Formation of amyloid fibrils by bovine carbonic anhydrase

Rana, Anshul; Gupta, Teemish Praveen; Bansal, Sorav; Kundu, Bishwajit

doi:10.1016/j.bbapap.2008.02.020

Cited by 16 publications

(12 citation statements)

References 50 publications

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“…Carbonic anhydrase was the only protein tested whose effects were insignificant in the nematode models. However, its presence in muscle aggregates may reflect formation of amyloid fibrils, as were noted previously for its bovine ortholog [ 41 ]. Similarly, ankyrin-2 may be structurally disposed to aggregate since ankyrin-like domains can target proteins to aggrosomes in human cells [ 42 ].…”

Section: Discussionmentioning

confidence: 76%

Proteins that accumulate with age in human skeletal-muscle aggregates contribute to declines in muscle mass and function in Caenorhabditis elegans

Ayyadevara

Balasubramaniam

Suri

et al. 2016

Aging

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Protein aggregation increases with age in normal tissues, and with pathology and age in Alzheimer's hippocampus and mouse cardiac muscle. We now ask whether human skeletal muscle accumulates aggregates with age. Detergent-insoluble protein aggregates were isolated from vastus lateralis biopsies from 5 young (23–27 years of age) and 5 older (64–80 years) adults. Aggregates, quantified after gel electrophoresis, contain 2.1-fold more protein (P<0.0001) when isolated from older subjects relative to young. Of 515 proteins identified by liquid chromatography coupled to tandem mass spectrometry, 56 (11%) were significantly more abundant in older muscle, while 21 (4%) were depleted with age (each P<0.05). Orthologs to seven of these proteins were then targeted in C. elegans by RNA interference. Six of the seven knockdown treatments decreased protein aggregation (range 6–45%, P<0.01 to <0.0001) and increased muscle mass (range 1.5- to 1.85-fold, P<0.01 to <0.0001) in aged nematodes, and rescued mobility (range 1.4 to 1.65-fold, P≤0.0005 each) in a nematode amyloidopathy model. We conclude that specific aggregate proteins, discovered as differentially abundant in aging human muscle, have orthologs that contribute functionally to aggregation and age-associated muscle loss in nematodes, and thus can be considered potential drug targets for sarcopenia in humans.

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Section: Discussionmentioning

confidence: 76%

Proteins that accumulate with age in human skeletal-muscle aggregates contribute to declines in muscle mass and function in Caenorhabditis elegans

Ayyadevara

Balasubramaniam

Suri

et al. 2016

Aging

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“…Congo red birefringence assay Additional fibril characterization was performed using a Congo red binding assay (21,22). Congo Red can bind soluble proteins and not just insoluble fibrils (23).…”

Section: Resultsmentioning

confidence: 99%

Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels

Zhang

Huang²

2014

Food Sci Biotechnol

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The effects of heat-induced rice bran protein (RBP) fibrils on structure and properties of solutions and gels in a complex system were investigated using transmission electron microscopy (TEM), atomic force microscopy (AFM), Congo red spectral analysis, and circular dichroism (CD). Planar and 3-dimensional images of RBP fibrils all revealed structural details. A Congo red spectral shift indicated fibril formation. Fibril secondary structural components exhibited differences at pH 2.0 and pH 7.0. The β-type was decreased with an increased pH. Rheological results exhibited shear thinning behavior for all solutions. Addition of fibrils to RBP solutions, which made the system complex, resulted in an order of magnitude increase in viscosity and shear stress. Adding fibrils to RBP solutions accelerated the kinetics of gel formation, resulting in an increase in gel strength. Scanning electron microscopy (SEM) images showed gel network structural differences with and without fibrils at different pH values.

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“…In a study on the aggregation of HEWLs, Arnaudov and de Vries 129 found that at pH 2.0 and 57 ° C, both fi brillar and spherical aggregates were formed, but at pH 3 and 4, only spherical aggregates were observed. Rana et al 168 demonstrated that the incubation of bovine carbonic anhydrase II (BCA II) at 37 ° C under mildly denaturing conditions at pH 3.5 formed ordered amyloid aggregates, but amorphous aggregates were formed upon thermal incubation of the protein at 75 ° C for 5 min at pH 6.5.…”

Section: P H and Aggregate Morphologymentioning

confidence: 99%

“…178 Guanidine (Gdn) at 0.5 M suppressed the aggregation of HEWL above pH 5.5 during thermal -assisted refolding (98 ° C for 1 min) with a reduction in T m from 77.5 to 71.9 ° C. 190 In contrast, GdnHCl at concentrations ranging from 1.0 to 2.5 M increased aggregation of GCSF at 1 mg/mL at 37 ° C because of the enrichment of a highly aggregation -prone structure (no substantial loss of secondary structure but increased hydrophobic surface area). 18 An intermediate GdnHCl concentration of 1.5 M was found to be optimal for the generation of ordered amyloid aggregates of BCA II at pH 3.5 at 37 ° C. 168 Similarly, GdnHCl at 1 -3 M can induce aggregation of apo, Cu(I), or Cu(II) rusticyanin (Rc). 254 Often, denaturants have opposite effects on protein aggregation in a narrow concentration range.…”

Section: Denaturant and Reducing Agentsmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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Formation of amyloid fibrils by bovine carbonic anhydrase

Cited by 16 publications

References 50 publications

Proteins that accumulate with age in human skeletal-muscle aggregates contribute to declines in muscle mass and function in Caenorhabditis elegans

Proteins that accumulate with age in human skeletal-muscle aggregates contribute to declines in muscle mass and function in Caenorhabditis elegans

Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels

External Factors Affecting Protein Aggregation

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