Chaperone-like activity of β-casein

Zhang, Xuefeng; Fu, Xinmiao; Zhang, Hui; Liu, Chong; Wei, Jiao; Chang, Zengyi

doi:10.1016/j.biocel.2004.12.004

Cited by 92 publications

(97 citation statements)

References 32 publications

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“…For example, α S -CN is significantly better than β-CN at preventing the heat-induced aggregation of ovotransferrin (Matsudomi et al, 2004) or the reduction-induced aggregation of the insulin B-chain (Morgan et al, 2005). However, β-CN is more effective than α S -CN at inhibiting the heat-induced aggregation of catalase and the reduction-induced aggregation of lysozyme (Zhang et al, 2005). Treweek et al (2011) compared the chaperone ability of the individual α S -CN components, α S1 -and α S2 -CN, to prevent the amorphous or fibrillar aggregation of target proteins.…”

Section: The Chaperone Action Of Caseinsmentioning

confidence: 99%

“…Like sHsp, caseins are promiscuous chaperones: they stabilize a range of unrelated target proteins from amorphous aggregation induced by heat, reduction, and UV-induced stress (Bhattacharyya and Das, 1999;Matsudomi et al, 2004;Morgan et al, 2005;Zhang et al, 2005;Hassanisadi et al, 2008;Koudelka et al, 6133 2009;Treweek et al, 2011). Moreover, α S1 -and β-CN can also prevent the formation of fibrillar structures by target proteins, including α S2 -and κ-CN (Thorn et al, 2005, ovalbumin (Khodarahmi et al, 2008), and amyloid-β peptide (Carrotta et al, 2012).…”

Section: The Chaperone Action Of Caseinsmentioning

confidence: 99%

“…In preventing the heat-induced aggregation of catalase, α S -and β-CN form stable high-molecular-mass complexes with the enzyme (Morgan et al, 2005;Zhang et al, 2005). Like the sHsp, they show no refolding activity (Hassanisadi et al, 2008;Treweek et al, 2011).…”

Section: The Chaperone Action Of Caseinsmentioning

confidence: 99%

See 2 more Smart Citations

Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

Holt

Carver

Ecroyd

et al. 2013

Journal of Dairy Science

393

240

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A typical casein micelle contains thousands of casein molecules, most of which form thermodynamically stable complexes with nanoclusters of amorphous calcium phosphate. Like many other unfolded proteins, caseins have an actual or potential tendency to assemble into toxic amyloid fibrils, particularly at the high concentrations found in milk. Fibrils do not form in milk because an alternative aggregation pathway is followed that results in formation of the casein micelle. As a result of forming micelles, nutritious milk can be secreted and stored without causing either pathological calcification or amyloidosis of the mother's mammary tissue. The ability to sequester nanoclusters of amorphous calcium phosphate in a stable complex is not unique to caseins. It has been demonstrated using a number of noncasein secreted phosphoproteins and may be of general physiological importance in preventing calcification of other biofluids and soft tissues. Thus, competent noncasein phosphoproteins have similar patterns of phosphorylation and the same type of flexible, unfolded conformation as caseins. The ability to suppress amyloid fibril formation by forming an alternative amorphous aggregate is also not unique to caseins and underlies the action of molecular chaperones such as the small heat-shock proteins. The open structure of the protein matrix of casein micelles is fragile and easily perturbed by changes in its environment. Perturbations can cause the polypeptide chains to segregate into regions of greater and lesser density. As a result, the reliable determination of the native structure of casein micelles continues to be extremely challenging. The biological functions of caseins, such as their chaperone activity, are determined by their composition and flexible conformation and by how the casein polypeptide chains interact with each other. These same properties determine how caseins behave in the manufacture of many dairy products and how they can be used as functional ingredients in other foods. aBStraCtA typical casein micelle contains thousands of casein molecules, most of which form thermodynamically stable complexes with nanoclusters of amorphous calcium phosphate. Like many other unfolded proteins, caseins have an actual or potential tendency to assemble into toxic amyloid fibrils, particularly at the high concentrations found in milk. Fibrils do not form in milk because an alternative aggregation pathway is followed that results in formation of the casein micelle. As a result of forming micelles, nutritious milk can be secreted and stored without causing either pathological calcification or amyloidosis of the mother's mammary tissue. The ability to sequester nanoclusters of amorphous calcium phosphate in a stable complex is not unique to caseins. It has been demonstrated using a number of noncasein secreted phosphoproteins and may be of general physiological importance in preventing calcification of other biofluids and soft tissues. Thus, competent noncasein phosphoproteins have similar patterns of phosp...

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Section: The Chaperone Action Of Caseinsmentioning

confidence: 99%

Section: The Chaperone Action Of Caseinsmentioning

confidence: 99%

See 1 more Smart Citation

Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

Holt

Carver

Ecroyd

et al. 2013

Journal of Dairy Science

393

240

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show abstract

“…Some authors (Smits and van Brouwershaven, 1980;Noh et al, 1989) reported that the addition of high concentration of -casein negatively affect the formation of the heat induced whey protein aggregations. Moreover, Zhang et al (2005) investigated that the application of s -casein and /or -casein rather than -casein in heated milk which hinder the aggregation of the denatured whey proteins. Their result demonstrated that the disordered caseins carry out a protective chaperone like to inhibit on the unfolding globular via phosphoserine residues as well as hydrophobic surface without development of the heat induced complexes.…”

Section: Milk Compositionmentioning

confidence: 99%

Role of Whey Protein-Casein Complexes on Yoghurt Texture

Mahomud

Katsuno

Nishizu

2017

RAS

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“…It was then demonstrated in 1999 that individual S-casein possessed molecular chaperone activity [109]. Since then, -and -casein have both been shown to also act as molecular chaperones [18,33,[110][111][112]. The presence of high numbers of phosphate groups in the casein proteins appears to be important for chaperone action against amorphously aggregating target proteins under both reduction and heat stress, with studies showing that removal of these in S-and -casein reduced their ability to prevent the aggregation of target proteins [113,114].…”

Section: S-casein As a Molecular Chaperonementioning

confidence: 99%

Alpha-Casein as a Molecular Chaperone

Treweek¹

2012

Milk Protein

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Chaperone-like activity of β-casein

Cited by 92 publications

References 32 publications

Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

Role of Whey Protein-Casein Complexes on Yoghurt Texture

Alpha-Casein as a Molecular Chaperone

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