Leptin signaling impairs macrophage defenses against Salmonella Typhimurium

The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being increasingly appreciated. However, the potential of master regulators of metabolism to control innate immunity are less understood. Here, we s...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 116; no. 33; pp. 16551 - 16560
Main Authors Fischer, Julia, Gutièrrez, Saray, Ganesan, Raja, Calabrese, Chiara, Ranjan, Rajeev, Cildir, Gökhan, Hos, Nina Judith, Rybniker, Jan, Wolke, Martina, Fries, Jochen W. U., Tergaonkar, Vinay, Plum, Georg, Antebi, Adam, Robinson, Nirmal
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 13.08.2019
SeriesPNAS Plus
Subjects
Online AccessGet full text

Cover

Loading…
Abstract The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being increasingly appreciated. However, the potential of master regulators of metabolism to control innate immunity are less understood. Here, we studied the cross-talk between leptin signaling and macrophage function in the context of bacterial infections. We found that upon infection with Gram-negative pathogens, such as Salmonella Typhimurium, leptin receptor (Lepr) expression increased in both mouse and human macrophages. Unexpectedly, both genetic Lepr ablation in macrophages and global pharmacologic leptin antagonization augmented lysosomal functions, reduced S. Typhimurium burden, and diminished inflammation in vitro and in vivo. Mechanistically, we show that leptin induction activates the mTORC2/Akt pathway and subsequently down-regulates Phlpp1 phosphatase, allowing for phosphorylated Akt to impair lysosomal-mediated pathogen clearance. These data highlight a link between leptin signaling, the mTORC2/Phlpp1/Akt axis, and lysosomal activity in macrophages and have important therapeutic implications for modulating innate immunity to combat Gram-negative bacterial infections.
AbstractList The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being increasingly appreciated. However, the potential of master regulators of metabolism to control innate immunity are less understood. Here, we studied the cross-talk between leptin signaling and macrophage function in the context of bacterial infections. We found that upon infection with Gram-negative pathogens, such as Salmonella Typhimurium, leptin receptor (Lepr) expression increased in both mouse and human macrophages. Unexpectedly, both genetic Lepr ablation in macrophages and global pharmacologic leptin antagonization augmented lysosomal functions, reduced S. Typhimurium burden, and diminished inflammation in vitro and in vivo. Mechanistically, we show that leptin induction activates the mTORC2/Akt pathway and subsequently down-regulates Phlpp1 phosphatase, allowing for phosphorylated Akt to impair lysosomal-mediated pathogen clearance. These data highlight a link between leptin signaling, the mTORC2/Phlpp1/Akt axis, and lysosomal activity in macrophages and have important therapeutic implications for modulating innate immunity to combat Gram-negative bacterial infections.
The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being increasingly appreciated. However, the potential of master regulators of metabolism to control innate immunity are less understood. Here, we studied the cross-talk between leptin signaling and macrophage function in the context of bacterial infections. We found that upon infection with Gram-negative pathogens, such as Typhimurium, leptin receptor (Lepr) expression increased in both mouse and human macrophages. Unexpectedly, both genetic ablation in macrophages and global pharmacologic leptin antagonization augmented lysosomal functions, reduced Typhimurium burden, and diminished inflammation in vitro and in vivo. Mechanistically, we show that leptin induction activates the mTORC2/Akt pathway and subsequently down-regulates Phlpp1 phosphatase, allowing for phosphorylated Akt to impair lysosomal-mediated pathogen clearance. These data highlight a link between leptin signaling, the mTORC2/Phlpp1/Akt axis, and lysosomal activity in macrophages and have important therapeutic implications for modulating innate immunity to combat Gram-negative bacterial infections.
In the present study, we identify and describe an important cross-talk between leptin signaling and macrophage functions in the context of Salmonella Typhimurium infection. Genetic ablation of leptin receptor or pharmacological antagonization of leptin augmented lysosomal functions in macrophages, reduced S. Typhimurium burden, and diminished inflammation both in vitro and in vivo. Leptin signaling activates mTORC2/Akt pathway through the down-regulation of Phlpp1 phosphatase, thus impairs lysosome-mediated pathogen clearance. The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being increasingly appreciated. However, the potential of master regulators of metabolism to control innate immunity are less understood. Here, we studied the cross-talk between leptin signaling and macrophage function in the context of bacterial infections. We found that upon infection with Gram-negative pathogens, such as Salmonella Typhimurium, leptin receptor (Lepr) expression increased in both mouse and human macrophages. Unexpectedly, both genetic Lepr ablation in macrophages and global pharmacologic leptin antagonization augmented lysosomal functions, reduced S . Typhimurium burden, and diminished inflammation in vitro and in vivo. Mechanistically, we show that leptin induction activates the mTORC2/Akt pathway and subsequently down-regulates Phlpp1 phosphatase, allowing for phosphorylated Akt to impair lysosomal-mediated pathogen clearance. These data highlight a link between leptin signaling, the mTORC2/Phlpp1/Akt axis, and lysosomal activity in macrophages and have important therapeutic implications for modulating innate immunity to combat Gram-negative bacterial infections.
Author Plum, Georg
Ranjan, Rajeev
Ganesan, Raja
Hos, Nina Judith
Fischer, Julia
Gutièrrez, Saray
Tergaonkar, Vinay
Rybniker, Jan
Antebi, Adam
Wolke, Martina
Fries, Jochen W. U.
Robinson, Nirmal
Cildir, Gökhan
Calabrese, Chiara
Author_xml – sequence: 1
  givenname: Julia
  surname: Fischer
  fullname: Fischer, Julia
– sequence: 2
  givenname: Saray
  surname: Gutièrrez
  fullname: Gutièrrez, Saray
– sequence: 3
  givenname: Raja
  surname: Ganesan
  fullname: Ganesan, Raja
– sequence: 4
  givenname: Chiara
  surname: Calabrese
  fullname: Calabrese, Chiara
– sequence: 5
  givenname: Rajeev
  surname: Ranjan
  fullname: Ranjan, Rajeev
– sequence: 6
  givenname: Gökhan
  surname: Cildir
  fullname: Cildir, Gökhan
– sequence: 7
  givenname: Nina Judith
  surname: Hos
  fullname: Hos, Nina Judith
– sequence: 8
  givenname: Jan
  surname: Rybniker
  fullname: Rybniker, Jan
– sequence: 9
  givenname: Martina
  surname: Wolke
  fullname: Wolke, Martina
– sequence: 10
  givenname: Jochen W. U.
  surname: Fries
  fullname: Fries, Jochen W. U.
– sequence: 11
  givenname: Vinay
  surname: Tergaonkar
  fullname: Tergaonkar, Vinay
– sequence: 12
  givenname: Georg
  surname: Plum
  fullname: Plum, Georg
– sequence: 13
  givenname: Adam
  surname: Antebi
  fullname: Antebi, Adam
– sequence: 14
  givenname: Nirmal
  surname: Robinson
  fullname: Robinson, Nirmal
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31350351$$D View this record in MEDLINE/PubMed
https://gup.ub.gu.se/publication/283353$$DView record from Swedish Publication Index
BookMark eNpd0Utv1DAQAGALFdFt4cwJFIkLl7Qev2JfkKqKR8VKPbScLW8ym_UqcYKdgPrvcbRloT1Z8nwzmscZOQlDQELeAr0AWvHLMbh0AYYKrSWAekFWQA2UShh6QlaUsqrUgolTcpbSnlJqpKavyCkHLimXsCLf1zhOPhTJt8F1PrSF70fnYyp6V8dh3LkWiwa3GBKmwrXOhzQVd67rcyNd54r7h3Hn-zn6uX9NXm5dl_DN43tOfnz5fH_9rVzffr25vlqXtdAwlQpqRFSO6UY3brup5cY0WmsBtXQKa6grxQ1zIAwgxYZrtYFGSiEY0wYcPyfloW76jeO8sWP0vYsPdnDetvNo81c724SWac4lz_7TwWfcY1NjmKLrnqQ9jQS_s-3wyyplqsqIXODjY4E4_JwxTbb3qV7GDzjMyTKmZCUqxnWmH57R_TDHvNpFVYJzDnpRlweVV5xSxO2xGaB2OaxdDmv_HTZnvP9_hqP_e8kM3h3APk1DPMaZ0pKKTP4A3PWsZg
CitedBy_id crossref_primary_10_2337_db21_0842
crossref_primary_10_1007_s11306_022_01921_8
crossref_primary_10_1111_jcmm_16605
crossref_primary_10_3390_pathogens9070587
crossref_primary_10_1371_journal_ppat_1009943
crossref_primary_10_4049_jimmunol_2000048
crossref_primary_10_1128_iai_00242_22
crossref_primary_10_3390_ijms22041933
crossref_primary_10_1016_j_tim_2022_01_006
crossref_primary_10_1007_s10753_019_01132_9
crossref_primary_10_1016_j_crimmu_2024_100077
crossref_primary_10_4049_jimmunol_2000490
crossref_primary_10_1210_endrev_bnaa027
crossref_primary_10_1016_j_bbagen_2020_129627
crossref_primary_10_1038_s41467_023_42432_x
Cites_doi 10.1038/nature25986
10.1016/j.immuni.2016.02.024
10.1097/EDE.0000000000000301
10.1016/j.molmed.2015.12.001
10.1038/onc.2012.540
10.3389/fcimb.2017.00428
10.1016/j.molmed.2013.05.001
10.1016/j.immuni.2010.11.024
10.4049/jimmunol.1200935
10.1186/s12889-018-5172-8
10.1152/ajplung.00447.2017
10.1128/mBio.02046-14
10.1016/j.chom.2012.04.012
10.1128/IAI.00976-08
10.1371/journal.ppat.1006227
10.1002/jcp.24273
10.1038/nrmicro955
10.1210/en.2008-1706
10.1016/j.molcel.2015.05.030
10.1111/j.1600-0854.2008.00804.x
10.1016/S0092-8674(00)81231-3
10.1091/mbc.12.1.155
10.1016/j.cytogfr.2017.03.001
10.4049/jimmunol.1003226
10.1083/jcb.201607005
10.1002/jcp.21843
10.1016/j.jim.2014.05.009
10.1371/journal.pone.0108138
10.1038/ni.2397
10.1016/j.micinf.2011.07.008
10.4049/jimmunol.168.8.4018
10.1016/S1473-3099(17)30753-3
10.1074/jbc.M509157200
10.1074/jbc.M706706200
10.1016/j.cell.2010.02.024
10.1091/mbc.e15-05-0272
10.1172/JCI45294
10.1126/science.aan4665
10.1371/journal.pgen.1000938
10.1016/S1473-3099(13)70318-9
10.1371/journal.ppat.1004159
10.1073/pnas.0813319106
10.1038/nri.2016.70
10.4049/jimmunol.1701712
10.1126/science.1106148
10.1083/jcb.201610060
10.1155/2013/487081
10.1126/science.1157535
10.1038/ncomms14338
ContentType Journal Article
Copyright Copyright © 2019 the Author(s). Published by PNAS.
Copyright National Academy of Sciences Aug 13, 2019
Copyright © 2019 the Author(s). Published by PNAS. 2019
Copyright_xml – notice: Copyright © 2019 the Author(s). Published by PNAS.
– notice: Copyright National Academy of Sciences Aug 13, 2019
– notice: Copyright © 2019 the Author(s). Published by PNAS. 2019
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QG
7QL
7QP
7QR
7SN
7SS
7T5
7TK
7TM
7TO
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
ADTPV
AOWAS
F1U
DOI 10.1073/pnas.1904885116
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Ecology Abstracts
Entomology Abstracts (Full archive)
Immunology Abstracts
Neurosciences Abstracts
Nucleic Acids Abstracts
Oncogenes and Growth Factors Abstracts
Virology and AIDS Abstracts
Technology Research Database
Environmental Sciences and Pollution Management
Engineering Research Database
AIDS and Cancer Research Abstracts
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
SwePub
SwePub Articles
SWEPUB Göteborgs universitet
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Virology and AIDS Abstracts
Oncogenes and Growth Factors Abstracts
Technology Research Database
Nucleic Acids Abstracts
Ecology Abstracts
Neurosciences Abstracts
Biotechnology and BioEngineering Abstracts
Environmental Sciences and Pollution Management
Entomology Abstracts
Genetics Abstracts
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
AIDS and Cancer Research Abstracts
Chemoreception Abstracts
Immunology Abstracts
Engineering Research Database
Calcium & Calcified Tissue Abstracts
MEDLINE - Academic
DatabaseTitleList
MEDLINE


CrossRef
Virology and AIDS Abstracts
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
Discipline Sciences (General)
EISSN 1091-6490
EndPage 16560
ExternalDocumentID oai_gup_ub_gu_se_283353
10_1073_pnas_1904885116
31350351
26850450
Genre Research Support, Non-U.S. Gov't
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIDDK NIH HHS
  grantid: P30 DK026687
– fundername: Deutsche Forschungsgemeinschaft (DFG)
  grantid: SFB670 (N31)
– fundername: Deutsches Zentrum für Infektionsforschung (DZIF)
  grantid: CL-02-2011
– fundername: Deutsche Forschungsgemeinschaft (DFG)
  grantid: D01
– fundername: Universität zu Köln (University of Cologne)
  grantid: 311/2014
– fundername: Deutsches Zentrum für Infektionsforschung (DZIF)
  grantid: TI 07.005_Fischer_00
– fundername: Universität zu Köln (University of Cologne)
  grantid: Gusyk funding
– fundername: Universität zu Köln (University of Cologne)
  grantid: Maria-Pesch
– fundername: Universität zu Köln (University of Cologne)
  grantid: Köln Fortune
GroupedDBID ---
-DZ
-~X
.55
0R~
123
29P
2AX
2FS
2WC
4.4
53G
5RE
5VS
85S
AACGO
AAFWJ
AANCE
ABBHK
ABOCM
ABPLY
ABPPZ
ABTLG
ABXSQ
ABZEH
ACGOD
ACIWK
ACNCT
ACPRK
ADACV
ADULT
AENEX
AEUPB
AEXZC
AFFNX
AFOSN
AFRAH
ALMA_UNASSIGNED_HOLDINGS
AQVQM
BKOMP
CS3
D0L
DCCCD
DIK
DOOOF
DU5
E3Z
EBS
EJD
F5P
FRP
GX1
H13
HH5
HYE
IPSME
JAAYA
JBMMH
JENOY
JHFFW
JKQEH
JLS
JLXEF
JPM
JSG
JST
KQ8
L7B
LU7
N9A
N~3
O9-
OK1
PNE
PQQKQ
R.V
RHF
RHI
RNA
RNS
RPM
RXW
SA0
SJN
TAE
TN5
UKR
VQA
W8F
WH7
WOQ
WOW
X7M
XSW
Y6R
YBH
YKV
YSK
ZCA
~02
~KM
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QG
7QL
7QP
7QR
7SN
7SS
7T5
7TK
7TM
7TO
7U9
8FD
C1K
FR3
H94
M7N
P64
RC3
7X8
5PM
.GJ
3O-
692
6TJ
79B
AAYJJ
ACKIV
ADTPV
AOWAS
AS~
F1U
F20
HGD
HQ3
HTVGU
JSODD
MVM
NEJ
NHB
P-O
VOH
WHG
ZCG
ID FETCH-LOGICAL-c481t-61ceee6a28d8dafbc5b9d88841c5a6ec1c76392a1491e0ed386b1d554422891a3
IEDL.DBID RPM
ISSN 0027-8424
IngestDate Sat Aug 24 00:42:14 EDT 2024
Tue Sep 17 21:27:46 EDT 2024
Fri Oct 25 06:52:32 EDT 2024
Thu Oct 10 16:41:19 EDT 2024
Fri Dec 06 02:51:13 EST 2024
Sat Sep 28 08:28:57 EDT 2024
Tue Dec 10 23:55:01 EST 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 33
Keywords Salmonella
macrophages
AKT
lysosomes
leptin
Language English
License Copyright © 2019 the Author(s). Published by PNAS.
This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c481t-61ceee6a28d8dafbc5b9d88841c5a6ec1c76392a1491e0ed386b1d554422891a3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Author contributions: J.F., G.P., and N.R. designed research; J.F., S.G., R.G., C.C., R.R., G.C., N.J.H., M.W., J.W.U.F., and N.R. performed research; V.T. and A.A. contributed new reagents/analytic tools; J.F., S.G., J.R., J.W.U.F., and N.R. analyzed data; and J.F., G.C., A.A., and N.R. wrote the paper.
1Present address: Department of Physiology, Institute of Neuroscience and Physiology, University of Gothenburg, SE-405 30 Gothenburg, Sweden.
Edited by Andres Vazquez-Torres, University of Colorado School of Medicine, Aurora, CO, and accepted by Editorial Board Member Carl F. Nathan July 2, 2019 (received for review March 25, 2019)
ORCID 0000-0002-7361-9491
0000-0002-7241-3029
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6697794/
PMID 31350351
PQID 2274333188
PQPubID 42026
PageCount 10
ParticipantIDs swepub_primary_oai_gup_ub_gu_se_283353
pubmedcentral_primary_oai_pubmedcentral_nih_gov_6697794
proquest_miscellaneous_2265747238
proquest_journals_2274333188
crossref_primary_10_1073_pnas_1904885116
pubmed_primary_31350351
jstor_primary_26850450
PublicationCentury 2000
PublicationDate 2019-08-13
PublicationDateYYYYMMDD 2019-08-13
PublicationDate_xml – month: 08
  year: 2019
  text: 2019-08-13
  day: 13
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: Washington
PublicationSeriesTitle PNAS Plus
PublicationTitle Proceedings of the National Academy of Sciences - PNAS
PublicationTitleAlternate Proc Natl Acad Sci U S A
PublicationYear 2019
Publisher National Academy of Sciences
Publisher_xml – sequence: 0
  name: National Academy of Sciences
– name: National Academy of Sciences
References e_1_3_3_50_2
Truett G. E. (e_1_3_3_35_2) 1998; 275
e_1_3_3_16_2
e_1_3_3_18_2
e_1_3_3_39_2
e_1_3_3_12_2
e_1_3_3_37_2
e_1_3_3_14_2
e_1_3_3_33_2
e_1_3_3_10_2
e_1_3_3_31_2
e_1_3_3_40_2
e_1_3_3_5_2
e_1_3_3_7_2
e_1_3_3_9_2
e_1_3_3_27_2
e_1_3_3_29_2
e_1_3_3_23_2
e_1_3_3_48_2
e_1_3_3_25_2
e_1_3_3_46_2
e_1_3_3_1_2
e_1_3_3_44_2
e_1_3_3_3_2
e_1_3_3_21_2
e_1_3_3_42_2
e_1_3_3_51_2
Gutiérrez S. (e_1_3_3_52_2) 2017
e_1_3_3_17_2
e_1_3_3_19_2
e_1_3_3_38_2
e_1_3_3_13_2
e_1_3_3_36_2
e_1_3_3_15_2
e_1_3_3_34_2
e_1_3_3_32_2
e_1_3_3_11_2
e_1_3_3_30_2
e_1_3_3_6_2
e_1_3_3_8_2
e_1_3_3_28_2
e_1_3_3_49_2
e_1_3_3_24_2
e_1_3_3_47_2
e_1_3_3_26_2
e_1_3_3_45_2
e_1_3_3_2_2
e_1_3_3_20_2
e_1_3_3_43_2
e_1_3_3_4_2
e_1_3_3_22_2
e_1_3_3_41_2
References_xml – ident: e_1_3_3_13_2
  doi: 10.1038/nature25986
– ident: e_1_3_3_4_2
  doi: 10.1016/j.immuni.2016.02.024
– ident: e_1_3_3_9_2
  doi: 10.1097/EDE.0000000000000301
– ident: e_1_3_3_19_2
  doi: 10.1016/j.molmed.2015.12.001
– ident: e_1_3_3_21_2
  doi: 10.1038/onc.2012.540
– ident: e_1_3_3_6_2
  doi: 10.3389/fcimb.2017.00428
– ident: e_1_3_3_11_2
  doi: 10.1016/j.molmed.2013.05.001
– ident: e_1_3_3_44_2
  doi: 10.1016/j.immuni.2010.11.024
– start-page: e56514
  year: 2017
  ident: e_1_3_3_52_2
  article-title: Isolation of Salmonella typhimurium-containing phagosomes from macrophages
  publication-title: J. Vis. Exp.
  contributor:
    fullname: Gutiérrez S.
– ident: e_1_3_3_27_2
  doi: 10.4049/jimmunol.1200935
– ident: e_1_3_3_10_2
  doi: 10.1186/s12889-018-5172-8
– ident: e_1_3_3_38_2
  doi: 10.1152/ajplung.00447.2017
– ident: e_1_3_3_17_2
  doi: 10.1128/mBio.02046-14
– ident: e_1_3_3_51_2
  doi: 10.1016/j.chom.2012.04.012
– ident: e_1_3_3_32_2
  doi: 10.1128/IAI.00976-08
– ident: e_1_3_3_8_2
  doi: 10.1371/journal.ppat.1006227
– ident: e_1_3_3_18_2
  doi: 10.1002/jcp.24273
– ident: e_1_3_3_3_2
  doi: 10.1038/nrmicro955
– ident: e_1_3_3_25_2
  doi: 10.1210/en.2008-1706
– ident: e_1_3_3_20_2
  doi: 10.1016/j.molcel.2015.05.030
– ident: e_1_3_3_26_2
  doi: 10.1111/j.1600-0854.2008.00804.x
– ident: e_1_3_3_36_2
  doi: 10.1016/S0092-8674(00)81231-3
– ident: e_1_3_3_40_2
– ident: e_1_3_3_37_2
  doi: 10.1091/mbc.12.1.155
– ident: e_1_3_3_30_2
  doi: 10.1016/j.cytogfr.2017.03.001
– ident: e_1_3_3_34_2
  doi: 10.4049/jimmunol.1003226
– volume: 275
  start-page: R29
  year: 1998
  ident: e_1_3_3_35_2
  article-title: Misty (m) affects growth traits
  publication-title: Am. J. Physiol.
  contributor:
    fullname: Truett G. E.
– ident: e_1_3_3_5_2
  doi: 10.1083/jcb.201607005
– ident: e_1_3_3_22_2
  doi: 10.1002/jcp.21843
– ident: e_1_3_3_23_2
  doi: 10.1016/j.jim.2014.05.009
– ident: e_1_3_3_24_2
  doi: 10.1371/journal.pone.0108138
– ident: e_1_3_3_7_2
  doi: 10.1038/ni.2397
– ident: e_1_3_3_33_2
  doi: 10.1016/j.micinf.2011.07.008
– ident: e_1_3_3_39_2
  doi: 10.4049/jimmunol.168.8.4018
– ident: e_1_3_3_2_2
  doi: 10.1016/S1473-3099(17)30753-3
– ident: e_1_3_3_49_2
  doi: 10.1074/jbc.M509157200
– ident: e_1_3_3_43_2
  doi: 10.1074/jbc.M706706200
– ident: e_1_3_3_42_2
  doi: 10.1016/j.cell.2010.02.024
– ident: e_1_3_3_29_2
  doi: 10.1091/mbc.e15-05-0272
– ident: e_1_3_3_31_2
  doi: 10.1172/JCI45294
– ident: e_1_3_3_12_2
  doi: 10.1126/science.aan4665
– ident: e_1_3_3_15_2
  doi: 10.1371/journal.pgen.1000938
– ident: e_1_3_3_1_2
  doi: 10.1016/S1473-3099(13)70318-9
– ident: e_1_3_3_46_2
  doi: 10.1371/journal.ppat.1004159
– ident: e_1_3_3_48_2
  doi: 10.1073/pnas.0813319106
– ident: e_1_3_3_14_2
  doi: 10.1038/nri.2016.70
– ident: e_1_3_3_50_2
  doi: 10.4049/jimmunol.1701712
– ident: e_1_3_3_28_2
  doi: 10.1126/science.1106148
– ident: e_1_3_3_45_2
  doi: 10.1083/jcb.201610060
– ident: e_1_3_3_16_2
  doi: 10.1155/2013/487081
– ident: e_1_3_3_41_2
  doi: 10.1126/science.1157535
– ident: e_1_3_3_47_2
  doi: 10.1038/ncomms14338
SSID ssj0009580
Score 2.4532614
Snippet The dynamic interplay between metabolism and immune responses in health and disease, by which different immune cells impact on metabolic processes, are being...
In the present study, we identify and describe an important cross-talk between leptin signaling and macrophage functions in the context of Salmonella...
SourceID swepub
pubmedcentral
proquest
crossref
pubmed
jstor
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 16551
SubjectTerms Ablation
activation
Adult
AKT
AKT protein
Animals
Bacterial infections
Biological Sciences
cells
Crosstalk
expression
Farmaceutisk vetenskap
Female
Gram-negative bacteria
host-defense
Humans
Immune clearance
Immune response
Immune system
Immunity
infection
Infections
Inflammation - pathology
Innate immunity
leptin
Leptin - antagonists & inhibitors
Leptin - metabolism
lysosome
lysosomes
Lysosomes - metabolism
Macrophages
Macrophages - immunology
Macrophages - microbiology
Mechanistic Target of Rapamycin Complex 2 - metabolism
Metabolism
Mice
Mice, Inbred C57BL
Models, Biological
pathogen
Pathogens
Phagosomes - metabolism
Pharmaceutical Sciences
Phosphoprotein Phosphatases - metabolism
Phosphorylation
PNAS Plus
Proto-Oncogene Proteins c-akt - metabolism
RAW 264.7 Cells
receptor
Receptors, Leptin - metabolism
Regulators
Rodents
Salmonella
Salmonella Infections, Animal
Salmonella typhimurium - immunology
Signal Transduction
Signaling
Young Adult
Title Leptin signaling impairs macrophage defenses against Salmonella Typhimurium
URI https://www.jstor.org/stable/26850450
https://www.ncbi.nlm.nih.gov/pubmed/31350351
https://www.proquest.com/docview/2274333188
https://search.proquest.com/docview/2265747238
https://pubmed.ncbi.nlm.nih.gov/PMC6697794
https://gup.ub.gu.se/publication/283353
Volume 116
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB4BJy5VKdCmpchIFaKHfTh-bHJECISgoEotEjfLiZ3dSCRdbTb_vzN5oag9cY3tJJoZe76xvxkDfHNSSrQbIrWnbiKVyiaJoG04GSYuckqLJlH44VHfPsm7Z_W8A6rPhWlI-2mST8uXYlrmq4ZbuS7SWc8Tm_18uNIaUUssZ7uwi-63D9GHSrtRm3cS4vIrQ9nX81mI2bq01RQ9IBot4gy6vUhwoegsbeSVWmLi_yDnv8zJUX3RxifdvId3HZhkl-1PH8COLz_AQTddK3bR1ZT-fgj3P4i9UjKia1jKQGeUHplvKlZYusRrhcsKcz7DoBYH2qXNETayX_YFrZT4UQzj1VVe1Ju8Lo7g6eb699XtpLtHYZLKiG8xOkRP6LUNI5S-zZJUJbHDyFfyVFntU57iIhOHFoMl7ufeiUgn3CHOoPJgMbfiGPZK_NonYEpb5Xjm5DzzEuduHGVq7qmfS2RsRQAXvRzNui2XYZpj7oUwJH3zKv0Ajhs5D_1CHSkEmPMATnrBm25CVSbE6FkIXICiAM6GZpwKdL5hS_-npj5aYXSEICSAj62ehpf3ig5gMdLg0IHKbI9b0PqactudtQVw3up6NGRZrw0-Wtam8iakDDbx-c2f-AL7iMdi2rLm4gT2tpvaf0XMs01OyeOo08bS_wJU9QHl
link.rule.ids 230,314,727,780,784,885,27924,27925,53791,53793
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VcoALokAhUMBICJXDPhw_NjmiimqhuxUSrdSb5cTObqQmrDab_89MXiiCE9fYTqLxeOYb-5sxwEcnpUS9IVJ76iZSqWySCNqGk2HiIqe0aBKF19d6eSu_36m7I1B9LkxD2k-TfFreF9My3zbcyl2Rznqe2OzH-kJrRC2xnD2Ah0osYt4H6UOt3ajNPAnRAMtQ9hV9FmK2K201RR-IaotIg-4vElwoOk0b-aWWmvgv0Pk3d3JUYbTxSpdP4UkHJ9mX9rdP4MiXz-CkW7AVO--qSn9-Dlcr4q-UjAgblnLQGSVI5vuKFZau8dqiYWHOZxjW4kC7sTkCR_bT3qOeEkOKYcS6zYt6n9fFC7i9_HpzsZx0NylMUhnxA8aH6Au9tmGE8rdZkqokdhj7Sp4qq33KUzQzcWgxXOJ-7p2IdMIdIg0qEBZzK07huMSvvQKmtFWOZ07OMy9x9cZRpuae-rlExlYEcN7L0ezaghmmOeheCEPSN3-kH8BpI-ehX6gjhRBzHsBZL3jTLanKhBg_C4EmKArgw9CMi4FOOGzpf9XURyuMjxCGBPCynafh5f1EB7AYzeDQgQptj1tQ_5qC252-BfCpnevRkE29M_hoU5vKm5By2MTr__7Ee3i0vFmvzOrb9dUbeIzoLKYNbC7O4Piwr_1bRECH5F2j778B9DgEVA
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB5BkRAXRIHSlAJGQqgcdrOJH5scUWFV6EOVoFJvlhM7u5GaEG02_78zeUEEJ66xnUQzY_sb-5sZgA9WCIF2Q6T21M6ElNks4XQMJ8LERlYq3gYKX16psxvx_Vbe_lHqqyXtp0k-L--KeZlvWm5lVaT-wBPzry9PlULUEgu_spn_EB5JjkY2OOpjvt2oiz4JcREWoRiy-iy5X5WmnuM-iKaLaINqGPGAS7pRm-xNHT3xX8Dzb_7kJMtouzOtnsHTHlKyz92v78MDVz6H_X7S1uykzyz96QWcXxCHpWRE2jAUh84oSDLf1qwwVMprg4sLsy5D1xYHmrXJETyyH-YObZVYUgy91k1eNNu8KV7Czerrz9OzWV9NYZaKKNihj4j7oVMmjFAHJktSmcQW_V8RpNIolwYpLjVxaNBlCtzCWR6pJLCINihJWBwYfgB7JX7tEJhURtogs2KROYEzOI4yuXDUzyYiNtyDk0GOuuqSZuj2snvJNUlf_5a-BwetnMd-oYokwsyFB8eD4HU_rWodog_NOS5DkQfvx2acEHTLYUr3q6E-SqKPhFDEg1ednsaXD4r2YDnR4NiBkm1PW9AG26Tbvc158LHT9WTIuqk0Plo3unY6pDg2fvTfn3gHj6-_rPTFt6vz1_AEAVpMZ9gBP4a93bZxbxAE7ZK3rbnfA7DPBWc
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=Leptin+signaling+impairs+macrophage+defenses+against+Salmonella+Typhimurium&rft.jtitle=Proceedings+of+the+National+Academy+of+Sciences+-+PNAS&rft.au=Fischer%2C+Julia&rft.au=Guti%C3%A8rrez%2C+Saray&rft.au=Ganesan%2C+Raja&rft.au=Calabrese%2C+Chiara&rft.date=2019-08-13&rft.issn=0027-8424&rft.eissn=1091-6490&rft.volume=116&rft.issue=33&rft.spage=16551&rft.epage=16560&rft_id=info:doi/10.1073%2Fpnas.1904885116&rft.externalDBID=n%2Fa&rft.externalDocID=10_1073_pnas_1904885116
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0027-8424&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0027-8424&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0027-8424&client=summon