Diabetic individuals with COVID-19 exhibit reduced efficacy of gliptins in inhibiting dipeptidyl peptidase 4 (DPP4). A suggested explanation for increased COVID-19 susceptibility in patients with type 2 diabetes mellitus (T2DM)

Dipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been identified as the most important risk factor for SARS-CoV-2, and that gliptins (DPP4 inhibitors) are a prescribed diabetic treatment, this study ai...

Full description

Saved in:
Bibliographic Details
Published inLife sciences (1973) Vol. 336; p. 122292
Main Authors Mora-Rodríguez, José María, Sánchez, Belén G, Bort, Alicia, Díaz-Yuste, Alba, Ballester-González, Rubén, Arrieta, Francisco, Sebastián-Martín, Alba, Díaz-Laviada, Inés
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.2024
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Dipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been identified as the most important risk factor for SARS-CoV-2, and that gliptins (DPP4 inhibitors) are a prescribed diabetic treatment, this study aims to unravel the impact of DPP4 in the intersection of T2DM/COVID-19. We analyzed 189 serum human samples, divided into six clinical groups (controls, T2DM, T2DM + gliptins, COVID-19, COVID-19 + T2DM, and COVID-19 + T2DM + gliptins), measuring DPP4 protein concentration and activity by Western blot, ELISA, and commercial activity kits. The obtained results were verified in Huh-7 cellular models. Both DPP4 concentration and activity were decreased in COVID-19 patients, and as in T2DM patients, compared to controls. Despite these lower levels, the ratio of DPP4 activity/concentration in COVID-19 sera was the highest (0.782 ± 0.289 μU/ng vs. 0.547 ± 0.050 μU/ng in controls, p < 0.0001), suggesting a compensating mechanism in these patients. Supernatants of Huh-7 cells incubated with COVID-19 serum showed a consistent and significantly lower DPP4 concentration and activity. Furthermore, COVID-19 + T2DM + gliptins patients showed a higher serum DPP4 concentration and activity than T2DM + gliptin subjects (p < 0.05), indicating that sera from COVID-19 convalescents interfere with gliptins. Either SARS-CoV-2 or some metabolites present in the sera of COVID-19-convalescent patients interact with soluble DPP4 or even gliptins themselves since the inhibitory effect of gliptins on DPP4 activity is being prevented. The interactions between DPP4, gliptins, and SARS-CoV-2 should be further elucidated to reveal the mechanism of action for these interesting observations.
AbstractList Dipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been identified as the most important risk factor for SARS-CoV-2, and that gliptins (DPP4 inhibitors) are a prescribed diabetic treatment, this study aims to unravel the impact of DPP4 in the intersection of T2DM/COVID-19. We analyzed 189 serum human samples, divided into six clinical groups (controls, T2DM, T2DM + gliptins, COVID-19, COVID-19 + T2DM, and COVID-19 + T2DM + gliptins), measuring DPP4 protein concentration and activity by Western blot, ELISA, and commercial activity kits. The obtained results were verified in Huh-7 cellular models. Both DPP4 concentration and activity were decreased in COVID-19 patients, and as in T2DM patients, compared to controls. Despite these lower levels, the ratio of DPP4 activity/concentration in COVID-19 sera was the highest (0.782 ± 0.289 μU/ng vs. 0.547 ± 0.050 μU/ng in controls, p < 0.0001), suggesting a compensating mechanism in these patients. Supernatants of Huh-7 cells incubated with COVID-19 serum showed a consistent and significantly lower DPP4 concentration and activity. Furthermore, COVID-19 + T2DM + gliptins patients showed a higher serum DPP4 concentration and activity than T2DM + gliptin subjects (p < 0.05), indicating that sera from COVID-19 convalescents interfere with gliptins. Either SARS-CoV-2 or some metabolites present in the sera of COVID-19-convalescent patients interact with soluble DPP4 or even gliptins themselves since the inhibitory effect of gliptins on DPP4 activity is being prevented. The interactions between DPP4, gliptins, and SARS-CoV-2 should be further elucidated to reveal the mechanism of action for these interesting observations.
AIMSDipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been identified as the most important risk factor for SARS-CoV-2, and that gliptins (DPP4 inhibitors) are a prescribed diabetic treatment, this study aims to unravel the impact of DPP4 in the intersection of T2DM/COVID-19.MATERIALS AND METHODSWe analyzed 189 serum human samples, divided into six clinical groups (controls, T2DM, T2DM + gliptins, COVID-19, COVID-19 + T2DM, and COVID-19 + T2DM + gliptins), measuring DPP4 protein concentration and activity by Western blot, ELISA, and commercial activity kits. The obtained results were verified in Huh-7 cellular models.KEY FINDINGSBoth DPP4 concentration and activity were decreased in COVID-19 patients, and as in T2DM patients, compared to controls. Despite these lower levels, the ratio of DPP4 activity/concentration in COVID-19 sera was the highest (0.782 ± 0.289 μU/ng vs. 0.547 ± 0.050 μU/ng in controls, p < 0.0001), suggesting a compensating mechanism in these patients. Supernatants of Huh-7 cells incubated with COVID-19 serum showed a consistent and significantly lower DPP4 concentration and activity. Furthermore, COVID-19 + T2DM + gliptins patients showed a higher serum DPP4 concentration and activity than T2DM + gliptin subjects (p < 0.05), indicating that sera from COVID-19 convalescents interfere with gliptins.SIGNIFICANCEEither SARS-CoV-2 or some metabolites present in the sera of COVID-19-convalescent patients interact with soluble DPP4 or even gliptins themselves since the inhibitory effect of gliptins on DPP4 activity is being prevented. The interactions between DPP4, gliptins, and SARS-CoV-2 should be further elucidated to reveal the mechanism of action for these interesting observations.
ArticleNumber 122292
Author Díaz-Yuste, Alba
Díaz-Laviada, Inés
Mora-Rodríguez, José María
Arrieta, Francisco
Ballester-González, Rubén
Bort, Alicia
Sánchez, Belén G
Sebastián-Martín, Alba
Author_xml – sequence: 1
  givenname: José María
  surname: Mora-Rodríguez
  fullname: Mora-Rodríguez, José María
  email: josem.mora@uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain. Electronic address: josem.mora@uah.es
– sequence: 2
  givenname: Belén G
  surname: Sánchez
  fullname: Sánchez, Belén G
  email: belen.sanchezg@uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain. Electronic address: belen.sanchezg@uah.es
– sequence: 3
  givenname: Alicia
  surname: Bort
  fullname: Bort, Alicia
  email: alicia.bort@uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain. Electronic address: alicia.bort@uah.es
– sequence: 4
  givenname: Alba
  surname: Díaz-Yuste
  fullname: Díaz-Yuste, Alba
  email: alba.diazy@edu.uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain. Electronic address: alba.diazy@edu.uah.es
– sequence: 5
  givenname: Rubén
  surname: Ballester-González
  fullname: Ballester-González, Rubén
  email: ruben.ballester@salud.madrid.org
  organization: Immunology Service, Ramón y Cajal Hospital, Ramón y Cajal Institute for Health Research (IRYCIS), Madrid, Spain. Electronic address: ruben.ballester@salud.madrid.org
– sequence: 6
  givenname: Francisco
  surname: Arrieta
  fullname: Arrieta, Francisco
  email: farrietab.hrc@salud.madrid.org
  organization: Endocrinology and Nutrition Service, Ramón y Cajal University Hospital, IRYCIS, Madrid, Spain. Electronic address: farrietab.hrc@salud.madrid.org
– sequence: 7
  givenname: Alba
  surname: Sebastián-Martín
  fullname: Sebastián-Martín, Alba
  email: alba.sebastian@uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain. Electronic address: alba.sebastian@uah.es
– sequence: 8
  givenname: Inés
  surname: Díaz-Laviada
  fullname: Díaz-Laviada, Inés
  email: ines.diazlaviada@uah.es
  organization: Department of Systems Biology, School of Medicine and Health Sciences, Alcalá University, Alcalá de Henares, Spain; Health Research Institute of Castilla-La Mancha (IDISCAM), Spain; Chemical Research Institute "Andrés M. del Río" (IQAR), Alcalá de Henares, Spain. Electronic address: ines.diazlaviada@uah.es
BackLink https://www.ncbi.nlm.nih.gov/pubmed/38030058$$D View this record in MEDLINE/PubMed
BookMark eNpFUctu1DAUtVARnRY-gA3ycrpI8DOPZTXDo1JRuyhsLce-nnqUSULsQPO9_ZE6zACSJfta55x7js4FOuv6DhB6T0lOCS0-7vPWhZwRxnPKGKvZK7SiVVlnpOD0DK0IYSLjjMhzdBHCnhAiZcnfoHNeEZ6GaoWet143EL3BvrP-l7eTbgP-7eMj3tz9uNlmtMbw9OgbH_EIdjJgMTjnjTYz7h3etX6IvguJns4fnO922PoB0r-dW3x86ABY4PX2_l5c5fgah2m3gxAXtaeh1Z2Ovu-w68ekYkZIcPvfQJiCWVQa3_o4L6uGhIcunpzGeQDM0tIlCgR8gDYBp4DXD2z77eoteu1SKnh3ui_R98-fHjZfs9u7Lzeb69vMcCFipiXTleCuJo3TtKmEYxZcyYqaF9oWrLKFM1KSxkpaigpKaSQxzLpS1IXghF-i9VF3GPufU0qnDj4Zb1M86KegWFXLknBKRILSI9SMfQgjODWM_qDHWVGilm7VXqVu1dKtOnabOB9O8lNzAPuP8bdM_gKQ3KRK
CitedBy_id crossref_primary_10_1097_MD_0000000000038062
crossref_primary_10_1016_j_jff_2024_106237
Cites_doi 10.1038/nature12005
10.1016/j.ijid.2020.04.086
10.1093/infdis/jiy574
10.1016/j.cmet.2018.10.001
10.1038/s41591-022-02156-9
10.1038/ni1008-1091
10.1038/s41586-020-2180-5
10.1016/j.metop.2021.100134
10.1038/nsb882
10.1007/0-306-47920-6_2
10.1007/s13205-022-03406-w
10.1016/j.isci.2020.101160
10.1016/j.lfs.2021.119410
10.15420/ecr.2018.33.1
10.1002/prot.23004
10.1038/s41467-020-17556-z
10.1111/1753-0407.13052
10.3892/ijo.2023.5489
10.1016/j.bbrc.2013.03.010
10.3389/fpubh.2021.591982
10.1016/j.cell.2020.02.058
10.3390/biomedicines10112897
10.1038/nature02145
10.3390/biomedicines10082026
10.1007/s00005-020-00602-5
10.1002/iub.1709
10.3389/fendo.2019.00505
10.1016/S0969-2126(03)00160-6
10.3389/fimmu.2015.00386
10.1016/j.jmb.2005.11.014
10.1210/clinem/dgab078
10.2217/bmm-2021-0717
10.1371/journal.pone.0166275
10.1111/jcmm.17492
10.1111/cei.13163
10.2217/fvl-2022-0112
10.1371/journal.pone.0251916
10.1016/j.cell.2020.02.052
10.1016/j.cell.2023.01.019
10.1016/j.virol.2018.03.015
10.1016/j.expneurol.2023.114379
10.1038/s41366-020-00689-y
ContentType Journal Article
Copyright Copyright © 2023. Published by Elsevier Inc.
Copyright_xml – notice: Copyright © 2023. Published by Elsevier Inc.
DBID NPM
AAYXX
CITATION
7X8
DOI 10.1016/j.lfs.2023.122292
DatabaseName PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle PubMed
CrossRef
MEDLINE - Academic
DatabaseTitleList PubMed
MEDLINE - Academic
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
DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
Biology
EISSN 1879-0631
EndPage 122292
ExternalDocumentID 10_1016_j_lfs_2023_122292
38030058
Genre Journal Article
GroupedDBID ---
--K
--M
-~X
.~1
0R~
1B1
1RT
1~.
4.4
457
5GY
5RE
5VS
6TJ
7-5
71M
8P~
9JM
AABNK
AACTN
AAEDT
AAEDW
AAHBH
AAIKJ
AAKOC
AALRI
AAOAW
AAQFI
AAXKI
AAXUO
ABFNM
ABFRF
ABJNI
ABLJU
ABMAC
ABMZM
ABZDS
ACDAQ
ACGFO
ACGFS
ACIUM
ACIWK
ACPRK
ACRLP
ADBBV
ADEZE
AEBSH
AEFWE
AEKER
AENEX
AFJKZ
AFKWA
AFRAH
AFTJW
AFXIZ
AGUBO
AGYEJ
AIEXJ
AIKHN
AITUG
AJOXV
AJRQY
AKRWK
ALCLG
ALMA_UNASSIGNED_HOLDINGS
AMFUW
AMRAJ
ANZVX
AXJTR
BKOJK
BLXMC
BNPGV
C45
CNWQP
CS3
DU5
EBS
EFJIC
EO8
EO9
EP2
EP3
F5P
FDB
FIRID
FNPLU
FYGXN
G-Q
GBLVA
IH2
IHE
J1W
K-O
KOM
L7B
M34
M41
MO0
N9A
NPM
O-L
O9-
OAUVE
OGGZJ
OVD
OZT
P-8
P-9
P2P
PC.
Q38
RIG
ROL
RPZ
SDF
SDG
SDP
SES
SEW
SPCBC
SSH
SSP
SSZ
T5K
TEORI
YZZ
~G-
.55
.GJ
29L
3O-
53G
AAQXK
AAYXX
ABTAH
ABXDB
ADMUD
AFFNX
AGHFR
AHHHB
ASPBG
AVWKF
AZFZN
CITATION
EJD
FEDTE
FGOYB
G-2
HMG
HMT
HVGLF
HZ~
H~9
J5H
MVM
R2-
SIN
SPT
WUQ
X7M
Y6R
YYP
ZGI
ZKB
ZXP
ZY4
7X8
ID FETCH-LOGICAL-c344t-a52a843f90bfa1b84f2def726936ad628d6fc550bd51748e75c50c2df74964303
ISSN 0024-3205
IngestDate Fri Aug 16 12:15:55 EDT 2024
Thu Sep 26 16:09:32 EDT 2024
Wed Oct 23 09:56:25 EDT 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Keywords COVID-19
DPP4
Type 2 diabetes
Enzymatic activity
Gliptins
Language English
License Copyright © 2023. Published by Elsevier Inc.
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c344t-a52a843f90bfa1b84f2def726936ad628d6fc550bd51748e75c50c2df74964303
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://doi.org/10.1016/j.lfs.2023.122292
PMID 38030058
PQID 2895703104
PQPubID 23479
PageCount 1
ParticipantIDs proquest_miscellaneous_2895703104
crossref_primary_10_1016_j_lfs_2023_122292
pubmed_primary_38030058
PublicationCentury 2000
PublicationDate 2024-Jan-01
2024-01-00
20240101
PublicationDateYYYYMMDD 2024-01-01
PublicationDate_xml – month: 01
  year: 2024
  text: 2024-Jan-01
  day: 01
PublicationDecade 2020
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Life sciences (1973)
PublicationTitleAlternate Life Sci
PublicationYear 2024
References Zhao (10.1016/j.lfs.2023.122292_bb0160) 2020; 96
Engel (10.1016/j.lfs.2023.122292_bb0200) 2006; 355
Sebastian-Martin (10.1016/j.lfs.2023.122292_bb0035) 2022; 10
Chen (10.1016/j.lfs.2023.122292_bb0010) 2023; 186
Love (10.1016/j.lfs.2023.122292_bb0080) 2021; 106
Rohrborn (10.1016/j.lfs.2023.122292_bb0090) 2015; 6
Russell (10.1016/j.lfs.2023.122292_bb0105) 2023; 29
Raj (10.1016/j.lfs.2023.122292_bb0005) 2013; 495
Du (10.1016/j.lfs.2023.122292_bb0045) 2023; 62
Lan (10.1016/j.lfs.2023.122292_bb0165) 2020; 581
Latini (10.1016/j.lfs.2023.122292_bb0030) 2022; 26
Sanchez (10.1016/j.lfs.2023.122292_bb0110) 2022; 10
Inn (10.1016/j.lfs.2023.122292_bb0145) 2018; 518
Li (10.1016/j.lfs.2023.122292_bb0025) 2003; 426
Rasmussen (10.1016/j.lfs.2023.122292_bb0130) 2003; 10
Nabeno (10.1016/j.lfs.2023.122292_bb0190) 2013; 434
Arulmozhiraja (10.1016/j.lfs.2023.122292_bb0195) 2016; 11
Nadasdi (10.1016/j.lfs.2023.122292_bb0120) 2022; 16
Yang (10.1016/j.lfs.2023.122292_bb0065) 2021; 16
Baum (10.1016/j.lfs.2023.122292_bb0135) 2003; 524
Walls (10.1016/j.lfs.2023.122292_bb0170) 2020; 181
Casrouge (10.1016/j.lfs.2023.122292_bb0150) 2018; 194
Posadas-Sanchez (10.1016/j.lfs.2023.122292_bb0050) 2021; 276
Li (10.1016/j.lfs.2023.122292_bb0015) 2020; 23
Kase (10.1016/j.lfs.2023.122292_bb0040) 2023; 363
Tsalamandris (10.1016/j.lfs.2023.122292_bb0115) 2019; 14
Heng TS, Painter MW, Immunological Genome Project C (10.1016/j.lfs.2023.122292_bb0155) 2008; 9
Kifle (10.1016/j.lfs.2023.122292_bb0055) 2021; 12
Li (10.1016/j.lfs.2023.122292_bb0205) 2011; 79
Magdy Beshbishy (10.1016/j.lfs.2023.122292_bb0100) 2021; 9
Sarkar (10.1016/j.lfs.2023.122292_bb0095) 2019; 10
Baggio (10.1016/j.lfs.2023.122292_bb0125) 2020; 11
da Cruz Freire (10.1016/j.lfs.2023.122292_bb0185) 2022; 12
Krejner-Bienias (10.1016/j.lfs.2023.122292_bb0075) 2021; 69
Algaissi (10.1016/j.lfs.2023.122292_bb0175) 2019; 219
Nargis (10.1016/j.lfs.2023.122292_bb0085) 2018; 70
Bassendine (10.1016/j.lfs.2023.122292_bb0210) 2020; 12
Hoffmann (10.1016/j.lfs.2023.122292_bb0020) 2020; 181
Thoma (10.1016/j.lfs.2023.122292_bb0180) 2003; 11
Varin (10.1016/j.lfs.2023.122292_bb0070) 2019; 29
Schlicht (10.1016/j.lfs.2023.122292_bb0140) 2020; 44
Nag (10.1016/j.lfs.2023.122292_bb0060) 2023
References_xml – volume: 495
  start-page: 251
  issue: 7440
  year: 2013
  ident: 10.1016/j.lfs.2023.122292_bb0005
  article-title: Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
  publication-title: Nature
  doi: 10.1038/nature12005
  contributor:
    fullname: Raj
– volume: 96
  start-page: 131
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0160
  article-title: Lymphopenia is associated with severe coronavirus disease 2019 (COVID-19) infections: a systemic review and meta-analysis
  publication-title: Int. J. Infect. Dis.
  doi: 10.1016/j.ijid.2020.04.086
  contributor:
    fullname: Zhao
– volume: 219
  start-page: 829
  issue: 5
  year: 2019
  ident: 10.1016/j.lfs.2023.122292_bb0175
  article-title: Elevated human dipeptidyl peptidase 4 expression reduces the susceptibility of hDPP4 transgenic mice to Middle East respiratory syndrome coronavirus infection and disease
  publication-title: J. Infect. Dis.
  doi: 10.1093/infdis/jiy574
  contributor:
    fullname: Algaissi
– volume: 29
  start-page: 320
  issue: 2
  year: 2019
  ident: 10.1016/j.lfs.2023.122292_bb0070
  article-title: Circulating levels of soluble dipeptidyl peptidase-4 are dissociated from inflammation and induced by enzymatic DPP4 inhibition
  publication-title: Cell Metab.
  doi: 10.1016/j.cmet.2018.10.001
  contributor:
    fullname: Varin
– volume: 29
  start-page: 334
  issue: 2
  year: 2023
  ident: 10.1016/j.lfs.2023.122292_bb0105
  article-title: Comorbidities, multimorbidity and COVID-19
  publication-title: Nat. Med.
  doi: 10.1038/s41591-022-02156-9
  contributor:
    fullname: Russell
– volume: 9
  start-page: 1091
  issue: 10
  year: 2008
  ident: 10.1016/j.lfs.2023.122292_bb0155
  article-title: The Immunological Genome Project: networks of gene expression in immune cells
  publication-title: Nat. Immunol.
  doi: 10.1038/ni1008-1091
  contributor:
    fullname: Heng TS, Painter MW, Immunological Genome Project C
– volume: 581
  start-page: 215
  issue: 7807
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0165
  article-title: Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
  publication-title: Nature
  doi: 10.1038/s41586-020-2180-5
  contributor:
    fullname: Lan
– volume: 12
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0055
  article-title: SARS-CoV-2 and diabetes: a potential therapeutic effect of dipeptidyl peptidase 4 inhibitors in diabetic patients diagnosed with COVID-19
  publication-title: Metabol. Open
  doi: 10.1016/j.metop.2021.100134
  contributor:
    fullname: Kifle
– volume: 10
  start-page: 19
  issue: 1
  year: 2003
  ident: 10.1016/j.lfs.2023.122292_bb0130
  article-title: Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
  publication-title: Nat. Struct. Biol.
  doi: 10.1038/nsb882
  contributor:
    fullname: Rasmussen
– volume: 524
  start-page: 19
  year: 2003
  ident: 10.1016/j.lfs.2023.122292_bb0135
  article-title: Structure-function relationship of DPP IV: insights into its dimerisation and gelatinase activity
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/0-306-47920-6_2
  contributor:
    fullname: Baum
– volume: 12
  start-page: 344
  issue: 12
  year: 2022
  ident: 10.1016/j.lfs.2023.122292_bb0185
  article-title: Evaluation of the anti-diabetic drug sitagliptin as a novel attenuate to SARS-CoV-2 evidence-based in silico: molecular docking and molecular dynamics
  publication-title: 3 Biotech
  doi: 10.1007/s13205-022-03406-w
  contributor:
    fullname: da Cruz Freire
– volume: 23
  issue: 6
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0015
  article-title: The MERS-CoV receptor DPP4 as a candidate binding target of the SARS-CoV-2 spike
  publication-title: iScience
  doi: 10.1016/j.isci.2020.101160
  contributor:
    fullname: Li
– volume: 276
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0050
  article-title: Dipeptidylpeptidase-4 levels and DPP4 gene polymorphisms in patients with COVID-19. Association with disease and with severity
  publication-title: Life Sci.
  doi: 10.1016/j.lfs.2021.119410
  contributor:
    fullname: Posadas-Sanchez
– volume: 14
  start-page: 50
  issue: 1
  year: 2019
  ident: 10.1016/j.lfs.2023.122292_bb0115
  article-title: The role of inflammation in diabetes: current concepts and future perspectives
  publication-title: Eur. Cardiol.
  doi: 10.15420/ecr.2018.33.1
  contributor:
    fullname: Tsalamandris
– volume: 79
  start-page: 1800
  issue: 6
  year: 2011
  ident: 10.1016/j.lfs.2023.122292_bb0205
  article-title: Possible ligand release pathway of dipeptidyl peptidase IV investigated by molecular dynamics simulations
  publication-title: Proteins
  doi: 10.1002/prot.23004
  contributor:
    fullname: Li
– volume: 11
  start-page: 3766
  issue: 1
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0125
  article-title: Plasma levels of DPP4 activity and sDPP4 are dissociated from inflammation in mice and humans
  publication-title: Nat. Commun.
  doi: 10.1038/s41467-020-17556-z
  contributor:
    fullname: Baggio
– volume: 12
  start-page: 649
  issue: 9
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0210
  article-title: COVID-19 and comorbidities: a role for dipeptidyl peptidase 4 (DPP4) in disease severity?
  publication-title: J. Diabetes
  doi: 10.1111/1753-0407.13052
  contributor:
    fullname: Bassendine
– volume: 62
  issue: 3
  year: 2023
  ident: 10.1016/j.lfs.2023.122292_bb0045
  article-title: Effect of DPP4/CD26 expression on SARS-CoV-2 susceptibility, immune response, adenosine (derivatives m(6)(2)A and CD) regulations on patients with cancer and healthy individuals
  publication-title: Int. J. Oncol.
  doi: 10.3892/ijo.2023.5489
  contributor:
    fullname: Du
– volume: 434
  start-page: 191
  issue: 2
  year: 2013
  ident: 10.1016/j.lfs.2023.122292_bb0190
  article-title: A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2013.03.010
  contributor:
    fullname: Nabeno
– volume: 9
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0100
  article-title: Factors behind the higher COVID-19 risk in diabetes: a critical review
  publication-title: Front. Public Health
  doi: 10.3389/fpubh.2021.591982
  contributor:
    fullname: Magdy Beshbishy
– volume: 181
  start-page: 281
  issue: 2
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0170
  article-title: Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein
  publication-title: Cell
  doi: 10.1016/j.cell.2020.02.058
  contributor:
    fullname: Walls
– volume: 10
  issue: 11
  year: 2022
  ident: 10.1016/j.lfs.2023.122292_bb0110
  article-title: A highly sensitive immunoassay for determination of immune response to SARS-CoV-2 in capillary blood samples
  publication-title: Biomedicines
  doi: 10.3390/biomedicines10112897
  contributor:
    fullname: Sanchez
– volume: 426
  start-page: 450
  issue: 6965
  year: 2003
  ident: 10.1016/j.lfs.2023.122292_bb0025
  article-title: Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
  publication-title: Nature
  doi: 10.1038/nature02145
  contributor:
    fullname: Li
– volume: 10
  issue: 8
  year: 2022
  ident: 10.1016/j.lfs.2023.122292_bb0035
  article-title: Role of dipeptidyl peptidase-4 (DPP4) on COVID-19 physiopathology
  publication-title: Biomedicines
  doi: 10.3390/biomedicines10082026
  contributor:
    fullname: Sebastian-Martin
– volume: 69
  start-page: 1
  issue: 1
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0075
  article-title: DPP4 inhibitors and COVID-19-holy grail or another dead end?
  publication-title: Arch. Immunol. Ther. Exp. (Warsz)
  doi: 10.1007/s00005-020-00602-5
  contributor:
    fullname: Krejner-Bienias
– volume: 70
  start-page: 112
  issue: 2
  year: 2018
  ident: 10.1016/j.lfs.2023.122292_bb0085
  article-title: Significance of circulatory DPP4 activity in metabolic diseases
  publication-title: IUBMB Life
  doi: 10.1002/iub.1709
  contributor:
    fullname: Nargis
– volume: 10
  start-page: 505
  year: 2019
  ident: 10.1016/j.lfs.2023.122292_bb0095
  article-title: Increased plasma dipeptidyl peptidase-4 (DPP4) activity is an obesity-independent parameter for glycemic deregulation in type 2 diabetes patients
  publication-title: Front. Endocrinol. (Lausanne)
  doi: 10.3389/fendo.2019.00505
  contributor:
    fullname: Sarkar
– volume: 11
  start-page: 947
  issue: 8
  year: 2003
  ident: 10.1016/j.lfs.2023.122292_bb0180
  article-title: Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
  publication-title: Structure
  doi: 10.1016/S0969-2126(03)00160-6
  contributor:
    fullname: Thoma
– volume: 6
  start-page: 386
  year: 2015
  ident: 10.1016/j.lfs.2023.122292_bb0090
  article-title: DPP4 in diabetes
  publication-title: Front. Immunol.
  doi: 10.3389/fimmu.2015.00386
  contributor:
    fullname: Rohrborn
– volume: 355
  start-page: 768
  issue: 4
  year: 2006
  ident: 10.1016/j.lfs.2023.122292_bb0200
  article-title: Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2005.11.014
  contributor:
    fullname: Engel
– volume: 106
  start-page: 1553
  issue: 6
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0080
  article-title: DPP4 activity, hyperinsulinemia, and atherosclerosis
  publication-title: J. Clin. Endocrinol. Metab.
  doi: 10.1210/clinem/dgab078
  contributor:
    fullname: Love
– volume: 16
  start-page: 317
  issue: 5
  year: 2022
  ident: 10.1016/j.lfs.2023.122292_bb0120
  article-title: Decreased circulating dipeptidyl peptidase-4 enzyme activity is prognostic for severe outcomes in COVID-19 inpatients
  publication-title: Biomark. Med
  doi: 10.2217/bmm-2021-0717
  contributor:
    fullname: Nadasdi
– volume: 11
  issue: 11
  year: 2016
  ident: 10.1016/j.lfs.2023.122292_bb0195
  article-title: Comparative binding analysis of dipeptidyl peptidase IV (DPP-4) with antidiabetic drugs - an ab initio fragment molecular orbital study
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0166275
  contributor:
    fullname: Arulmozhiraja
– volume: 26
  start-page: 4940
  issue: 19
  year: 2022
  ident: 10.1016/j.lfs.2023.122292_bb0030
  article-title: Expression analysis of miRNA hsa-let7b-5p in naso-oropharyngeal swabs of COVID-19 patients supports its role in regulating ACE2 and DPP4 receptors
  publication-title: J. Cell. Mol. Med.
  doi: 10.1111/jcmm.17492
  contributor:
    fullname: Latini
– volume: 194
  start-page: 166
  issue: 2
  year: 2018
  ident: 10.1016/j.lfs.2023.122292_bb0150
  article-title: Lymphocytes are a major source of circulating soluble dipeptidyl peptidase 4
  publication-title: Clin. Exp. Immunol.
  doi: 10.1111/cei.13163
  contributor:
    fullname: Casrouge
– year: 2023
  ident: 10.1016/j.lfs.2023.122292_bb0060
  article-title: DPP-4 inhibitors as a savior for COVID-19 patients with diabetes
  publication-title: Futur. Virol.
  doi: 10.2217/fvl-2022-0112
  contributor:
    fullname: Nag
– volume: 16
  issue: 5
  year: 2021
  ident: 10.1016/j.lfs.2023.122292_bb0065
  article-title: DPP-4 inhibitors may improve the mortality of coronavirus disease 2019: a meta-analysis
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0251916
  contributor:
    fullname: Yang
– volume: 181
  start-page: 271
  issue: 2
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0020
  article-title: SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor
  publication-title: Cell
  doi: 10.1016/j.cell.2020.02.052
  contributor:
    fullname: Hoffmann
– volume: 186
  start-page: 850
  issue: 4
  year: 2023
  ident: 10.1016/j.lfs.2023.122292_bb0010
  article-title: A bat MERS-like coronavirus circulates in pangolins and utilizes human DPP4 and host proteases for cell entry
  publication-title: Cell
  doi: 10.1016/j.cell.2023.01.019
  contributor:
    fullname: Chen
– volume: 518
  start-page: 324
  year: 2018
  ident: 10.1016/j.lfs.2023.122292_bb0145
  article-title: Reduction of soluble dipeptidyl peptidase 4 levels in plasma of patients infected with Middle East respiratory syndrome coronavirus
  publication-title: Virology
  doi: 10.1016/j.virol.2018.03.015
  contributor:
    fullname: Inn
– volume: 363
  year: 2023
  ident: 10.1016/j.lfs.2023.122292_bb0040
  article-title: The original strain of SARS-CoV-2, the Delta variant, and the Omicron variant infect microglia efficiently, in contrast to their inability to infect neurons: analysis using 2D and 3D cultures
  publication-title: Exp. Neurol.
  doi: 10.1016/j.expneurol.2023.114379
  contributor:
    fullname: Kase
– volume: 44
  start-page: 2335
  issue: 11
  year: 2020
  ident: 10.1016/j.lfs.2023.122292_bb0140
  article-title: Circulating levels of soluble Dipeptidylpeptidase-4 are reduced in human subjects hospitalized for severe COVID-19 infections
  publication-title: Int. J. Obes.
  doi: 10.1038/s41366-020-00689-y
  contributor:
    fullname: Schlicht
SSID ssj0005573
Score 2.4846904
Snippet Dipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been...
AIMSDipeptidyl peptidase 4 (DPP4) has been proposed as a coreceptor for SARS-CoV-2 cellular entry. Considering that type 2 diabetes mellitus (T2DM) has been...
SourceID proquest
crossref
pubmed
SourceType Aggregation Database
Index Database
StartPage 122292
Title Diabetic individuals with COVID-19 exhibit reduced efficacy of gliptins in inhibiting dipeptidyl peptidase 4 (DPP4). A suggested explanation for increased COVID-19 susceptibility in patients with type 2 diabetes mellitus (T2DM)
URI https://www.ncbi.nlm.nih.gov/pubmed/38030058
https://search.proquest.com/docview/2895703104
Volume 336
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnZ1Lb9NAEIBXbRGoF0QLlPDSIoGUEDly7PXrGBpQqVSooEXlZK2968hV6kR1fGgP_Fn-CDO7XtuFVAIukWNv1lbm8854PA9CXrMokJwnwrIlSy2WpsziPGSWC8ukHzlBxBMVbfHJPzhlh2fe2cbmXidqqVolo_R6bV7J_0gV9oFcMUv2HyTbTAo7YBvkC58gYfj8KxnrcJY8HeZNWlWdrbb_-dvHqTWOhhIbYOer4SWWaAXjUmLJCGzxDkbibI4Lho4kzws1Dh0HIl9iqIu4mg_1Bii6IUNTdHp8zN440QhWk7KazZSrFHsEzHnRxizmBRqiJXqOzUWUVamiZ1Qgrko0rMu5luv9wBdYJXRVKYfwiTM9Mu4Kk7edZ3JYq25daSoKug7jI8Da-rIQOgpgOqu0l_xwUeqwAExQ0ocanfRVfR8XgLAa-07O9diibT6Gned1ThC6gpongHqma-t7Vepeg5N5wrveFId1vClSa4AwwLIMtWqqVYTrdhf5MfZAd9bqH-0KOR_NMywF77ijP8cCQssLBaQb2tgsIGxVcRMgaQ5tkjtwv3gYqzr60Yld8gLXvKJXwYq_nW-b3DMz3LS3bnmIUsbUyQNyv34KohON9A7ZkMUuuav7ol7tkp1a45S0X5dFHzwkPw3ttEM7RX6oAY3WtNOadmpop4uMGtrh57Slnba004Z2ymgfWR-M6IQ2pNMO6RRIpw3p7QXcJB1PZUjXV4qkU4ca0qkhnfaR88Ejcvrh_cn-gVW3KLFSl7GVxT0HVjY3i-wk4-MkZJkjZBbAMuf6XPhOKPws9Tw7EVgRPpSBl3p26ogsYFgIz3Yfk61iUcgnBP6RIBKJJ7kt0MoXPGDCF47ryzCzExn0yFsjyHipK9HEJkTzPAYAYgQg1gD0yCsj6hj0Bb4E5IVcVDAojLDo3thmPbKnGWimM8w8vfXIM7Ld3jXPydbqspIvwCpfJS8Vob8AZHrdzQ
link.rule.ids 315,786,790,27955,27956
linkProvider Elsevier
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=Diabetic+individuals+with+COVID-19+exhibit+reduced+efficacy+of+gliptins+in+inhibiting+dipeptidyl+peptidase+4+%28DPP4%29.+A+suggested+explanation+for+increased+COVID-19+susceptibility+in+patients+with+type+2+diabetes+mellitus+%28T2DM%29&rft.jtitle=Life+sciences+%281973%29&rft.au=Mora-Rodr%C3%ADguez%2C+Jos%C3%A9+Mar%C3%ADa&rft.au=S%C3%A1nchez%2C+Bel%C3%A9n+G&rft.au=Bort%2C+Alicia&rft.au=D%C3%ADaz-Yuste%2C+Alba&rft.date=2024-01-01&rft.eissn=1879-0631&rft.volume=336&rft.spage=122292&rft_id=info:doi/10.1016%2Fj.lfs.2023.122292&rft_id=info%3Apmid%2F38030058&rft.externalDocID=38030058
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0024-3205&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0024-3205&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0024-3205&client=summon