Iron transport and storage

Crichton, Robert R.; Charloteaux-Wauters, Mireille

doi:10.1111/j.1432-1033.1987.tb11155.x

Cited by 489 publications

(253 citation statements)

References 301 publications

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“…The finding that low oxygen concentration also increases iron release from hepatocytes, 0.9-2.5 6.5 together with the fact that iron is most readily mobilized from ferritin under reducing conditions [26], may be indicative of a reduction process. Speculations in this direction have been presented in discussions on iron release from BeWo choriocarcinoma cells [77].…”

Section: Release Of Iron From Hepatocytesmentioning

confidence: 93%

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The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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INTRODUCTIONThe role of transferrin and its cell surface receptor in cellular iron metabolism has received considerable interest during the last decade. Hence, over this period several reviews covering various aspects of the topic have been published.In this review we attempt to summarize the new knowledge and controversies encountered during the last 4-5 years. The focus is on iron metabolism by the hepatocyte. We also view the concept of transferrin-cell interactions from angles which previously may not have been given particular attention, and we include some aspects of iron metabolism not normally covered by reviews of this type. Central parts of what may be regarded as well-established knowledge either have been entirely omitted, or are only briefly described or mentioned to the extent considered relevant to the particular topic discussed. Important aspects of iron metabolism such as iron adsorption, haemochromatosis, ferritin iron and iron in infection and neoplasia are not covered in the present paper. Instead, the reader is referred to one or more of the recently published reviews [1-5] and references therein.

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Section: Release Of Iron From Hepatocytesmentioning

confidence: 93%

“…However, following entry into the protein core ferrous iron is oxidized to the ferric state, and release of iron from ferritin is best achieved under reducing conditions [26]. Furthermore, biosynthesis of haem requires ferrous iron for insertion into the porphyrin moiety [27].…”

Section: Reductive Iron Releasementioning

confidence: 99%

The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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“…One of the major branches of this family is the so-called mammaliantype ferritins, which have been widely studied, and are found in mammals, fish, invertebrates, and other eukaryotes [2][3][4][5][6]. The structure of horse spleen ferritin has been determined by single-crystal X-ray diffraction analysis and consists of 24 subunits of approx.…”

Section: Introductionmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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Two distinct ferritin like iron containing proteins have been identified and isolated from the fungus Absidia spinosa; one from the spores and another from the mycelia. The mycelial protein has been purified and consists of two subunits of approx. 20 kDa. The N-terminal sequences of both subunits have been determined. The holoprotein as isolated contains approx. 750 iron atoms/molecule and exhibits a beme-like UV-Vis spectrum. Based on the beme spectrum and the high degree of sequence homology found, it has been established that the mycelial protein is a bacterioferritin. This is the first example demonstrating the presence of a bacterioferritin in a eukaryotic organism.

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“…These proteins have association constants for ferric ion of more than 1022 and are normally only partly saturated (7). To scavenge this essential nutrient from such a hostile iron-restricted environment, many bacterial pathogens produce and secrete low-molecular-weight, Fe (III)-specific ligands, termed siderophores, and express cognate cell surface receptors which bind respective ferric siderophore complexes as the first step in the iron uptake pathway (3,13,25,26,32).…”

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confidence: 99%

Siderophore‐Mediated Utilization of Iron Bound to Transferrin by Vibrio parahaemolyticus

Yamamoto

Okujo

Matsuura

et al. 1994

Microbiology and Immunology

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Vibrio parahaemolyticus produces a structurally novel type of siderophore, termed vibrioferrin, in response to iron-limitation. This study was performed to examine whether vibrioferrin can assimilate iron from human iron-binding proteins for growth. Comparison of the growth rates between V. parahaemolyticus AQ 3354 and its spontaneously arising, vibrioferrindeficient mutant revealed that vibrioferrin was able to sequester iron from 30% iron-saturated human transferrin for growth, but not from human lactoferrin even if fully saturated with iron. In both strains, iron limitation induced two high-molecular-weight outer membrane proteins with apparent molecular masses of approximately 78 and 83 kDa. Since only the outer membrane fraction including these proteins showed a binding capacity to ferric vibrioferrin complex, either of them may function as its cell surface receptor. These results suggested that the organism might utilize such a source of host iron through the action of vibrioferrin during in vivo survival and proliferation, although its importance in pathogenesis is unknown.

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Iron transport and storage

Cited by 489 publications

References 301 publications

The role of transferrin in the mechanism of cellular iron uptake

The role of transferrin in the mechanism of cellular iron uptake

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Siderophore‐Mediated Utilization of Iron Bound to Transferrin by Vibrio parahaemolyticus

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