Oligomeric structure of brain abundant proteins GAP-43 and BASP1

Zakharov, V. V.; Mosevitsky, Mark I.

doi:10.1016/j.jsb.2010.01.010

Cited by 33 publications

(55 citation statements)

References 70 publications

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“…It has been proposed recently that the toxic oligomers are, just like fibrils, a general phenomenon that forms relatively independently of protein sequence [36]. The oligomerisation of other proteins such as calcitonin [37], α-Syn [38], Syrian hamster prion protein [39], GAP-43 and BASP1 [40] is consistent with this. The oligomers have since been shown to display significant toxicity-related effects relative both to monomers, fibrils and proto-fibrils [41,42].…”

Section: Protein Misfolding Oligomerisation and Toxicitysupporting

confidence: 55%

Detection of mis-folded protein aggregates from a clinical perspective

et al. 2016

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Neurodegenerative Protein Misfolding Diseases (PMDs), such as Alzheimer's (AD), Parkinson's (PD) and prion diseases, are generally difficult to diagnose before irreversible damage to the central nervous system damage has occurred. Detection of the misfolded proteins that ultimately lead to these conditions offers a means for providing early detection and diagnosis of this class of disease. In this review, we discuss recent developments surrounding protein misfolding diseases with emphasis on the cytotoxic oligomers implicated in their aetiology. We also discuss the relationship of misfolded proteins with biological membranes. Finally, we discuss how far techniques for providing early diagnoses for PMDs have advanced and describe promising clinical approaches. We conclude that antibodies with specificity towards oligomeric species of AD and PD and lectins with specificity for particular glycosylation, show promise. However, it is not clear which approach may yield a reliable clinical test first. Relevance for patients: Individuals suffering from protein misfolding diseases will likely benefit form earlier, less-or even non-invasive diagnosis techniques. The current state and possible future directions for these are subject of this review.

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Section: Protein Misfolding Oligomerisation and Toxicitysupporting

confidence: 55%

Detection of mis-folded protein aggregates from a clinical perspective

et al. 2016

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“…Even single atom images were obtained using the aberration-corrected TEM and STEM [20]. In the biological materials research field, only some researchers reported highresolution image using TEM [21][22][23]. However, the preparation method of biological samples requires special techniques and is time consuming.…”

Section: Introductionmentioning

confidence: 99%

Electron microscopy of Staphylococcus epidermidis fibril and biofilm formation using image-enhancing ionic liquid

et al. 2014

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We established an optimized biofilm observation method using a hydrophilic ionic liquid (IL), 1-butyl-3-methylimidazolium tetrafluoroborate ([BMIM][BF4]). In the present study, a biofilm was formed by Staphylococcus epidermidis. Using field emission (FE) scanning electron microscopy (SEM) and transmission electron microscopy (TEM), the colonization of assemblages formed by microbial cells was observed as a function of the cultivation time. FE-TEM analysis revealed that the fibril comprises three types of protein. In addition, the ultrastructure of each protein monomer was visualized. It was expected that the curly-structured protein plays an important role in extension during fibril formation. Compared to the conventional sample preparation method for electron microscopy, a fine structure was easily obtained by the present method using IL. This observation technique can provide valuable information to characterize the ultrastructure of the fibril and biofilm that has not been revealed till date. Furthermore, these findings of the molecular architecture of the fibril and the colonization behavior of microbial cells during biofilm formation are useful for the development of antibacterial drugs and microbial utilization.

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“…The distortions are immediately suggestive of AOs, polypeptide structures forming pores in membranes. 32,35 Such pores are reported to form from disordered and usually aggregated protein states and show a large range of dimensions, from around 20 nm 35,36 to 70-90 nm 35,37 and 100-250 nm. 32 The latter pore size, very similar to that obtained here for HAMLETinduced distortions (Fig.…”

Section: Membrane Distortions and Formation Of Aos By Hamlet Studied mentioning

confidence: 99%

HAMLET Forms Annular Oligomers When Deposited with Phospholipid Monolayers

Baumann

Gjerde

Ying

et al. 2012

Journal of Molecular Biology

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Recently, the anticancer activity of human α-lactalbumin made lethal to tumor cells (HAMLET) has been linked to its increased membrane affinity in vitro, at neutral pH, and ability to cause leakage relative to the inactive native bovine α-lactalbumin (BLA) protein. In this study, atomic force microscopy resolved membrane distortions and annular oligomers (AOs) produced by HAMLET when deposited at neutral pH on mica together with a negatively charged lipid monolayer. BLA, BAMLET (HAMLET's bovine counterpart) and membrane-binding Peptide C, corresponding to BLA residues 75-100, also form AO-like structures under these conditions but at higher subphase concentrations than HAMLET. The N-terminal Peptide A, which binds to membranes at acidic but not at neutral pH, did not form AOs. This suggests a correlation between the capacity of the proteins/peptides to integrate into the membrane at neutral pH-as observed by liposome content leakage and circular dichroism experiments-and the formation of AOs, albeit at higher concentrations. Formation of AOs, which might be important to HAMLET's tumor toxic action, appears related to the increased tendency of the protein to populate intermediately folded states compared to the native protein, the formation of which is promoted by, but not uniquely dependent on, the oleic acid molecules associated with HAMLET.

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Oligomeric structure of brain abundant proteins GAP-43 and BASP1

Cited by 33 publications

References 70 publications

Detection of mis-folded protein aggregates from a clinical perspective

Detection of mis-folded protein aggregates from a clinical perspective

Electron microscopy of Staphylococcus epidermidis fibril and biofilm formation using image-enhancing ionic liquid

HAMLET Forms Annular Oligomers When Deposited with Phospholipid Monolayers

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