Phosphoglycerate mutase 1 in cancer: A promising target for diagnosis and therapy.


Journal

IUBMB life
ISSN: 1521-6551
Titre abrégé: IUBMB Life
Pays: England
ID NLM: 100888706

Informations de publication

Date de publication:
10 2019
Historique:
received: 15 03 2019
accepted: 22 05 2019
pubmed: 7 6 2019
medline: 16 5 2020
entrez: 7 6 2019
Statut: ppublish

Résumé

Altered enzymatic machineries are a substantial biochemical characteristic of tumor cell metabolism that switch metabolic profile from oxidative phosphorylation to amplified glycolysis as well as increased lactate production under hypoxia conditions. Reprogrammed metabolic profile is an emerging hallmark of cancer. Overexpression of several glycolytic enzymes and glucose transporters has been reported in 24 different types of cancers that represent approximately 70% of all the cancer cases around the globe. Thus, targeting glycolytic enzymes could serve as tempting avenue for drug design against cancer. Phosphoglycerate mutase 1 (PGAM1) is an important glycolytic enzyme that catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate. Recent investigations have revealed the overexpression of PGAM1 in several human cancers that is linked with tumor growth, survival, and invasion. The aim of this review is to update scientific research network with cancer-specific role of PGAM1 to elucidate its capability as bonafide therapeutic target for cancer therapy. Moreover, we have also summarized the reported genetic and pharmacological inhibitors of PGAM1. This study suggests that further investigations on PGAM1 should focus on the exploration of molecular mechanisms of PGAM1 overexpression in development of cancer, assessment of biosafety profiles of known inhibitors of PGAM1, and utilization of PGAM1 inhibitors in combinatorial therapies. These future studies will surely support the unbiased strategies for the development of novel PGAM1 inhibitors for cancer therapies.

Identifiants

pubmed: 31169978
doi: 10.1002/iub.2100
doi:

Substances chimiques

Glyceric Acids 0
3-phosphoglycerate 820-11-1
Phosphoglycerate Mutase EC 5.4.2.11
phosphoglycerate mutase 1, human EC 5.4.2.11

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

1418-1427

Informations de copyright

© 2019 International Union of Biochemistry and Molecular Biology.

Références

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Auteurs

Farzana Sharif (F)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Azhar Rasul (A)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Asma Ashraf (A)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Ghulam Hussain (G)

Department of Physiology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Tahira Younis (T)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Iqra Sarfraz (I)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Muhammad Asrar Chaudhry (MA)

Department of Zoology, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Shazia A Bukhari (SA)

Department of Biochemistry, Faculty of Life Sciences, Government College University Faisalabad (GCUF), Pakistan.

Xin Y Ji (XY)

Henan International Joint Laboratory of Protein Regulation, College of Medicine, Henan University, Kaifeng, Henan, China.

Zeliha Selamoglu (Z)

Department of Medical Biology, Faculty of Medicine, Nigde Ömer Halisdemir University, Turkey.

Muhammad Ali (M)

Quaid-e-Azam University, Islamabad, Pakistan.

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Classifications MeSH