Abstract

This research will explore the regulation of ferritin phenotypes in mammalian cells. Using a combination of translational assays and cloned DNA hybridization techniques, shall investigate ferritin gene expression in normal and iron-loaded rat liver and Hela cells. cDNA to rat and human ferritin mRNAs will be cloned. These probes will be used to determine the number and distribution of ferritin mRNA species in free and membrane-bound polysomes and in messenger ribonucleoprotein (mRNP) particles. The structural relationships of ferritin mRNAs will be determined by sequencing. The number and chromosomal arrangement of ferritin genes will be examined to determine whether the different ferritin mRNAs arise from differential splicing of a common nuclear transcipt or from two or more genes. Factors regulating the rate of ferritin subunit synthesis will be explored, with particular attention to the role of ferritin mRNP particles in translational control. Developmental aspects of ferritin gene expression will be examined in Friend cells in collaborative studies. Finally, in other collaborative studies, we shall explore the possibility that abnormalities in ferritin gene expression are related to known abnormalties in iron metabolism.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
5R01AM017775-12
Application #
3151087
Study Section
Pathobiochemistry Study Section (PBC)
Project Start
1977-07-01
Project End
1986-08-31
Budget Start
1985-09-01
Budget End
1986-08-31
Support Year
12
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Tufts University
Department
Type
Schools of Medicine
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code

  Publications

Zheng, H D; Bhavsar, D; Drysdale, J (1995) An unusual human ferritin H sequence from chromosome 4. DNA Seq 5:173-5
Zheng, H; Bhavsar, D; Volz, A et al. (1994) Exclusion of ferritins and iron-responsive element (IRE)-binding proteins as candidates for the hemochromatosis gene. Hum Genet 94:159-64
Bhavsar, D; Zheng, H; Drysdale, J (1994) Chimerism in PCR products from a multigene family. Biochem Biophys Res Commun 205:944-7
Papadopoulos, P; Bhavsar, D; Zappone, E et al. (1992) A second human ferritin H locus on chromosome 11. Cytogenet Cell Genet 61:107-8
Mauvieux, V; Dugast, I; el Kahloun, A et al. (1991) A HindIII RFLP at the FTHP1 locus on chromosome 6. Nucleic Acids Res 19:3762
Summers, K M; Tam, K S; Bartley, P B et al. (1991) Fine mapping of a human chromosome 6 ferritin heavy chain pseudogene: relevance to haemochromatosis. Hum Genet 88:175-8
Chorney, M J; Le Gall, J Y; Drysdale, J W (1991) D6S110 detects polymorphic HindIII fragments associated with individual HLA-A class I haplotypes. Nucleic Acids Res 19:200
Zappone, E; Dugast, I; Papadopoulos, P et al. (1991) Polymorphism in a ferritin H gene from chromosome 6p. Hum Genet 86:557-61
Dugast, I J; Papadopoulos, P; Zappone, E et al. (1990) Identification of two human ferritin H genes on the short arm of chromosome 6. Genomics 6:204-11
Beaumont, C; Dugast, I; Renaudie, F et al. (1989) Transcriptional regulation of ferritin H and L subunits in adult erythroid and liver cells from the mouse. Unambiguous identification of mouse ferritin subunits and in vitro formation of the ferritin shells. J Biol Chem 264:7498-504

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