Targeting Membrane HDM-2 by PNC-27 Induces Necrosis in Leukemia Cells But Not in Normal Hematopoietic Cells.


Journal

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

Informations de publication

Date de publication:
Sep 2020
Historique:
received: 31 05 2020
revised: 18 06 2020
accepted: 20 06 2020
entrez: 4 9 2020
pubmed: 4 9 2020
medline: 22 9 2020
Statut: ppublish

Résumé

Anticancer peptide PNC-27 binds to HDM-2 protein on cancer cell membranes inducing the formation of cytotoxic transmembrane pores. Herein, we investigated HDM-2 membrane expression and the effect of PNC-27 treatment on human non-stem cell acute myelogenous leukemia cell lines: U937, acute monocytic leukemia; OCI-AML3, acute myelomonocytic leukemia and HL60, acute promyelocytic leukemia. We measured cell surface membrane expression of HDM-2 using flow cytometry. Cell viability was assessed using MTT assay while direct cytotoxicity was measured by lactate dehydrogenase (LDH) release and induction of apoptotic markers annexin V and caspase-3. HDM-2 is expressed at high levels in membranes of U937, OCI-AML3 and HL-60 cells. PNC-27 can bind to membrane HDM-2 to induce cell necrosis and LDH release within 4 h. Targeting membrane HDM-2 can be a potential strategy to treat leukemia. PNC-27 targeting membrane HDM-2 demonstrated significant anti-leukemia activity in a variety of leukemic cell lines.

Sections du résumé

BACKGROUND/AIM OBJECTIVE
Anticancer peptide PNC-27 binds to HDM-2 protein on cancer cell membranes inducing the formation of cytotoxic transmembrane pores. Herein, we investigated HDM-2 membrane expression and the effect of PNC-27 treatment on human non-stem cell acute myelogenous leukemia cell lines: U937, acute monocytic leukemia; OCI-AML3, acute myelomonocytic leukemia and HL60, acute promyelocytic leukemia.
MATERIALS AND METHODS METHODS
We measured cell surface membrane expression of HDM-2 using flow cytometry. Cell viability was assessed using MTT assay while direct cytotoxicity was measured by lactate dehydrogenase (LDH) release and induction of apoptotic markers annexin V and caspase-3.
RESULTS RESULTS
HDM-2 is expressed at high levels in membranes of U937, OCI-AML3 and HL-60 cells. PNC-27 can bind to membrane HDM-2 to induce cell necrosis and LDH release within 4 h.
CONCLUSION CONCLUSIONS
Targeting membrane HDM-2 can be a potential strategy to treat leukemia. PNC-27 targeting membrane HDM-2 demonstrated significant anti-leukemia activity in a variety of leukemic cell lines.

Identifiants

pubmed: 32878773
pii: 40/9/4857
doi: 10.21873/anticanres.14488
doi:

Substances chimiques

Antineoplastic Agents 0
PNC-27 0
Tumor Suppressor Protein p53 0
L-Lactate Dehydrogenase EC 1.1.1.27
MDM2 protein, human EC 2.3.2.27
Proto-Oncogene Proteins c-mdm2 EC 2.3.2.27

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

4857-4867

Informations de copyright

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

Auteurs

Anusha Thadi (A)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Lauren Lewis (L)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Eve Goldstein (E)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Anshu Aggarwal (A)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Marian Khalili (M)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Lindsay Steele (L)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Boris Polyak (B)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A.

Shabnam Seydafkan (S)

Department of Pathology and Laboratory Medicine, SUNY Downstate Medical Center, Brooklyn, NY, U.S.A.

Martin H Bluth (MH)

Department of Pathology, Wayne State University School of Medicine, Detroit, MI, U.S.A.

Kristine A Ward (KA)

Department of Hematology and Oncology, Leukemia Program, University of Pennsylvania, Philadelphia, PA, U.S.A.

Michael Styler (M)

Department of Hematology and Oncology, Bone Marrow Transplant Program, Fox Chase Cancer Center, Philadelphia, PA, U.S.A.

Paul M Campbell (PM)

The Marvin and Concetta Greenberg Pancreatic Cancer Institute, Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, PA, U.S.A.

Matthew R Pincus (MR)

Department of Pathology and Laboratory Medicine, SUNY Downstate Medical Center, Brooklyn, NY, U.S.A. Wilbur.Bowne@jefferson.edu mrpincus2010@gmail.com.

Wilbur B Bowne (WB)

Division of Surgical Oncology, Department of Surgery, Drexel University College of Medicine, Philadelphia, PA, U.S.A. Wilbur.Bowne@jefferson.edu mrpincus2010@gmail.com.
Department of Surgery, Thomas Jefferson University, Sidney Kimmel Medical College, Philadelphia, PA, U.S.A.

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Classifications MeSH