Midkine is a potent regulator of the catecholamine biosynthesis pathway in mouse aorta

Life Sciences
Laura EzquerraThomas F Deuel

Abstract

To discover regulatory pathways dependent on midkine (Mk the gene, MK the protein) signaling, we compared the transcriptional profiles of aortae obtained from Mk -/- and wild type (WT, +/+) mice; the comparison demonstrated an extraordinary high level expression of tyrosine hydroxylase (12-fold), the rate-limiting enzyme in catecholamine biosynthesis, DOPA decarboxylase (73-fold), and dopamine beta-hydroxylase (75-fold) in aortae of Mk -/- mice compared with aortae of WT (+/+) mice. Phenylethanolamine-N-methyltransferase, the enzyme catalyzing the conversion of norepinephrine into epinephrine, was not detected in either Mk -/- and WT (+/+) mouse aorta. The protein levels of tyrosine hydroxylase, DOPA decarboxylase and dopamine beta-hydroxylase confirmed the analysis of the transcriptional profiles. Surprisingly, MK failed to regulate the enzymes of the catecholamine biosynthesis pathway in 10 other tissues studied. Furthermore, the expression levels of the enzymes of catecholamine biosynthesis in aortae of Mk -/- mice were effectively the same as those in aortae of Pleiotrophin (Ptn the gene, PTN the protein) genetically deficient (Ptn -/-) mice when compared with WT (+/+) mice. The remarkable increases in levels of expression ...Continue Reading

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Citations

May 1, 2010·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Takashi Muramatsu
Jul 31, 2013·Pharmacology, Biochemistry, and Behavior·Marta Vicente-RodríguezGonzalo Herradón
Sep 19, 2017·Journal of Cardiovascular Development and Disease·Kathleen C Woulfe, Carmen C Sucharov

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