Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin

Quintana, Carmen; Cowley, J. M.; Marhic, C.

doi:10.1016/j.jsb.2004.03.001

Cited by 170 publications

(167 citation statements)

References 49 publications

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“…The structure of the iron core in ferritin is intensively studied by various structural techniques such as electron nanodiffraction and high resolution electron microscopy. As a result, various models of the corefrom monocrystalline to polyphasic -have been suggested [29][30][31][32][33]. It should be noted that Mössbauer spectra of ferritin and its analogues, both in paramagnetic and magnetic states, were also fitted using different approaches: 1) using a model-free way with a distribution function of quadrupole splitting or magnetic hyperfine field, 2) using one quadrupole doublet or one magnetic sextet, 3) using more than one spectral component.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

Dubiel

Cieślak

Alenkina

et al. 2014

Journal of Inorganic Biochemistry

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An iron-polymaltose complex Ferrum Lek used as antianemic drug and considered as a ferritin analogue and human liver ferritin were investigated in the temperature range of 295-90 K by means of 57 Fe Mössbauer spectroscopy with a high velocity resolution (in 4096 channels). The Debye temperatures Ө D =50224 K for Ferrum Lek and Ө D =46116 K for human liver ferritin were determined from the temperature dependence of the center shift obtained using two different fitting procedures.

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Section: Introductionmentioning

confidence: 99%

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

Dubiel

Cieślak

Alenkina

et al. 2014

Journal of Inorganic Biochemistry

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“…Due to the large amount of iron nuclei stored in the center of the molecule, ferritin can also be detected by highenergy electron imaging techniques [16][17][18][19] without any additional heavy metal staining. Though these techniques lead to radiation damage of the protein shell, they allow for subsequent cross-validation in terms of presence and location of the molecule.…”

mentioning

confidence: 99%

Non-destructive imaging of an individual protein

et al. 2012

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The mode of action of proteins is to a large extent given by their ability to adopt different conformations. This is why imaging single biomolecules at atomic resolution is one of the ultimate goals of biophysics and structural biology. The existing protein database has emerged from X-ray crystallography, NMR or cryo-TEM investigations. However, these tools all require averaging over a large number of proteins and thus over different conformations. This of course results in the loss of structural information. Likewise it has been shown that even the emergent X-FEL technique will not get away without averaging over a large quantity of molecules. Here we report the first recordings of a protein at sub-nanometer resolution obtained from one individual ferritin by means of low-energy electron holography. One single protein could be imaged for an extended period of time without any sign of radiation damage. Since ferritin exhibits an iron core, the holographic reconstructions could also be cross-validated against TEM images of the very same molecule by imaging the iron cluster inside the molecule while the protein shell is decomposed

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“…Bone interstitial fluid flow is also believed to aid in delivering nutrients and transporting metabolic waste products from the bone cells [17]. To better understand interstitial fluid movement in bone, techniques using markers or tracers such as procion red (300-400 Da, diameter <1 nm), reactive red (1470 Da, diameter ~1 nm), microperoxidase (1860 Da, diameter ~2 nm), horseradish peroxidase (40 kDa, diameter ~6 nm), ferritin (440 kDa, diameter ~12 nm [20]), and different-sized dextrans (range 300 Da-2000 kDa, diameter ~1 nm-60 nm) have been used to map how different sized molecules travel through the various porosities in bone [1,5,8,[13][14][15][16]19,[22][23][24].…”

Section: Introductionmentioning

confidence: 99%

Mapping bone interstitial fluid movement: Displacement of ferritin tracer during histological processing

Ciani¹,

Doty²,

Fritton³

2005

Bone

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Bone interstitial fluid flow is thought to play a fundamental role in the mechanical stimulation of bone cells, either via shear stresses or cytoskeletal deformations. Recent evidence indicates that osteocytes are surrounded by a fiber matrix that may be involved in the mechanotransduction of external stimuli as well as in nutrient exchange. In our previous tracer studies designed to map how different-sized molecules travel through the bone porosities, we found that injected ferritin was confined to blood vessels and did not pass into the mineralized matrix. However, other investigators have shown that ferritin forms halo-shaped labeling that enters the mineralized matrix around blood vessels. This labeling is widely used to explain normal interstitial fluid movement in bone; in particular, it is said to demonstrate bulk centrifugal interstitial fluid movement away from a highly pressurized vascular porosity. In addition, appositional ferritin fronts are said to demonstrate centrifugal interstitial fluid movement from the medullary canal to the periosteal surface. The purpose of this study was to investigate the conflicting ferritin labeling results by evaluating the role of different histological processes in the formation of ferritin "halos." Ferritin was injected into the rat vasculature and allowed to circulate for 5 min. Samples obtained from tibiae were reacted for different times with Perl's reagent and then were either paraffin-embedded or sectioned with a cryostat. Halo-like labeling surrounding vascular pores was found in all groups, ranging from 1.2-3.9% for the samples treated with the shortest histological processes (unembedded, frozen sections) to 5.6-15% for the samples treated with the longest histological processes (paraffin-embedded sections). These results indicate that different histological processing methods are able to create ferritin "halos," with some processing methods allowing more redistribution of the ferritin tracer than others. Based on these results and the fact that "halo" labeling has not been found with any other tracer, as we seek to further delineate the movement of interstitial fluid and the role it plays in bone mechanotransduction, we believe that ferritin "halo" labeling should not be used to demonstrate physiological bone interstitial fluid flow.

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Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin

Cited by 170 publications

References 49 publications

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy

Non-destructive imaging of an individual protein

Mapping bone interstitial fluid movement: Displacement of ferritin tracer during histological processing

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