Literature DB >> 34094663

ENO1 monoclonal antibody inhibits invasion, proliferation and clone formation of cervical cancer cells.

Yuanfeng Gou1,2, Fei Li3, Xiaqin Huo1,2, Chunyan Hao3, Xiaojuan Yang1,2, Yaping Pei1,2, Na Li1,2, Huiling Liu1,2, Bingdong Zhu3.   

Abstract

α-enolase (ENO1), highly expressing in cell membranes, cytoplasm and nuclei of cervical cancer and other tumors, acts as a plasminogen receptor and a glycolytic enzyme. ENO1 is found to be associated with tumorigenesis, invasion and migration, and proves to be an ideal target of tumor therapy. In this study, ENO1 monoclonal antibodies (ENO1mAb) was prepared to blockade ENO1 and the therapeutic role was observed in cervical cancer cells. First, ENO1mAb was prepared and screened by evaluating the inhibitory effect on migration and invasion of cervical cancer cells, which is supposed to block ENO1 expressed on cell membrane. Second, folic acid (FA) conjugated PLGA nanoparticles (FA-SS-PLGA) targeting tumor cells were prepared to mediate ENO1mAb entry into cells and its anti-tumor effects were investigated in vitro. We found that PLGA/FA-SS-PLGA nanoparticles-mediated ENO1mAb could antagonize the activity of ENO1 enzyme, significantly decreased the contents of lactic acid and pyruvate, and inhibited the proliferation, migration and clone formation of cervical cancer cells compared with the sham control (P < 0.05). In summary, ENO1mAb could specifically block ENO1 expressed on cell membrane and inhibit ENO1 glycolysis enzyme activity inside tumor cells, and plays a therapeutic role against cervical cancer cells. It suggests that ENO1mAb has promising anti-tumor effects. AJCR
Copyright © 2021.

Entities:  

Keywords:  ENO1; PLGA nanoparticles; cervical cancer; glycolysis; monoclonal antibody

Year:  2021        PMID: 34094663      PMCID: PMC8167678     

Source DB:  PubMed          Journal:  Am J Cancer Res        ISSN: 2156-6976            Impact factor:   6.166


  51 in total

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6.  Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-Enolase.

Authors:  Roser López-Alemany; Colin Longstaff; Stephen Hawley; Massoud Mirshahi; Pere Fábregas; Merce Jardí; Elizabeth Merton; Lindsey A Miles; Jordi Félez
Journal:  Am J Hematol       Date:  2003-04       Impact factor: 10.047

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9.  Development and characterization of hyaluronic acid modified PLGA based nanoparticles for improved efficacy of cisplatin in solid tumor.

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10.  SF2312 is a natural phosphonate inhibitor of enolase.

Authors:  Paul G Leonard; Nikunj Satani; David Maxwell; Yu-Hsi Lin; Naima Hammoudi; Zhenghong Peng; Federica Pisaneschi; Todd M Link; Gilbert R Lee; Duoli Sun; Basvoju A Bhanu Prasad; Maria Emilia Di Francesco; Barbara Czako; John M Asara; Y Alan Wang; William Bornmann; Ronald A DePinho; Florian L Muller
Journal:  Nat Chem Biol       Date:  2016-10-10       Impact factor: 15.040

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  2 in total

1.  Alpha-Enolase (ENO1) Correlates with Invasiveness of Cutaneous Melanoma-An In Vitro and a Clinical Study.

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Journal:  Diagnostics (Basel)       Date:  2022-01-20

2.  FAM126A interacted with ENO1 mediates proliferation and metastasis in pancreatic cancer via PI3K/AKT signaling pathway.

Authors:  Yongning Li; Ying Li; Jun Luo; Xueqin Fu; Peng Liu; Songbai Liu; Yaozhen Pan
Journal:  Cell Death Discov       Date:  2022-05-05
  2 in total

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