ACBWZ ACCFJ ACCZN ACGFS ACGOF ACMXC ACPOU ACSCC ACXBN ACXME ACXQS ADAWD ADBTR ADDAD ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFEBI AFFPM AFGKR AFPWT AFVGU AFZJQ AGJLS AHBTC AHEFC AIACR AIURR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ATUGU AZBYB AZVAB BAFTC BDRZF BFHJK BHBCM BMXJE BROTX BRXPI BSCLL BY8 C45 CAG COF CS3 CYRXZ D-6 D-7 D-E D-F DC6 DCZOG DPXWK DR2 DRFUL DRMAN DRSTM DU5 EAD EAP EAS EBC EBD EBS ECF ECT ECV EIHBH EJD EMB EMK EMOBN ENC EPT ESX EX3 F00 F01 F04 FEDTE FUBAC FZ0 G-S G.N GODZA H.X HF~ HVGLF HZI HZ~ IHE IX1 J0M K48 KBYEO LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRMAN MRSTM MSFUL MSMAN MSSTM MXFUL MXMAN MXSTM N04 N05 N9A NF~ O66 O9- OVD P2P P2W P2X P2Z P4B P4D PALCI Q.N Q11 QB0 Q~Q R.K RIWAO RJQFR ROL RX1 SAMSI SUPJJ SV3 TEORI TUS UB1 W8V W99 WBKPD WH7 WHWMO WIH WIJ WIK WOHZO WOW WQ9 WQJ WRC WUP WVDHM WXI WXSBR XG1 YFH ZZTAW ~IA ~WT ADOJX AITYG HGLYW OIG CGR CUY CVF ECM EIF NPM AAYXX CITATION 7T5 H94 7X8 |
| ID | FETCH-LOGICAL-c5302-7347206a64fa4ca129ae369f5f2765f0408edc7cbc2befc0bd54c9838a1cd9a03 |
| IEDL.DBID | DR2 |
| ISSN | 1067-1927 |
| IngestDate | Fri Aug 16 21:21:23 EDT 2024 Fri Aug 16 09:46:28 EDT 2024 Fri Aug 23 00:43:18 EDT 2024 Sat Sep 28 07:42:59 EDT 2024 Sat Aug 24 01:01:30 EDT 2024 Wed Jan 17 05:01:55 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c5302-7347206a64fa4ca129ae369f5f2765f0408edc7cbc2befc0bd54c9838a1cd9a03 |
| Notes | istex:3E84FD690C8BEC660F278DC8C86425274E8E577D ark:/67375/WNG-FF91ZM23-H ArticleID:WRR102 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| PMID | 16630101 |
| PQID | 19446509 |
| PQPubID | 23462 |
| PageCount | 9 |
| ParticipantIDs | proquest_miscellaneous_67890310 proquest_miscellaneous_19446509 crossref_primary_10_1111_j_1743_6109_2006_00102_x pubmed_primary_16630101 wiley_primary_10_1111_j_1743_6109_2006_00102_x_WRR102 istex_primary_ark_67375_WNG_FF91ZM23_H |
| PublicationCentury | 2000 |
| PublicationDate | 2006-03 March–April 2006 2006 Mar-Apr 2006-03-00 20060301 |
| PublicationDateYYYYMMDD | 2006-03-01 |
| PublicationDate_xml | – month: 03 year: 2006 text: 2006-03 |
| PublicationDecade | 2000 |
| PublicationPlace | Malden, USA |
| PublicationPlace_xml | – name: Malden, USA – name: United States |
| PublicationTitle | Wound repair and regeneration |
| PublicationTitleAlternate | Wound Repair Regen |
| PublicationYear | 2006 |
| Publisher | Blackwell Publishing Inc |
| Publisher_xml | – name: Blackwell Publishing Inc |
| References | Cross SE, Naylor IL, Coleman RA, Teo TC. An experimental model to investigate the dynamics of wound contraction. Br J Plast Surg 1995; 48: 189-97. Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 Is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001; 14: 303-13. Berwin B, Hart JP, Rice S, Gass C, Pizzo SV, Post SR, Nicchitta CV. Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J 2003; 22: 6127-36. Low QE, Drugea IA, Duffner LA, Quinn DG, Cook DN, Rollins BJ, Kovacs EJ, DiPietro LA. Wound healing in MIP-1alpha(−/−) and MCP-1(−/−) mice. Am J Pathol 2001; 159: 457-63. Breloer M, Dorner B, More SH, Roderian T, Fleischer B, Von Bonin A. Heat shock proteins as "danger signals": eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-gamma production in T cells. Eur J Immunol 2001; 31: 2051-9. Yan LJ, Rajasekaran NS, Sathyanarayanan S, Benjamin IJ. Mouse HSF1 disruption perturbs redox state and increases mitochondrial oxidative stress in kidney. Antioxid Redox Signal 2005; 7: 465-71. Dybdahl B, Wahba A, Lien E, Flo TH, Waage A, Qureshi N, Sellevold OF, Espevik T, Sundan A. Inflammatory response after open heart surgery: release of heat-shock protein 70 and signaling through toll-like receptor-4. Circulation 2002; 105: 685-90. Shi Y, Zheng W, Rock KL. Cell injury releases endogenous adjuvants that stimulate cytotoxic T cell responses. Proc Natl Acad Sci USA 2000; 97: 14590-5. Vabulas RM, Wagner H, Schild H. Heat shock proteins as ligands of toll-like receptors. Curr Top Microbiol Immunol 2002; 270: 169-84. Lee RH, Efron DT, Tantry U, Stuelten C, Moldawer LL, Abouhamze A, Barbul A. Inhibition of tumor necrosis factor-alpha attenuates wound breaking strength in rats. Wound Rep Reg 2000; 8: 547-53. Petrof EO, Ciancio MJ, Chang EB. Role and regulation of intestinal epithelial heat shock proteins in health and disease. Chin J Dig Dis 2004; 5: 45-50. Roland CR, Nakafusa Y, Flye MW. Gadolinium chloride inhibits lipopolysaccharide-induced mortality and in vivo prostaglandin E2 release by splenic macrophages. J Gastrointest Surg 1999; 3: 301-7. Shi Y, Evans JE, Rock KL. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 2003; 425: 516-21. Radsak MP, Hilf N, Singh-Jasuja H, Braedel S, Brossart P, Rammensee HG, Schild H. The heat shock protein gp96 binds to human neutrophils and monocytes and stimulates effector functions. Blood 2003; 101: 2810-15. Angelidis CE, Lazaridis I, Pagoulatos GN. Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms. Eur J Biochem 1999; 259: 505-12. Asea A, Kraeft SK, Kurt-Jones EA, Stevenson MA, Chen LB, Finberg RW, Koo GC, Calderwood SK. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 2000; 6: 435-42. Laplante AF, Moulin V, Auger FA, Landry J, Li H, Morrow G, Tanguay RM, Germain L. Expression of heat shock proteins in mouse skin during wound healing. J Histochem Cytochem 1998; 46: 1291-301. Adding LC, Bannenberg GL, Gustafsson LE. Basic experimental studies and clinical aspects of gadolinium salts and chelates. Cardiovasc Drug Rev 2001; 19: 41-56. Srivastava PK, Menoret A, Basu S, Binder RJ, Mc Quade KL. Heat shock proteins come of age: primitive functions acquire new roles in an adaptive world. Immunity 1998; 8: 657-65. Bae JS, Jang KH, Park SC, Jin HK. Promotion of dermal wound healing by polysaccharides isolated from Phellinus gilvus in rats. J Vet Med Sci 2005; 67: 111-4. Bolger AP, Genth-Zotz S, Anker SD. Heat shock proteins and endotoxin combined as a trigger for inflammatory cytokine release during cardiopulmonary bypass: a possible third way? Circulation 2002; 106: e49-e50. Panjwani NN, Popova L, Srivastava PK. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs. J Immunol 2002; 168: 2997-3003. Bethke K, Staib F, Distler M, Schmitt U, Jonuleit H, Enk AH, Galle PR, Heike M. Different efficiency of heat shock proteins (HSP) to activate human monocytes and dendritic cells: superiority of HSP60. J Immunol 2002; 169: 6141-8. Forsdyke DR. Heat shock proteins as mediators of aggregation-induced 'danger' signals: implications of the slow evolutionary fine-tuning of sequences for the antigenicity of cancer cells. Cell Stress Chaperones 1999; 4: 205-10. Jadus MR, Williams CC, Avina MD, Ly M, Kim S, Liu Y, Narasaki R, Lowell CA, Wepsic HT. Macrophages kill T9 glioma tumor cells bearing the membrane isoform of macrophage colony stimulating factor through a phagocytosis-dependent pathway. J Immunol 1998; 160: 361-8. Hilf N, Singh-Jasuja H, Schwarzmaier P, Gouttefangeas C, Rammensee HG, Schild H. Human platelets express heat shock protein receptors and regulate dendritic cell maturation. Blood 2002; 99: 3676-82. Yan LJ, Christians ES, Liu L, Xiao X, Sohal RS, Benjamin IJ. Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage. EMBO J 2002; 21: 5164-72. Welch WJ. The role of heat-shock proteins as molecular chaperones. Curr Opin Cell Biol 1991; 3: 1033-8. Ang D, Liberek K, Skowyra D, Zylicz M, Georgopoulos C. Biological role and regulation of the universally conserved heat shock proteins. J Biol Chem 1991; 266: 24233-6. Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2002; 2: 185-94. Srivastava PK. Purification of heat shock protein-peptide complexes for use in vaccination against cancers and intracellular pathogens. Methods 1997; 12: 165-71. Teshima S, Rokutan K, Takahashi M, Nikawa T, Kishi K. Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony-stimulating factor. Biochem J 1996; 315 (Part 2): 497-504. Chen D, Androlewicz MJ. Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing. Immunol Lett 2001; 75: 143-8. Delneste Y, Magistrelli G, Gauchat J, Haeuw J, Aubry J, Nakamura K, Kawakami-Honda N, Goetsch L, Sawamura T, Bonnefoy J, Jeannin P. Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002; 17: 353-62. Shi Y, Rock KL, Zheng W. Cell death releases endogenous adjuvants that selectively enhance immune surveillance of particulate antigens. Eur J Immunol 2002; 32: 155-62. Reynolds LE, Conti FJ, Lucas M, Grose R, Robinson S, Stone M, Saunders G, Dickson C, Hynes RO, Lacy-Hulbert A, Hodivala-Dilke K. Accelerated re-epithelialization in beta3-integrin-deficient- mice is associated with enhanced TGF-beta1 signaling. Nat Med 2005; 11: 167-74. Yamamura I, Hirata H, Hosokawa N, Nagata K. Transcriptional activation of the mouse HSP47 gene in mouse osteoblast MC3T3-E1 cells by TGF-beta 1. Biochem Biophys Res Commun 1998; 244: 68-74. Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992; 355: 33-45. Byrne CR, Hanson PJ. Induction of heat shock protein 72 by a nitric oxide donor in guinea-pig gastric mucosal cells. Eur J Pharmacol 1998; 353: 117-22. Lin ZQ, Kondo T, Ishida Y, Takayasu T, Mukaida N. Essential involvement of IL-6 in the skin wound-healing process as evidenced by delayed wound healing in IL-6-deficient mice. J Leukoc Biol 2003; 73: 713-21. Christians ES, Yan LJ, Benjamin IJ. Heat shock factor 1 and heat shock proteins: critical partners in protection against acute cell injury. Crit Care Med 2002; 30: S43-S50. Feder ME, Hofmann GE. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 1999; 61: 243-82. Fink AL. Chaperone-mediated protein folding. Physiol Rev 1999; 79: 425-49. Oberringer M, Baum HP, Jung V, Welter C, Frank J, Kuhlmann M, Mutschler W, Hanselmann RG. Differential expression of heat shock protein 70 in well healing and chronic human wound tissue. Biochem Biophys Res Commun 1995; 214: 1009-14. Mori R, Kondo T, Ohshima T, Ishida Y, Mukaida N. Accelerated wound healing in tumor necrosis factor receptor p55-deficient mice with reduced leukocyte infiltration. FASEB J 2002; 16: 963-74. Binder RJ, Han DK, Srivastava PK. CD91: a receptor for heat shock protein gp96. Nat Immunol 2000; 1: 151-5. Gordon CB, Li DG, Stagg CA, Manson P, Udelsman R. Impaired wound healing in Cushing's syndrome: the role of heat shock proteins. Surgery 1994; 116: 1082-7. Deepe GS Jr., Gibbons RS. Cellular and molecular regulation of vaccination with heat shock protein 60 from Histoplasma capsulatum. Infect Immun 2002; 70: 3759-67. Kondo H, Watabe S. Temperature-dependent enhancement of cell proliferation and mRNA expression for type I collagen and HSP70 in primary cultured goldfish cells. Comp Biochem Physiol A Mol Integr Physiol 2004; 138: 221-8. Klosterhalfen B, Klinge U, Tietze L, Henze U, Muys L, Mittermayer C, Bhardwaj RS. Expression of heat shock protein 70 (HSP70) at the interface of polymer-implants in vivo. J Mater Sci Mater Med 2000; 11: 175-81. Keagle JN, Welch WJ, Young DM. Expression of heat shock proteins in a linear rodent wound. Wound Rep Reg 2001; 9: 378-85. Shukla A, Dubey MP, Srivastava R, Srivastava BS. Differential expression of proteins during healing of cutaneous wounds in experimental normal and chronic models. Biochem Biophys Res Commun 1998; 244: 434-9. Shi J, Kokubo Y, Wake K. Expression of P-selectin on hepatic endothelia and platelets promoting neutrophil removal by liver macrophages. Blood 1998; 92: 520-8. Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 2000; 12: 1539-46. Goldmann O, Rohde M, Chhatwal GS, Medina E. Role of macrophages in host resistance to group A streptococci. Infect Immun 2004; 72: 2956-23. Welch WJ. How cells respond to str 2002; 16 2002; 17 1998; 160 2002; 270 2000; 6 2000; 8 2002; 99 1995; 214 2004; 5 2000; 1 1998; 353 2005; 67 1998; 46 2004; 72 2004; 138 1991; 266 2000; 12 1992; 355 2000; 11 2000; 97 1997; 12 2001; 19 2002; 106 2002; 105 1998; 92 2001; 14 1998; 244 1999; 259 1991; 3 1994; 116 2002; 30 2002; 32 2002; 2 1999; 4 1999; 3 1999; 61 1993; 268 2003; 73 2003; 425 1995; 48 2002; 168 2002; 169 2001; 9 2002; 21 1999; 79 2005; 7 2002; 70 2003; 101 2001; 159 2005; 11 2001; 31 2003; 22 2001; 75 1996; 315 1998; 8 e_1_2_6_53_2 Bethke K (e_1_2_6_52_2) 2002; 169 e_1_2_6_30_2 e_1_2_6_19_2 Teshima S (e_1_2_6_54_2) 1996; 315 e_1_2_6_13_2 e_1_2_6_34_2 e_1_2_6_11_2 e_1_2_6_32_2 e_1_2_6_17_2 e_1_2_6_38_2 e_1_2_6_55_2 e_1_2_6_15_2 e_1_2_6_36_2 e_1_2_6_57_2 e_1_2_6_20_2 e_1_2_6_41_2 Bolger AP (e_1_2_6_51_2) 2002; 106 Srivastava PK (e_1_2_6_16_2) 1998; 8 e_1_2_6_9_2 e_1_2_6_3_2 e_1_2_6_5_2 e_1_2_6_24_2 e_1_2_6_47_2 e_1_2_6_22_2 e_1_2_6_49_2 e_1_2_6_28_2 e_1_2_6_43_2 e_1_2_6_26_2 e_1_2_6_50_2 e_1_2_6_31_2 Gordon CB (e_1_2_6_18_2) 1994; 116 Forsdyke DR. (e_1_2_6_7_2) 1999; 4 Christians ES (e_1_2_6_45_2) 2002; 30 Binder RJ (e_1_2_6_8_2) 2000; 1 Feder ME (e_1_2_6_42_2) 1999; 61 e_1_2_6_12_2 e_1_2_6_35_2 e_1_2_6_58_2 e_1_2_6_10_2 e_1_2_6_33_2 e_1_2_6_39_2 e_1_2_6_14_2 e_1_2_6_37_2 e_1_2_6_56_2 Jadus MR (e_1_2_6_29_2) 1998; 160 e_1_2_6_40_2 Breloer M (e_1_2_6_6_2) 2001; 31 e_1_2_6_4_2 e_1_2_6_23_2 e_1_2_6_48_2 e_1_2_6_2_2 e_1_2_6_21_2 e_1_2_6_27_2 e_1_2_6_44_2 e_1_2_6_25_2 e_1_2_6_46_2 |
| References_xml | – volume: 3 start-page: 1033 year: 1991 end-page: 8 article-title: The role of heat‐shock proteins as molecular chaperones publication-title: Curr Opin Cell Biol – volume: 1 start-page: 151 year: 2000 end-page: 5 article-title: CD91 publication-title: a receptor for heat shock protein gp96 – volume: 46 start-page: 1291 year: 1998 end-page: 301 article-title: Expression of heat shock proteins in mouse skin during wound healing publication-title: J Histochem Cytochem – volume: 70 start-page: 3759 year: 2002 end-page: 67 article-title: Cellular and molecular regulation of vaccination with heat shock protein 60 from Histoplasma capsulatum publication-title: Infect Immun – volume: 61 start-page: 243 year: 1999 end-page: 82 article-title: Heat‐shock proteins, molecular chaperones, and the stress response publication-title: evolutionary and ecological physiology – volume: 21 start-page: 5164 year: 2002 end-page: 72 article-title: Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage publication-title: EMBO J – volume: 105 start-page: 685 year: 2002 end-page: 90 article-title: Inflammatory response after open heart surgery: release of heat‐shock protein 70 and signaling through toll‐like receptor‐4 publication-title: Circulation – volume: 214 start-page: 1009 year: 1995 end-page: 14 article-title: Differential expression of heat shock protein 70 in well healing and chronic human wound tissue publication-title: Biochem Biophys Res Commun – volume: 425 start-page: 516 year: 2003 end-page: 21 article-title: Molecular identification of a danger signal that alerts the immune system to dying cells publication-title: Nature – volume: 48 start-page: 189 year: 1995 end-page: 97 article-title: An experimental model to investigate the dynamics of wound contraction publication-title: Br J Plast Surg – volume: 14 start-page: 303 year: 2001 end-page: 13 article-title: CD91 Is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin publication-title: Immunity – volume: 355 start-page: 33 year: 1992 end-page: 45 article-title: Protein folding in the cell publication-title: Nature – volume: 268 start-page: 56 year: 1993 end-page: 64 article-title: How cells respond to stress publication-title: Sci Am – volume: 259 start-page: 505 year: 1999 end-page: 12 article-title: Aggregation of hsp70 and hsc70 in vivo is distinct and temperature‐dependent and their chaperone function is directly related to non‐aggregated forms publication-title: Eur J Biochem – volume: 244 start-page: 434 year: 1998 end-page: 9 article-title: Differential expression of proteins during healing of cutaneous wounds in experimental normal and chronic models publication-title: Biochem Biophys Res Commun – volume: 8 start-page: 657 year: 1998 end-page: 65 article-title: Heat shock proteins come of age publication-title: primitive functions acquire new roles in an adaptive world – volume: 12 start-page: 165 year: 1997 end-page: 71 article-title: Purification of heat shock protein‐peptide complexes for use in vaccination against cancers and intracellular pathogens publication-title: Methods – volume: 92 start-page: 520 year: 1998 end-page: 8 article-title: Expression of P‐selectin on hepatic endothelia and platelets promoting neutrophil removal by liver macrophages publication-title: Blood – volume: 2 start-page: 185 year: 2002 end-page: 94 article-title: Roles of heat‐shock proteins in innate and adaptive immunity publication-title: Nat Rev Immunol – volume: 73 start-page: 713 year: 2003 end-page: 21 article-title: Essential involvement of IL‐6 in the skin wound‐healing process as evidenced by delayed wound healing in IL‐6‐deficient mice publication-title: J Leukoc Biol – volume: 31 start-page: 2051 year: 2001 end-page: 9 article-title: Heat shock proteins as “danger signals” publication-title: eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-gamma production in T cells – volume: 169 start-page: 6141 year: 2002 end-page: 8 article-title: Different efficiency of heat shock proteins (HSP) to activate human monocytes and dendritic cells publication-title: superiority of HSP60 – volume: 266 start-page: 24233 year: 1991 end-page: 6 article-title: Biological role and regulation of the universally conserved heat shock proteins publication-title: J Biol Chem – volume: 67 start-page: 111 year: 2005 end-page: 4 article-title: Promotion of dermal wound healing by polysaccharides isolated from Phellinus gilvus in rats publication-title: J Vet Med Sci – volume: 159 start-page: 457 year: 2001 end-page: 63 article-title: Wound healing in MIP‐1alpha(−/−) and MCP‐1(−/−) mice publication-title: Am J Pathol – volume: 4 start-page: 205 year: 1999 end-page: 10 article-title: Heat shock proteins as mediators of aggregation‐induced ‘danger’ signals publication-title: implications of the slow evolutionary fine-tuning of sequences for the antigenicity of cancer cells – volume: 116 start-page: 1082 year: 1994 end-page: 7 article-title: Impaired wound healing in Cushing's syndrome publication-title: the role of heat shock proteins – volume: 30 start-page: S43 year: 2002 end-page: S50 article-title: Heat shock factor 1 and heat shock proteins publication-title: critical partners in protection against acute cell injury – volume: 315 start-page: 497 issue: (Part 2) year: 1996 end-page: 504 article-title: Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony‐stimulating factor publication-title: Biochem J – volume: 22 start-page: 6127 year: 2003 end-page: 36 article-title: Scavenger receptor‐A mediates gp96/GRP94 and calreticulin internalization by antigen‐presenting cells publication-title: EMBO J – volume: 168 start-page: 2997 year: 2002 end-page: 3003 article-title: Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs publication-title: J Immunol – volume: 11 start-page: 167 year: 2005 end-page: 74 article-title: Accelerated re‐epithelialization in beta3‐integrin‐deficient‐ mice is associated with enhanced TGF‐beta1 signaling publication-title: Nat Med – volume: 79 start-page: 425 year: 1999 end-page: 49 article-title: Chaperone‐mediated protein folding publication-title: Physiol Rev – volume: 97 start-page: 14590 year: 2000 end-page: 5 article-title: Cell injury releases endogenous adjuvants that stimulate cytotoxic T cell responses publication-title: Proc Natl Acad Sci USA – volume: 7 start-page: 465 year: 2005 end-page: 71 article-title: Mouse HSF1 disruption perturbs redox state and increases mitochondrial oxidative stress in kidney publication-title: Antioxid Redox Signal – volume: 101 start-page: 2810 year: 2003 end-page: 15 article-title: The heat shock protein gp96 binds to human neutrophils and monocytes and stimulates effector functions publication-title: Blood – volume: 8 start-page: 547 year: 2000 end-page: 53 article-title: Inhibition of tumor necrosis factor‐alpha attenuates wound breaking strength in rats publication-title: Wound Rep Reg – volume: 9 start-page: 378 year: 2001 end-page: 85 article-title: Expression of heat shock proteins in a linear rodent wound publication-title: Wound Rep Reg – volume: 75 start-page: 143 year: 2001 end-page: 8 article-title: Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing publication-title: Immunol Lett – volume: 160 start-page: 361 year: 1998 end-page: 8 article-title: Macrophages kill T9 glioma tumor cells bearing the membrane isoform of macrophage colony stimulating factor through a phagocytosis‐dependent pathway publication-title: J Immunol – volume: 11 start-page: 175 year: 2000 end-page: 81 article-title: Expression of heat shock protein 70 (HSP70) at the interface of polymer‐implants in vivo publication-title: J Mater Sci Mater Med – volume: 17 start-page: 353 year: 2002 end-page: 62 article-title: Involvement of LOX‐1 in dendritic cell‐mediated antigen cross‐presentation publication-title: Immunity – volume: 12 start-page: 1539 year: 2000 end-page: 46 article-title: Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF‐kappa B pathway publication-title: Int Immunol – volume: 99 start-page: 3676 year: 2002 end-page: 82 article-title: Human platelets express heat shock protein receptors and regulate dendritic cell maturation publication-title: Blood – volume: 5 start-page: 45 year: 2004 end-page: 50 article-title: Role and regulation of intestinal epithelial heat shock proteins in health and disease publication-title: Chin J Dig Dis – volume: 6 start-page: 435 year: 2000 end-page: 42 article-title: HSP70 stimulates cytokine production through a CD14‐dependant pathway, demonstrating its dual role as a chaperone and cytokine publication-title: Nat Med – volume: 244 start-page: 68 year: 1998 end-page: 74 article-title: Transcriptional activation of the mouse HSP47 gene in mouse osteoblast MC3T3‐E1 cells by TGF‐beta 1 publication-title: Biochem Biophys Res Commun – volume: 270 start-page: 169 year: 2002 end-page: 84 article-title: Heat shock proteins as ligands of toll‐like receptors publication-title: Curr Top Microbiol Immunol – volume: 138 start-page: 221 year: 2004 end-page: 8 article-title: Temperature‐dependent enhancement of cell proliferation and mRNA expression for type I collagen and HSP70 in primary cultured goldfish cells publication-title: Comp Biochem Physiol A Mol Integr Physiol – volume: 16 start-page: 963 year: 2002 end-page: 74 article-title: Accelerated wound healing in tumor necrosis factor receptor p55‐deficient mice with reduced leukocyte infiltration publication-title: FASEB J – volume: 353 start-page: 117 year: 1998 end-page: 22 article-title: Induction of heat shock protein 72 by a nitric oxide donor in guinea‐pig gastric mucosal cells publication-title: Eur J Pharmacol – volume: 106 start-page: e49 year: 2002 end-page: e50 article-title: Heat shock proteins and endotoxin combined as a trigger for inflammatory cytokine release during cardiopulmonary bypass publication-title: a possible third way? – volume: 3 start-page: 301 year: 1999 end-page: 7 article-title: Gadolinium chloride inhibits lipopolysaccharide‐induced mortality and in vivo prostaglandin E2 release by splenic macrophages publication-title: J Gastrointest Surg – volume: 32 start-page: 155 year: 2002 end-page: 62 article-title: Cell death releases endogenous adjuvants that selectively enhance immune surveillance of particulate antigens publication-title: Eur J Immunol – volume: 72 start-page: 2956 year: 2004 end-page: 23 article-title: Role of macrophages in host resistance to group A streptococci publication-title: Infect Immun – volume: 19 start-page: 41 year: 2001 end-page: 56 article-title: Basic experimental studies and clinical aspects of gadolinium salts and chelates publication-title: Cardiovasc Drug Rev – ident: e_1_2_6_34_2 doi: 10.1016/S0002-9440(10)61717-8 – ident: e_1_2_6_55_2 doi: 10.1006/bbrc.1998.8216 – volume: 116 start-page: 1082 year: 1994 ident: e_1_2_6_18_2 article-title: Impaired wound healing in Cushing's syndrome publication-title: the role of heat shock proteins contributor: fullname: Gordon CB – ident: e_1_2_6_31_2 doi: 10.1182/blood.V92.2.520 – ident: e_1_2_6_48_2 doi: 10.1182/blood.V99.10.3676 – volume: 8 start-page: 657 year: 1998 ident: e_1_2_6_16_2 article-title: Heat shock proteins come of age publication-title: primitive functions acquire new roles in an adaptive world contributor: fullname: Srivastava PK – ident: e_1_2_6_20_2 doi: 10.1177/002215549804601109 – ident: e_1_2_6_28_2 doi: 10.1128/IAI.72.5.2956-2963.2004 – ident: e_1_2_6_15_2 doi: 10.1038/355033a0 – ident: e_1_2_6_24_2 doi: 10.1016/0007-1226(95)90001-2 – ident: e_1_2_6_40_2 doi: 10.1016/S0014-2999(98)00388-4 – ident: e_1_2_6_33_2 doi: 10.1189/jlb.0802397 – ident: e_1_2_6_43_2 doi: 10.1152/physrev.1999.79.2.425 – ident: e_1_2_6_25_2 doi: 10.1292/jvms.67.111 – volume: 61 start-page: 243 year: 1999 ident: e_1_2_6_42_2 article-title: Heat‐shock proteins, molecular chaperones, and the stress response publication-title: evolutionary and ecological physiology contributor: fullname: Feder ME – ident: e_1_2_6_19_2 doi: 10.1006/bbrc.1995.2386 – ident: e_1_2_6_30_2 doi: 10.1016/S1091-255X(99)80072-9 – volume: 160 start-page: 361 year: 1998 ident: e_1_2_6_29_2 article-title: Macrophages kill T9 glioma tumor cells bearing the membrane isoform of macrophage colony stimulating factor through a phagocytosis‐dependent pathway publication-title: J Immunol doi: 10.4049/jimmunol.160.1.361 contributor: fullname: Jadus MR – ident: e_1_2_6_10_2 doi: 10.1093/emboj/cdg572 – ident: e_1_2_6_38_2 doi: 10.1046/j.1432-1327.1999.00078.x – ident: e_1_2_6_44_2 doi: 10.1016/j.cbpb.2004.04.001 – ident: e_1_2_6_32_2 doi: 10.1046/j.1524-475x.2000.00547.x – ident: e_1_2_6_56_2 doi: 10.1038/nm1165 – ident: e_1_2_6_47_2 doi: 10.1093/emboj/cdf528 – ident: e_1_2_6_3_2 doi: 10.1002/1521-4141(200201)32:1<155::AID-IMMU155>3.0.CO;2-P – ident: e_1_2_6_46_2 doi: 10.1089/ars.2005.7.465 – ident: e_1_2_6_23_2 doi: 10.1038/nature01991 – volume: 169 start-page: 6141 year: 2002 ident: e_1_2_6_52_2 article-title: Different efficiency of heat shock proteins (HSP) to activate human monocytes and dendritic cells publication-title: superiority of HSP60 contributor: fullname: Bethke K – ident: e_1_2_6_57_2 doi: 10.1111/j.1443-9573.2004.00154.x – volume: 4 start-page: 205 year: 1999 ident: e_1_2_6_7_2 article-title: Heat shock proteins as mediators of aggregation‐induced ‘danger’ signals publication-title: implications of the slow evolutionary fine-tuning of sequences for the antigenicity of cancer cells contributor: fullname: Forsdyke DR. – ident: e_1_2_6_39_2 doi: 10.1016/S0021-9258(18)54216-2 – ident: e_1_2_6_53_2 doi: 10.1093/intimm/12.11.1539 – ident: e_1_2_6_49_2 doi: 10.1161/hc0602.103617 – ident: e_1_2_6_13_2 doi: 10.1016/S1074-7613(01)00111-X – ident: e_1_2_6_21_2 doi: 10.1006/bbrc.1998.8286 – volume: 30 start-page: S43 year: 2002 ident: e_1_2_6_45_2 article-title: Heat shock factor 1 and heat shock proteins publication-title: critical partners in protection against acute cell injury contributor: fullname: Christians ES – ident: e_1_2_6_14_2 doi: 10.1038/nri749 – volume: 315 start-page: 497 issue: 2 year: 1996 ident: e_1_2_6_54_2 article-title: Induction of heat shock proteins and their possible roles in macrophages during activation by macrophage colony‐stimulating factor publication-title: Biochem J doi: 10.1042/bj3150497 contributor: fullname: Teshima S – ident: e_1_2_6_12_2 doi: 10.1182/blood-2002-07-2261 – volume: 31 start-page: 2051 year: 2001 ident: e_1_2_6_6_2 article-title: Heat shock proteins as “danger signals” publication-title: eukaryotic Hsp60 enhances and accelerates antigen-specific IFN-gamma production in T cells contributor: fullname: Breloer M – ident: e_1_2_6_36_2 doi: 10.1016/0955-0674(91)90125-I – ident: e_1_2_6_37_2 doi: 10.1038/scientificamerican0593-56 – ident: e_1_2_6_22_2 doi: 10.1006/meth.1997.0464 – ident: e_1_2_6_50_2 doi: 10.1128/IAI.70.7.3759-3767.2002 – ident: e_1_2_6_17_2 doi: 10.1046/j.1524-475x.2001.00378.x – ident: e_1_2_6_35_2 doi: 10.1038/74697 – volume: 1 start-page: 151 year: 2000 ident: e_1_2_6_8_2 article-title: CD91 publication-title: a receptor for heat shock protein gp96 contributor: fullname: Binder RJ – ident: e_1_2_6_41_2 doi: 10.1016/S0165-2478(00)00294-7 – ident: e_1_2_6_58_2 doi: 10.1023/A:1008931725401 – ident: e_1_2_6_11_2 doi: 10.1007/978-3-642-59430-4_11 – ident: e_1_2_6_5_2 doi: 10.4049/jimmunol.168.6.2997 – ident: e_1_2_6_26_2 doi: 10.1096/fj.01-0776com – ident: e_1_2_6_2_2 doi: 10.1093/intimm/12.11.1539 – ident: e_1_2_6_4_2 doi: 10.1073/pnas.260497597 – ident: e_1_2_6_9_2 doi: 10.1016/S1074-7613(02)00388-6 – ident: e_1_2_6_27_2 doi: 10.1111/j.1527-3466.2001.tb00182.x – volume: 106 start-page: e49 year: 2002 ident: e_1_2_6_51_2 article-title: Heat shock proteins and endotoxin combined as a trigger for inflammatory cytokine release during cardiopulmonary bypass publication-title: a possible third way? contributor: fullname: Bolger AP |
| SSID | ssj0005598 |
| Score | 2.1445491 |
| Snippet | ABSTRACT
Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are... Injury causes tissue breakdown, which releases large quantities of intracellular contents into the extracellular space. Some of these materials are... |
| SourceID | proquest crossref pubmed wiley istex |
| SourceType | Aggregation Database Index Database Publisher |
| StartPage | 129 |
| SubjectTerms | Animals Cells, Cultured Chemokine CCL2 - metabolism Female HSP70 Heat-Shock Proteins - pharmacology HSP90 Heat-Shock Proteins - pharmacology Interleukin-6 - metabolism Macrophages - drug effects Membrane Glycoproteins - pharmacology Mice Mice, Inbred BALB C Phagocytosis - drug effects Tumor Necrosis Factor-alpha - metabolism Up-Regulation Wound Healing - drug effects |
| Title | In vivo delivery of heat shock protein 70 accelerates wound healing by up-regulating macrophage-mediated phagocytosis |
| URI | https://api.istex.fr/ark:/67375/WNG-FF91ZM23-H/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1743-6109.2006.00102.x https://www.ncbi.nlm.nih.gov/pubmed/16630101 https://search.proquest.com/docview/19446509 https://search.proquest.com/docview/67890310 |
| Volume | 14 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1La9wwEBYlueTSB0lb96lD6c2LVrYs-1hKtttCclgaEnoRejbLEjusd9NsT_0J_Y35JZmRdzfZkEIpxRcjJGFJM6PP0sw3hLwDyC19KXTqeCXTPBiTAjiyKbeaGWazksccSweHxfAo_3IiTpb-TxgL0_FDrA_cUDOivUYF16bdVHKk10S68PWdAuM9xJPIq4f4aHTDJIU85PHiE-wCgBp516nnno42dqptnPTL-2DoJqqN29LgEZmsBtR5o0x685np2Z93uB7_z4gfk4dL9Eo_dOL2hDzw9S5ZfK7pxfiioQ76B81Y0CZQtPG0PQVrSyMVxLimklFtLWxzyE7R0h-Y0AnrYUA8NQs6P7_69Xvqv8eEYlB0pjG92CkYPCiPES6AjikWNHYxa9pxu0eOBvtfPw7TZUaH1GJ2olRmueSs0EUedG41YA3ts6IKInBZiAAGpfTOSmssNz5YZpzIbVVmpe5bV2mWPSVbdVP754SyIriS5547E3LvhIbHM6u5dlLYQiekv1o9dd4Rd6hbPzwwkQonEtNwRsc-xtVlQt7HZV430NMJOr5JoY4PP6nBoOp_O-CZGibk7UoOFKgj3rHo2jfzVvUrZKBj1Z9rFBh6DKA6Ic86Abr5PEB_SPmXEBHF4K-_Wx2PRvDy4h_bvSQ73cESeta9Iluz6dy_Bqg1M2-iEl0DtMAeGg |
| link.rule.ids | 315,786,790,1382,27957,27958,46329,46753 |
| linkProvider | Wiley-Blackwell |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Pb9MwFLfQdoALA_EvGzAfELdUrhPHyREhug7WHqpNm7hYtmOzapBMTbutnPgIfEY-yd5z2o5OQ0II5RJZduJ_7_ln-73fI-QNQG7pcqHjkhcyTr0xMYAjG3OrmWE2yXmIsTQYZv2j9OOJOFmEA0JfmJYfYnXghpIR9DUKOB5Ir0s58msiX_jqUoHxDgDKTZB-EfZXoxsuKWQiD1efoBkA1sjbZj13fGltrdrEbr-6C4iu49qwMPW2yNdlk1p7lLPObGo69vsttsf_1OZH5OECwNJ37Yx7TO656gmZ71f0YnxR0xJ-AMIxp7WnqOZpcwoKlwY2iHFFJaPaWljpkKCioZcY0wnzoU88NXM6O__14-fEfQkxxSDpm8YIY6eg8yA9OLkAQKaYUNv5tG7GzVNy1Ptw-L4fL4I6xBYDFMUySSVnmc5Sr1OrAW5ol2SFF57LTHjQKbkrrbTGcuO8ZaYUqS3yJNddWxaaJc_IRlVX7gWhLPNlzlPHS-NTVwoNj2NWc11KYTMdke5y-NR5y92hftvzQEcq7EiMxBls-xhXVxF5G8Z5VUBPztD2TQp1PNxTvV7R_TzgiepHZHc5ERRIJF6z6MrVs0Z1CyShY8Wfc2TofQy4OiLP2xl0Uz0AgMj6FxER5sFf11sdj0bwsv2P5XbJ_f7h4EAd7A8_7ZAH7TkTGtq9JBvTycy9AuQ1Na-DRF0DoaAiPA |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1LbxMxELZQKyEuPMRredUHxG0jx_vw7hFRlhRohCKqVlwsP2kUsRtlk9Jw4ifwG_klzHiTlFRFQgjtZWXZ1tqeGX9rz3xDyHOA3MIVmYotL0Wceq1jAEcm5kYxzUxS8JBj6XCYD47StyfZycr_CWNhOn6IzYEbakaw16jgU-u3lRzpNZEufHOnwHgP8ORumiccJXx_dEElhUTk4eYTDAOgGnHZq-eKnra2ql2c9fOrcOg2rA37UnWLTNYj6txRJr3FXPfMt0tkj_9nyLfJzRV8pS87ebtDrrn6Llke1PRsfNZQC_2Daixp4ykaedqegrmlgQtiXFPBqDIG9jmkp2jpV8zohPUwIp7qJV1Mf37_MXOfQ0YxKPqiML_YKVg8KA8hLgCPKRY0Zjlv2nF7jxxVrz--GsSrlA6xwfREsUhSwVmu8tSr1CgAG8oleekzz0WeebAohbNGGG24dt4wbbPUlEVSqL6xpWLJfbJTN7V7SCjLvS146rjVPnU2U_A4ZhRXVmQmVxHpr1dPTjvmDvnbHw9MpMSJxDycwbOPcXkekRdhmTcN1GyCnm8ik8fDN7Kqyv6nQ57IQUT21nIgQR_xkkXVrlm0sl8iBR0r_1wjx9hjQNURedAJ0MXnAfxDzr-IZEEM_vq75fFoBC-P_rHdHrn-Yb-S7w-G7x6TG90hE3rZPSE789nCPQXYNdfPgj79AhrTIOs |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=In+vivo+delivery+of+heat+shock+protein+70+accelerates+wound+healing+by+up%E2%80%90regulating+macrophage%E2%80%90mediated+phagocytosis&rft.jtitle=Wound+repair+and+regeneration&rft.au=Kovalchin%2C+PhD%2C+Joseph+T.&rft.au=Wang%2C+MD%2C+PhD%2C+Ruibo&rft.au=Wagh%2C+MD%2C+Mihir+S.&rft.au=Azoulay%2C+BS%2C+Jason&rft.date=2006-03-01&rft.pub=Blackwell+Publishing+Inc&rft.issn=1067-1927&rft.eissn=1524-475X&rft.volume=14&rft.issue=2&rft.spage=129&rft.epage=137&rft_id=info:doi/10.1111%2Fj.1743-6109.2006.00102.x&rft.externalDBID=10.1111%252Fj.1743-6109.2006.00102.x&rft.externalDocID=WRR102 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1067-1927&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1067-1927&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1067-1927&client=summon |