Mathieu Ferron, PhD
Assistant Professor of Medicine
Canada Research Chair in Bone and Energy Metabolism
Biographical Sketch
After completing his undergraduate degree in Biochemistry at
the University of Montreal, Dr Ferron joined the laboratory of Dr Jean Vacher
within the Institut de Recherches Cliniques de Montreal (IRCM). There, he studied
bone metabolism and in particular the molecular mechanisms regulating the
differentiation of osteoclasts and completed his PhD in 2006, with focus on inositol
polyphosphate 4-phosphatases functions in bone remodeling and bone mass. Dr Ferron
moved to New York in 2006 to join the laboratory of Dr Gerard Karsenty at Columbia
University as a post-doctoral fellow, where he studied a novel endocrine link between
bones and glucose metabolism.
In 2013, he came back to the Institut de Recherches Cliniques de
Montreal (IRCM) to start his own laboratory, where he is interested in the function
of bone as an endocrine organ and in the role of vitamin K in glucose metabolism. His
primary academic affiliation is with University of Montreal where he currently holds
an appointment as Assistant Professor within the Faculty of Medicine.
Dr Ferron holds the Canada Research Chair in Bone and Energy
Metabolism.
Click here for pdf CV
Selected Scientific Contributions
During is postdoctoral training Dr Ferron became interested in a
novel endocrine interaction between bones and glucose metabolism. He contributed to
the discovery that osteocalcin is a bone-derived hormone stimulating insulin secretion
and insulin sensitivity. He demonstrated that injections or infusions of recombinant
osteocalcin in mice could be a therapeutic approach for the treatment of diet-induced
obesity and insulin resistance. Dr Ferron also established that insulin signaling in
bone cells, in particular in osteoblasts, was implicated in the control of whole body
glucose homeostasis. Dr Ferron work also includes several studies on bone metabolism,
in particular on the function and differentiation of osteoclasts and osteoblasts.
Click here for PubMed listing
Research Interests
Current projects in the laboratory fall into two areas:
Endocrine functions of bone and osteocalcin. It
was discovered recently that bone functions not only as a scaffold for the rest of the
body, but also as an endocrine organ. Bone cells secrete at least one hormone,
osteocalcin, produced specifically by osteoblasts, which is implicated in the control
of glucose metabolism. Our recent work has focused mainly on the regulation of
osteocalcin activity by other hormones, including insulin, and the effect of
osteocalcin on insulin secretion and insulin sensitivity. We are now interested in
identifying and characterizing novel physiological and pathological roles of
osteocalcin. We are also aiming to isolate additional bone-derived hormone(s), or
"osteokines", involved in bone endocrine function.
Physiological and pathological function of vitamin K and
γ-carboxylation. The only known biological function of vitamin K is to
serve as a co-factor for the γ-glutamyl carboxylase (GGCX), an enzyme
responsible for the conversion of glutamic acid residues (GLU) into
γ-carboxyglutamic acid (GLA) residues in specific secreted proteins. This
posttranslational modification is found in some coagulation factors (prothrombin,
factor IX, etc.), in MGP, a protein implicated in tissue mineralization, and in
osteocalcin, a bone-derived hormone affecting glucose metabolism. However, we still
don't know all the γ-carboxylated proteins and their functions. Recent findings
in humans and rodents suggest that vitamin K and γ-carboxylation may be involved
in the control of energy metabolism and the development of obesity and diabetes. Our
current goal is to address γ-carboxylation function in glucose metabolism in
vivo through the generation of tissue-specific knockout mice for the enzymes
implicated in this process. We are also planning to characterize, in a non-bias
proteomic approach, the "γ-carboxylome" (i.e. identifying all the GLA
proteins produced in tissues were the γ-glutamyl carboxylase is active).
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