Recombinant Methioninase Combined With Tumor-targeting

Animals Antimetabolites, Antineoplastic / pharmacology Carbon-Sulfur Lyases / pharmacology Combined Modality Therapy Disease Models, Animal Doxorubicin / pharmacology Drug Resistance, Neoplasm / drug effects Humans Immunohistochemistry Liposarcoma / drug therapy Mice Recombinant Proteins / pharmacology Salmonella typhimurium / physiology Xenograft Model Antitumor Assays
Dedifferentiated liposarcoma PDOX S. typhimurium A1-R combination nude mice recombinant methioninase tumor regression

Journal

Anticancer research
ISSN: 1791-7530
Titre abrégé: Anticancer Res
Pays: Greece
ID NLM: 8102988

Informations de publication

Date de publication:
May 2020
Historique:
received: 06 04 2020
revised: 15 04 2020
accepted: 16 04 2020
entrez: 6 5 2020
pubmed: 6 5 2020
medline: 19 5 2020
Statut: ppublish

Résumé

Dedifferentiated liposarcoma (DDLPS) is associated with a poor survival rate even with multi-modality treatment. In the present study, we evaluated the efficacy of recombinant methioninase (rMETase) combined with tumor-targeting Salmonella typhimurium (S. typhimurium) A1-R against a doxorubicin-resistant DDLPS in a patient-derived orthotopic xenograft (PDOX) mouse model. A recurrent high-grade DDLPS from the right retroperitoneum of a patient was grown orthotopically in the retroperitoneum of nude mice to establish a PDOX model. The PDOX models were randomly divided into the following groups: Control, no treatment; doxorubicin monotherapy; rMETase monotherapy; S. typhimurium A1-R monotherapy; S. typhimurium A1-R and rMETase combination therapy. Tumor length and width were measured before and after treatment. On day 14 after treatment, all treatments significantly inhibited DDLPS PDOX tumor growth compared to the untreated control except for doxorubicin monotherapy. rMETase combined with S. typhimurium A1-R was significantly more effective and regressed tumor volume compared to either rMETase or S. typhimurium A1-R alone. The relative body weight did not significantly differ between days 0 and 14 for individual groups. The combination of rMETase and S. typhimurium A1-R has important clinical potential for this recalcitrant sarcoma.

Sections du résumé

BACKGROUND/AIM OBJECTIVE
Dedifferentiated liposarcoma (DDLPS) is associated with a poor survival rate even with multi-modality treatment. In the present study, we evaluated the efficacy of recombinant methioninase (rMETase) combined with tumor-targeting Salmonella typhimurium (S. typhimurium) A1-R against a doxorubicin-resistant DDLPS in a patient-derived orthotopic xenograft (PDOX) mouse model.
MATERIALS AND METHODS METHODS
A recurrent high-grade DDLPS from the right retroperitoneum of a patient was grown orthotopically in the retroperitoneum of nude mice to establish a PDOX model. The PDOX models were randomly divided into the following groups: Control, no treatment; doxorubicin monotherapy; rMETase monotherapy; S. typhimurium A1-R monotherapy; S. typhimurium A1-R and rMETase combination therapy. Tumor length and width were measured before and after treatment.
RESULTS RESULTS
On day 14 after treatment, all treatments significantly inhibited DDLPS PDOX tumor growth compared to the untreated control except for doxorubicin monotherapy. rMETase combined with S. typhimurium A1-R was significantly more effective and regressed tumor volume compared to either rMETase or S. typhimurium A1-R alone. The relative body weight did not significantly differ between days 0 and 14 for individual groups.
CONCLUSION CONCLUSIONS
The combination of rMETase and S. typhimurium A1-R has important clinical potential for this recalcitrant sarcoma.

Identifiants

DOI: 10.21873/anticanres.14222 PMID: 32366396
pubmed: 32366396
pii: 40/5/2515
doi: 10.21873/anticanres.14222
doi:

Substances chimiques

Antimetabolites, Antineoplastic 0
Recombinant Proteins 0
Doxorubicin 80168379AG
Carbon-Sulfur Lyases EC 4.4.-
L-methionine gamma-lyase EC 4.4.1.11

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

2515-2523

Informations de copyright

Copyright© 2020, International Institute of Anticancer Research (Dr. George J. Delinasios), All rights reserved.

Auteurs

Kentaro Igarashi (K)

AntiCancer, Inc., San Diego, CA, U.S.A.
Department of Surgery, University of California, San Diego, CA, U.S.A.
Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Kei Kawaguchi (K)

AntiCancer, Inc., San Diego, CA, U.S.A.
Department of Surgery, University of California, San Diego, CA, U.S.A.

Ming Zhao (M)

AntiCancer, Inc., San Diego, CA, U.S.A.

Qinghong Han (Q)

AntiCancer, Inc., San Diego, CA, U.S.A.

Yuying Tan (Y)

AntiCancer, Inc., San Diego, CA, U.S.A.

Tasuku Kiyuna (T)

AntiCancer, Inc., San Diego, CA, U.S.A.
Department of Surgery, University of California, San Diego, CA, U.S.A.

Kentaro Miyake (K)

AntiCancer, Inc., San Diego, CA, U.S.A.
Department of Surgery, University of California, San Diego, CA, U.S.A.

Takashi Higuchi (T)

AntiCancer, Inc., San Diego, CA, U.S.A.
Department of Surgery, University of California, San Diego, CA, U.S.A.
Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Scott D Nelson (SD)

Department of Pathology, University of California, Los Angeles, CA, U.S.A.

Sarah M Dry (SM)

Department of Pathology, University of California, Los Angeles, CA, U.S.A.

Yunfeng Li (Y)

Department of Pathology, University of California, Los Angeles, CA, U.S.A.

Norio Yamamoto (N)

Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Katsuhiro Hayashi (K)

Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Hiroaki Kimura (H)

Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Shinji Miwa (S)

Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan.

Shree Ram Singh (SR)

Basic Research Laboratory, National Cancer Institute, Frederick, MD, U.S.A. all@anticancer.com tsuchi@med.kanazawa-u.ac.jp singhshr@mail.nih.gov.

Hiroyuki Tsuchiya (H)

Department of Orthopaedic Surgery, Kanazawa University, Kanazawa, Japan all@anticancer.com tsuchi@med.kanazawa-u.ac.jp singhshr@mail.nih.gov.

Robert M Hoffman (RM)

AntiCancer, Inc., San Diego, CA, U.S.A. all@anticancer.com tsuchi@med.kanazawa-u.ac.jp singhshr@mail.nih.gov.
Department of Surgery, University of California, San Diego, CA, U.S.A.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Actions chimiques et utilisations › Actions toxiques › Noxas › Antimétabolites › Antimétabolites antinéoplasiques › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Lyases › Carbon-sulfur lyases › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Thérapeutique › Association thérapeutique › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles biologiques › Modèles animaux de maladie humaine › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Glucides › Hétérosides › Aminosides › Anthracyclines › Daunorubicine › Doxorubicine › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Résistance aux substances › Résistance aux médicaments antinéoplasiques › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Disciplines des sciences naturelles › Chimie › Biochimie › Immunohistochimie › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Tumeurs › Tumeurs par type histologique › Tumeurs du tissu conjonctif et des tissus mous › Sarcomes › Liposarcome › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines recombinantes › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Bactéries › Proteobacteria › Gammaproteobacteria › Enterobacteriaceae › Salmonella › Salmonella enterica › Salmonella typhimurium › Recombinant Methioninase Combined With Tumor-targeting
questionsmedicales.fr › Techniques d'investigation › Transplantation tumorale › Tests d'activité antitumorale sur modèle de xénogreffe › Recombinant Methioninase Combined With Tumor-targeting