biomolecules
Review
Metformin and Cancer Glucose Metabolism: At the Bench or
at the Bedside?
Cecilia Marini
1,2,
*, Vanessa Cossu
3
, Matteo Bauckneht
2,3
, Francesco Lanfranchi
3
, Stefano Raffa
3
,
Anna Maria Orengo
2
, Silvia Ravera
4
, Silvia Bruno
4
and Gianmario Sambuceti
1,2
Citation: Marini, C.; Cossu, V.;
Bauckneht, M.; Lanfranchi, F.; Raffa,
S.; Orengo, A.M.; Ravera, S.; Bruno, S.;
Sambuceti, G. Metformin and Cancer
Glucose Metabolism: At the Bench or
at the Bedside? Biomolecules 2021, 11,
1231. https://doi.org/10.3390/
biom11081231
Academic Editor: Kateˇ rina Ka ˇ nková
Received: 14 July 2021
Accepted: 16 August 2021
Published: 18 August 2021
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4.0/).
1
CNR Institute of Molecular Bioimaging and Physiology (IBFM), 20054 Milan, Italy; Sambuceti@unige.it
2
IRCCS Ospedale Policlinico San Martino, 16132 Genoa, Italy; matteo.bauckneht@hsanmartino.it (M.B.);
annamaria.orengo@hsanmartino.it (A.M.O.)
3
Department of Health Sciences, University of Genoa, 16132 Genoa, Italy; vane.6291@gmail.com (V.C.);
dr.francescolanfranchi@gmail.com (F.L.); stefanoraffa@live.com (S.R.)
4
Department of Experimental Medicine, Human Anatomy, University of Genoa, 16132 Genoa, Italy;
silvia.ravera@unige.it (S.R.); silvia.bruno@unige.it (S.B.)
* Correspondence: Cecilia.Marini@unige.it; Tel.: +39-010-555-4812
Abstract: Several studies reported that metformin, the most widely used drug for type 2 diabetes,
might affect cancer aggressiveness. The biguanide seems to directly impair cancer energy asset,
with the consequent phosphorylation of AMP-activated protein kinase (AMPK) inhibiting cell
proliferation and tumor growth. This action is most often attributed to a well-documented blockage
of oxidative phosphorylation (OXPHOS) caused by a direct interference of metformin on Complex I
function. Nevertheless, several other pleiotropic actions seem to contribute to the anticancer potential
of this biguanide. In particular, in vitro and in vivo experimental studies recently documented
that metformin selectively inhibits the uptake of 2-[18F]-Fluoro-2-Deoxy-D-Glucose (FDG), via an
impaired catalytic function of the enzyme hexose-6P-dehydrogenase (H6PD). H6PD triggers a still
largely uncharacterized pentose-phosphate pathway (PPP) within the endoplasmic reticulum (ER)
that has been found to play a pivotal role in feeding the NADPH reductive power for both cellular
proliferation and antioxidant responses. Regardless of its exploitability in the clinical setting, this
metformin action might configure the ER metabolism as a potential target for innovative therapeutic
strategies in patients with solid cancers and potentially modifies the current interpretative model
of FDG uptake, attributing PET/CT capability to predict cancer aggressiveness to the activation of
H6PD catalytic function.
Keywords: metformin; glucose consumption; FDG PET/CT imaging; endoplasmic reticulum; tumor
metabolism; cancer therapy
1. Introduction
Since the 1950s, the biguanide metformin has been the most widely used antihy-
perglycemic drug to treat patients with type 2 diabetes. This drug exerts its effects by
reducing hepatic gluconeogenesis [1,2] and by increasing insulin sensitivity as well as glu-
cose consumption of peripheral tissues [3]. Besides this classical indication, a wide literature
proposed a potential efficacy of this biguanide in anticancer therapy, either alone or in com-
bination with other approaches [4]. The mechanisms underlying this action extend beyond
the antihyperglycemic action and possibly identify an anticancer potential of metformin in
nondiabetic patients.
As an obvious consequence, these expectations increased the interest in metformin up
to contaminate the field of basic research activity, as documented by the PubMed database
reported in Figure 1 that shows how (and when) the number of studies on experimental
animals and containing the terms “metformin” grew simultaneously with the expansion of
“non-clinical” studies containing the terms “metformin and cancer”.
Biomolecules 2021, 11, 1231. https://doi.org/10.3390/biom11081231 https://www.mdpi.com/journal/biomolecules