Novel zinc-responsive post-transcriptional mechanisms reciprocally regulate expression of the mouse Slc39a4 and Slc39a5 zinc transporters (Zip4 and Zip5)
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Benjamin P. Weaver
Abstract
Dietary zinc deficiency in mice is accompanied by enhanced expression of the zinc uptake transporter Slc39a4 (Zip4) and repressed expression of Slc39a5 (Zip5) in tissues which regulate zinc homeostasis (intestine, pancreas and visceral yolk sac). Herein, mechanisms controlling this differential expression were investigated. The induction of Zip4 mRNA during zinc deficiency, and its repression in response to zinc repletion were found to reflect changes in Zip4 mRNA stability and not changes in the relative rate of transcription of this gene. During zinc deficiency, ZIP4 protein levels are increased and this protein is localized on the apical membranes. Administration of an oral gavage of zinc caused ZIP4 internalization and degradation in enterocytes and visceral endoderm cells. Similarly, ZIP4 is induced by zinc deficiency in cultured mouse Hepa cells and is rapidly degraded in response to added zinc. Zip5 mRNA abundance does not change in response to zinc, but the translation of this mRNA was found to be zinc-responsive. During zinc deficiency, Zip5 mRNA remains associated with polysomes, while the protein is internalized and degraded in enterocytes, acinar cells and endoderm cells. After zinc-gavage, ZIP5 is rapidly resynthesized and targeted to the basolateral membranes of these cell types.
©2007 by Walter de Gruyter Berlin New York
Articles in the same Issue
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- A semi-rational design strategy of directed evolution combined with chemical synthesis of DNA sequences
- Novel zinc-responsive post-transcriptional mechanisms reciprocally regulate expression of the mouse Slc39a4 and Slc39a5 zinc transporters (Zip4 and Zip5)
- Lumazine proteins from photobacteria: localization of the single ligand binding site to the N-terminal domain
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- Overexpression and mass spectrometry analysis of mature human acid ceramidase
- Ultraviolet B radiation induces cell shrinkage and increases osmolyte transporter mRNA expression and osmolyte uptake in HaCaT keratinocytes
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- Acknowledgment
- Contents Biological Chemistry, Volume 388, 2007
- Author Index
- Subject Index
Articles in the same Issue
- FOXM1, a typical proliferation-associated transcription factor
- Salivary agglutinin/glycoprotein-340/DMBT1: a single molecule with variable composition and with different functions in infection, inflammation and cancer
- A semi-rational design strategy of directed evolution combined with chemical synthesis of DNA sequences
- Novel zinc-responsive post-transcriptional mechanisms reciprocally regulate expression of the mouse Slc39a4 and Slc39a5 zinc transporters (Zip4 and Zip5)
- Lumazine proteins from photobacteria: localization of the single ligand binding site to the N-terminal domain
- SARS-CoV accessory protein 7a directly interacts with human LFA-1
- Overexpression and mass spectrometry analysis of mature human acid ceramidase
- Ultraviolet B radiation induces cell shrinkage and increases osmolyte transporter mRNA expression and osmolyte uptake in HaCaT keratinocytes
- Macrophage paraoxonase 2 (PON2) expression is upregulated by unesterified cholesterol through activation of the phosphatidylinositol 3-kinase (PI3K) pathway
- Acknowledgment
- Contents Biological Chemistry, Volume 388, 2007
- Author Index
- Subject Index
