Associate Professor Mary Hunt


Technicians Diploma in Applied Science (Applied Biology)

Graduateship of the Institute of Biology

PhD. (Medical Biochemistry)


I graduated in 1994 with a Technicians Diploma in Applied Science – Applied Biology (with Distinction) from Dublin Institute of Technology (DIT) and in 1995 obtained a Graduateship of the Institute of Biology (with Distinction) from DIT. As part of my undergraduate studies, I undertook an Erasmus student placement at Karolinska Institute, Stockholm, Sweden in 1995 and accepted a post-graduate research position at the Karolinska Institute in Stockholm in 1996. My post-graduate research was focussed on novel enzymes in acyl-CoA metabolism, under the mentorship of Professor Stefan Alexson, Division of Clinical Chemistry, Karolinska Institute, Sweden. I defended my thesis in November 2001, entitled ‘Characterization of peroxisome proliferator-activated receptor alpha (PPARa) regulated acyl-CoA thioesterases involved in lipid metabolism’. Following completion of my PhD I spent a post-doctoral period at the Laboratory of Professor Ronald Wanders, Amsterdam Medical Centre, Amsterdam, The Netherlands, identifying patients with underlying acyl-CoA thioesterase deficiencies.

I subsequently returned to the Karolinska Institute in 2003, where I was awarded a stipend from AFA Insurance Jubilee Foundation, Sweden to continue my research.  In 2007 I obtained a research position at the Department of Genetics, Microbiology and Toxicology and was appointed Associate Professor in Molecular Genetics in 2008. I returned to the School of Biological Sciences at Dublin Institute of Technology in August 2010 to take up a position as Assistant Head of School.


Research Profile:



+353-1-402 4753


Publication list

Primary peer reviewed publications

1. Waluk, D., Schultz, N.,and Hunt, M. C. Identification of glycine N-acyltransferase-like 2 (GlyatL2) as a transferase that produces N-acyl glycines in humans. FASEB J. (2010) 24(8): 2795-2803.

2. Buch, C., Hunt, M. C., Alexson, S. E. H and Hallberg, E. Localization of peroxisomal matrix proteins by photobleaching Biochem. Biophys. Res. Commun. (2009) 338(2): 355-359.

3. Reilly, S-J., Tillander, V., Ofman, R, Alexson, S. E. H. and Hunt M. C. The nudix hydrolase 7 is a peroxisome proliferator-activated receptor alpha target gene involved in acyl-CoA metabolism in peroxisomes. J. Biochem. (2008) 144(5): 655-663.

4. Westin M. A., Hunt M. C., and Alexson S. E. H.Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of b-oxidation products out of peroxisomes. Cell. Mol. Life Sci. (2008) 65(6):982-90.

5. Westin, M. A. K., Hunt, M. C. and Alexson, S. E. H.Peroxisomes contain a specific phytanoyl-CoA/pristanoyl-CoA thioesterase acting as a novel auxiliary enzyme in alpha- and beta-oxidation of methyl-branched fatty acids in mouse. J. Biol. Chem. (2007) 282(27): 26707-26716.

6. Lundåsen T, Hunt M. C., Nilsson L.M., Sanyal, S., Angelin, B., Alexson S. E. H. and Rudling M. PPARalpha is a key regulator of hepatic FGF21. Biochem. Biophys. Res. Commun. (2007) 360(2):437-440.

7. Hunt, M. C., Greene, S., Hultenby, K., Svensson, L. T., Engberg, S. and Alexson, S. E. H. Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products. Cell. Mol. Life Sci. (2007) 64(12):1558-1570.

8. Dongol, B, Shah, Y., Kim, I., Gonzalez, F. J. and Hunt, M. C. The acyl-CoA thioesterase I (Acot1) is regulated by the peroxisome proliferator-activated receptor alpha and hepatocyte nuclear factor 4 alpha via a distal response element in the promotor. J. Lipid Res. (2007) 48(8): 1781-1791.

9. Reilly, S. J., O’Shea, E., O’Byrne, J., Alexson, S. E. H. and Hunt, M. C. A peroxisomal acyltransferase in mouse identifies a novel pathway for taurine conjugation of fatty acids. FASEB J. (2007) 21:99-107 

10. Hunt, M. C., Rautanen, A., Westin, M. A. K., Svensson, L. T., Alexson, S. E. H. Analysis of mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent functional evolution results in a reduced number of peroxisomal ACOTs. FASEB J. (2006) 20 (11) 1855-1864.

11. Westin M. A., Hunt M. C., and Alexson S. E. H. The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. J. Biol. Chem. (2005) 280 (46):38125-38132.

12. Hunt, M. C., Ruiter J., Mooyer, P., van Roermond C., Ijlst L. and Wanders R. J. A. Identification of fatty acid oxidation disorder patients with lowered acyl-CoA thioesterase activity in human skin fibroblasts. Eur. J. Clin. Invest. (2005) 35:38-46.

13. Solaas K, Kase B.F., Pham V, Bamberg K, Hunt M.C. and Alexson S.E.H. Differential regulation of cytosolic and peroxisomal bile acid amidation in mouse liver: PPARalpha activation favors formation of unconjugated bile acids. J. Lipid Res. (2004) 45 (6): 1051-1060.

14. Westin M. A., Alexson S. E. H. and Hunt M. C. Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARa) regulated peroxisomal acyl-CoA thioesterases. J. Biol. Chem. (2004) 279 (21): 21,841-21,848.

15. O’Byrne, J., Hunt, M. C., Rai, D. K., Saeki, M., Alexson, S. E. H. The human bile acid-CoA:amino acid N-acyltransferase functions in conjugation of fatty acids to glycine. J. Biol. Chem. (2003) 278 (36) 34237-34244.

16. Hunt, M. C., Solaas, K., Kase, B. F. and Alexson, S. E. H. Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. J. Biol. Chem. (2002) 277 (2) 1128-1138.

17. Hansson, M., Ellis, E., Hunt, M. C., Schmitz, G., Babiker, A. Marked induction of sterol 27-hydroxylase (CYP27) activity and mRNA levels during differentiation of human cultured monocytes into macrophages. Biochim. Biophys. Acta (2003) 1593: 283-289.

18. Hunt, M. C., Yang, Y. Z., Eggertsen, G., Carneheim, C. M., Gåfvels, M., Einarsson, C. and Alexson, S. E. H. The Peroxisome Proliferator-Activated Receptor Alpha (PPARa) regulates Bile Acid Biosynthesis. J. Biol. Chem. (2000) 275 (37) 28947-28953.

19. Hunt, M. C., Lindquist, P. J. G., Peters, J. M., Gonzalez, F. J., Diczfalusy, U., and Alexson, S. E. H. Involvement of the peroxisome proliferator-activated receptor a in regulating long chain acyl-CoA thioesterases. J. Lipid Res. (2000)  41:814-823.

20. Hunt, M. C., Nousiainen, S. E. B., Huttunen, M. K., Orii, K. J., Svensson, L. T., and Alexson, S. E. H. Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism. J. Biol. Chem. (1999) 274 (48): 34317-34326.


Review articles

1. Hunt, M. C., Alexson, S. E. H. Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism. Review article. Prog. Lipid Res. (2008) 47(6): 405-421.

2. Hunt, M. C., Yamada, J., Maltais, L. J., Wright, M., Podesta, E. J. And Alexson, S. E. H. A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases. J. Lipid Res. (2005) 46:2029-2032.

3. Hunt, M. C. and Alexson, S. E. H. The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Invited review article. Prog. Lipid Res. (2002) 41: 99-130. 


Peer reviewed conference proceedings

I. Hunt. M. C., O’Shea, E., Solaas, K. Kase, B. F. and Alexson S. E. H. New insights into bile acid amidation. Falk Symposium 141 ‘Bile acid biology and its therapeutic implications’. XVIII International bile acid meeting. Springer (2005) 41-50.

II. Hunt, M. C., Yang, Y. Z., Eggertsen, G., Carneheim, C. M., Gåfvels, M., Einarsson, C. and Alexson, S. E. H. The Peroxisome Proliferator-Activated Receptor Alpha (PPARa) is involved in Bile Acid Biosynthesis. Proceedings of ‘Biology of bile acids in health and disease’, XVI International Bile acid meeting. Kluwer Academic Publishers. (2001). 43-53

III. Hunt, M. C., Lindquist, P.J.G., Nousiainen, S., Huttunen, M., Orii, K., Svensson, T.L.T., Aoyama, T., Hashimoto, T., Diczfalusy, U. and S.E.H. Alexson. Acyl-CoA thioesterases belong to a novel gene family of peroxisome proliferator-regulated enzymes involved in lipid metabolism. Cell Biochemistry and Biophysics (2000), 32:317-324.

Conference Abstracts:

I have presented over 40 Conference Abstracts for poster or oral presentation and have attended 28 National and International Conferences.


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