The impact of thioredoxin reduction of allosteric disulfide bonds on the therapeutic potential of monoclonal antibodies.
Allosteric Site
Antibodies, Monoclonal
/ chemistry
Antibody-Dependent Cell Cytotoxicity
/ immunology
Antigens
/ chemistry
Antineoplastic Agents, Immunological
/ chemistry
B-Lymphocytes
/ cytology
Cell Line
Cell Membrane
/ metabolism
Cell Proliferation
Complement System Proteins
Disulfides
/ chemistry
Humans
Immunoglobulin Fc Fragments
/ chemistry
Immunoglobulin G
/ chemistry
Kinetics
Leukocytes, Mononuclear
/ cytology
Oxidative Stress
Oxygen
/ chemistry
Protein-Tyrosine Kinases
/ chemistry
Receptor, ErbB-2
/ chemistry
Thioredoxins
/ chemistry
Trastuzumab
/ chemistry
allosteric regulation
antibody-dependent cellular cytotoxicity (ADCC)
biotherapeutic
complement-dependent cytotoxicity (CDC)
disulfide
disulfide bond
functional effects
monoclonal antibody
redox regulation
safety and efficacy
thioredoxin (Trx)
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
20 12 2019
20 12 2019
Historique:
received:
14
08
2019
revised:
04
11
2019
pubmed:
16
11
2019
medline:
23
6
2020
entrez:
16
11
2019
Statut:
ppublish
Résumé
Therapeutic mAbs are used to manage a wide range of cancers and autoimmune disorders. However, mAb-based treatments are not always successful, highlighting the need for a better understanding of the factors influencing mAb efficacy. Increased levels of oxidative stress associated with several diseases are counteracted by the activities of various oxidoreductase enzymes, such as thioredoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs. Here, using an array of
Identifiants
pubmed: 31727737
pii: S0021-9258(20)30276-3
doi: 10.1074/jbc.RA119.010637
pmc: PMC6926469
doi:
Substances chimiques
Antibodies, Monoclonal
0
Antigens
0
Antineoplastic Agents, Immunological
0
Disulfides
0
Immunoglobulin Fc Fragments
0
Immunoglobulin G
0
Thioredoxins
52500-60-4
Complement System Proteins
9007-36-7
ERBB2 protein, human
EC 2.7.10.1
Protein-Tyrosine Kinases
EC 2.7.10.1
Receptor, ErbB-2
EC 2.7.10.1
Trastuzumab
P188ANX8CK
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
19616-19634Informations de copyright
© 2019 Gurjar et al.
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