Cited by 326Iron Metabolism and DisordersNeurological diseases and metabolismTrace Elements in Health

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Regulation of Synthesis and Turnover of Ferritin in Rat Liver

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Drysdale, James W., Munro, Hamish N.·1966·Journal of Biological Chemistry

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Abstract

Synthesis of liver ferritin induced by iron administration was investigated by treating rats by injection with pulse doses of leucine-' 4 C at various times after a single intraperitoneal dose of iron.The iron caused a rapid but transient increase of leucine uptake into ferritin without affecting incorporation into mixed liver proteins; the ferritin response was dose-dependent and was followed by an increase in liver ferritin content.Since the action of iron was insensitive to actinomycin D, it was considered to be independent of synthesis of new messenger ribonucleic acid.Ferritin turnover was studied by following loss of radioactivity from liver ferritin over a 72-hour period after leucine-14C administration.Repeated injections of iron during this period increased the iron to protein ratio of ferritin and retarded loss of radioactivity, thus suggesting that iron-rich ferritin molecules are less susceptible than iron-poor molecules to degradation.With the use of a sucrose density gradient to separate ferritin species of differing iron content, it was shown that the first fraction to become labeled after injection of leucine-14 C was low in iron.Subsequently there was progressive transfer of the label to ferritin fractions richer in iron over a 72-hour period.Repeated injection of iron caused a larger proportion of the initial radioactivity of the iron-poor fraction to be retained as iron-rich ferritin.To explain the actions of iron on ferritin metabolism by a single unifying hypothesis, it is proposed that iron can cause an apparent induction by stabilizing an unstable precursor of ferritin which would otherwise be rapidly degraded, and that iron can also stabilize iron-poor ferritin molecules by increasing their iron content and thus retarding their degradation.There are now many examples (1-4) of increased levels of certain enzyme activities and nonenzymic proteins in mammalian

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Self-citation
FERRITIN IN THE FUNGUS PHYCOMYCES
David, C. N., & Easterbrook, K. B. (1971) · The Journal of Cell Biology · doi:10.1083/jcb.48.1.15 · Cited by 65
Ferritin in Human Liver Cells of Homozygous Beta‐Thalassaemia: Ultrastructural Observations
Iancu, T. C., & Neustein, H. B. (1977) · British Journal of Haematology · doi:10.1111/j.1365-2141.1977.tb01026.x · Cited by 65
On the Mechanism of Iron-induced Synthesis of Apoferritin in HeLa Cells
Chu, L. L. H., & Fineberg, R. A. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36427-x · Cited by 65
The iron-loaded cell--the cytopathology of iron storage. A review.
Richter, G. W. (1978) · PubMed Central · Cited by 64
The effect of mixed-function oxidation of enzymes on their susceptibility to degradation by a nonlysosomal cysteine proteinase
Rivett, A. J. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90540-5 · Cited by 62
Synthesis and Degradation of Mixed Proteins, and Composition Changes in Skeletal Muscle of Malnourished and Refed Rats
Young, V. R., Stothers, S. C., & Vilaire, G. (1971) · Journal of Nutrition · doi:10.1093/jn/101.10.1379 · Cited by 61
In vitro reconstitution of ferritin
Pape, L., Multani, J. S., Stitt, C., & Saltman, P. (1968) · Biochemistry · doi:10.1021/bi00842a014 · Cited by 59
Iron regulation of ferritin gene expression
Munro, H. N. (1990) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240440205 · Cited by 58
Self-citation
Abnormal Hepatic Iron Accumulation in LEC Rats
Kato, J., Kohgo, Y., Sugawara, N., Katsuki, S., Shintani, N., Fujikawa, K., Miyazaki, E., Kobune, M., Takeichi, N., & Niitsu, Y. (1993) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.1993.tb02859.x · Cited by 56
Clinical and Laboratory Studies on the Action of Desferrioxamine
Cumming, R. L. C., Millar, J. A., Smith, J. A. M., & Goldberg, A. (1969) · British Journal of Haematology · doi:10.1111/j.1365-2141.1969.tb01371.x · Cited by 56
Human Ferritin Gene Expression
Drysdale, J. W. (1988) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60612-1 · Cited by 55
Self-citation

Authors: Drysdale, J. W., & Munro, H. N.
Affiliations: Massachusetts Institute of Technology (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1966-08
Volume: 241
Issue: 15
Pages: 3630-3637
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)99877-7
OpenAlex: W1551118417
Cited by: 326
References: 23
Citations by year: 2024: 3 · 2023: 1 · 2022: 1 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 2
FWCI: 14.11
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 19808 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: ferritin, liver, iron, ferritin synthesis, leucine incorporation, actinomycin D, mRNA, protein degradation
MeSH terms: Animals, Dactinomycin, Ferritins, Leucine, Liver, RNA, Messenger, Rats, In Vitro Techniques

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Regulation of Synthesis and Turnover of Ferritin in Rat Liver

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