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  • Title: Effects of hypoxia and intracellular iron chelation on hypoxia-inducible factor-1alpha and -1beta in the rat carotid body and glomus cells.
    Author: Baby SM, Roy A, Mokashi AM, Lahiri S.
    Journal: Histochem Cell Biol; 2003 Nov; 120(5):343-52. PubMed ID: 14600837.
    Abstract:
    The present investigation provides for the first time, unambiguous information on the occurrence of hypoxia-inducible factors (HIF-1alpha and HIF-1beta proteins) in normoxia (Nx) and their interaction with hypoxia (Hx) and intracellular Fe(2+) chelation in the rat carotid body (CB) glomus cells. HIF-1alpha bound to HIF-1beta translocated into the nucleus is identified on the basis of immunohistochemistry and immunofluorescence. In Nx, a weak expression of HIF-1alpha was observed in CB glomus cells. However, exposure of CB and glomus cells to Hx (Po(2) approximately 7 Torr) and Nx with ciclopirox olamine (CPX, 5 microM) for 1 h showed a significant ( P<0.001) increase in HIF-1alpha protein. The CBs and glomus cells exposed to Nx, Hx, and Nx with CPX showed a constant level of HIF-1beta protein expression. HIF-1alpha subunit is continuously synthesized and degraded under normoxic conditions, while it accumulates rapidly following exposure to low oxygen tensions. Hydroxylation of HIF-1alpha by prolyl hydroxylase for proteasomal degradation was dependent on iron, 2-oxoglutarate, and oxygen concentration. The intracellular iron that acts as a cofactor for prolyl hydroxylase activity belongs to the labile iron pool and can be easily chelated. Thus, chelation of intracellular labile iron by CPX in Nx significantly increased HIF-1alpha in CB glomus cells. Thus, the results are consistent with the hypothesis that HIF-1alpha which is present in the glomus cells translocates to the nucleus during exposure to Hx and to CPX in Nx.
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