Author: Gianpiero Pescarmona
Date: 27/01/2010


A phaeochromocytoma or pheochromocytoma, is a neuroendocrine tumor of the medulla of the adrenal glands (originating in the chromaffin cells), or extra-adrenal chromaffin tissue that failed to involute after birth [1] and secretes excessive amounts of catecholamines, usually adrenaline and noradrenaline.2 Extra-adrenal paragangliomas (often described as extra-adrenal pheochromocytomas) are closely related, though less common, tumors that originate in the ganglia of the sympathetic nervous system and are named based upon the primary anatomical site of origin.

Role of HIF

Papers pheochromocytoma HIF

Cyclic AMP represses the hypoxic induction of hypoxia-inducible factors in PC12 cells.
Torii S, Okamura N, Suzuki Y, Ishizawa T, Yasumoto K, Sogawa K.
J Biochem. 2009 Dec;146(6):839-44. Epub 2009 Aug 11.

Role of heme

pheochromocytoma SUCCINYL

Heme deficiency suppresses the expression of key neuronal genes and causes neuronal cell death.
Sengupta A, Hon T, Zhang L.
Brain Res Mol Brain Res. 2005 Jun 13;137(1-2):23-30. Epub 2005 Mar 17.

Synthesis of Arg-Gly-Asp (RGD) sequence conjugated thermo-reversible gel via the PEG spacer arm as an extracellular matrix for a pheochromocytoma cell (PC12) culture.
Park KH, Kim MH, Park SH, Lee HJ, Kim IK, Chung HM.
Biosci Biotechnol Biochem. 2004 Nov;68(11):2224-9.

An examination of heme action in gene expression: heme and heme deficiency affect the expression of diverse genes in erythroid k562 and neuronal PC12 cells.
Zhu Y, Lee HC, Zhang L.
DNA Cell Biol. 2002 Apr;21(4):333-46.

Succinate dehydrogenase

Papers Pheochromocytoma Succinate Dehydrogenase

Mitochondrion. 2009 Jul;9(4):254-60. Epub 2009 Mar 28.
Mutations in the heme b-binding residue of SDHC inhibit assembly of respiratory chain complex II in mammalian cells.

Lemarie A, Grimm S.

Respiratory chain complex II has been extensively studied but little is known about its assembly and the role of its heme group. Mutations in the phylogenetically conserved histidine 127 of the SDHC subunit have been shown to abrogate heme binding in yeast and bacteria without impairing complex II assembly or enzymatic activities. Here we show that in mammalian cells these mutations lead to a complete reduction of SDHC in mitochondria, a destabilisation of SDHD and SDHB, and to an abrogation of complex II enzymatic activities, suggesting that in mammalian cells complex II assembly is more complex than in lower organisms.

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