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Article ; Online: Creatine kinase/α-crystallin interaction functions in cataract development.

Hamilton, Paul D / Bozeman, Stephanie L / Andley, Usha P

2020 Volume 22, Page(s) 100748

Abstract: Creatine kinase (CK) is an energy storage enzyme that plays an important role in energy metabolism. CK/phosphocreatine functions as an energy buffer and links ATP production sites with ATP utilization sites. Several key mutations in the αA-crystallin ( ...

Abstract	Creatine kinase (CK) is an energy storage enzyme that plays an important role in energy metabolism. CK/phosphocreatine functions as an energy buffer and links ATP production sites with ATP utilization sites. Several key mutations in the αA-crystallin (
Language	English
Publishing date	2020-02-29
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808 ; 2405-5808
ISSN (online)	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2020.100748
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Article ; Online: In vitro

Hamilton, Paul D / Andley, Usha P

Biochemistry and biophysics reports

2018 Volume 15, Page(s) 7–12

Abstract: The aggregation of crystallins in lenses is associated with cataract formation. We previously reported that mutant crystallins are associated with an increased abundance of histones in knock-in and knockout mouse models. However, very little is known ... ...

Abstract	The aggregation of crystallins in lenses is associated with cataract formation. We previously reported that mutant crystallins are associated with an increased abundance of histones in knock-in and knockout mouse models. However, very little is known about the specific interactions between lens crystallins and histones. Here, we performed
Language	English
Publishing date	2018-06-01
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808 ; 2405-5808
ISSN (online)	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2018.05.005
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Article ; Online: Oxysterol Compounds in Mouse Mutant αA- and αB-Crystallin Lenses Can Improve the Optical Properties of the Lens.

Wang, Kehao / Hoshino, Masato / Uesugi, Kentaro / Yagi, Naoto / Pierscionek, Barbara K / Andley, Usha P

Investigative ophthalmology & visual science

2022 Volume 63, Issue 5, Page(s) 15

Abstract: Purpose: To investigate how cataract-linked mutations affect the gradient refractive index (GRIN) and lens opacification in mouse lenses and whether there is any effect on the optics of the lens from treatment with an oxysterol compound.: Methods: A ... ...

Abstract	Purpose: To investigate how cataract-linked mutations affect the gradient refractive index (GRIN) and lens opacification in mouse lenses and whether there is any effect on the optics of the lens from treatment with an oxysterol compound. Methods: A total of 35 mice including wild-type and knock-in mutants (Cryaa-R49C and Cryab-R120G) were used in these experiments: 26 mice were treated with topical VP1-001, an oxysterol, in one eye and vehicle in the other, and nine mice were untreated controls. Slit lamp biomicroscopy was used to analyze the lens in live animals and to provide apparent cataract grades. Refractive index in the lenses of 64 unfixed whole mouse eyes was calculated from measurements with X-ray phase tomography based on X-ray Talbot interferometry with a synchrotron radiation source. Results: Heterozygous Cryaa-R49C lenses had slightly irregularly shaped contours in the center of the GRIN and distinct disturbances of the gradient index at the anterior and posterior poles. Contours near the lens surface were denser in homozygous Cryab-R120G lenses. Treatment with topical VP1-001, an oxysterol, showed an improvement in refractive index profiles in 61% of lenses and this was supported by a reduction in apparent lens opacity grade by 1.0 in 46% of live mice. Conclusions: These results indicate that α-crystallin mutations alter the refractive index gradient of mouse lenses in distinct ways and suggest that topical treatment with VP1-001 may improve lens transparency and refractive index contours in some lenses with mutations.
MeSH term(s)	Animals ; Cataract/genetics ; Crystallins/genetics ; Disease Models, Animal ; Lens, Crystalline/metabolism ; Lens, Crystalline/physiology ; Mice ; Oxysterols/pharmacology
Chemical Substances	Crystallins ; Oxysterols
Language	English
Publishing date	2022-05-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	391794-0
ISSN	1552-5783 ; 0146-0404
ISSN (online)	1552-5783
ISSN	0146-0404
DOI	10.1167/iovs.63.5.15
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Article ; Online: Alpha-crystallin mutations alter lens metabolites in mouse models of human cataracts.

Frankfater, Cheryl / Bozeman, Stephanie L / Hsu, Fong-Fu / Andley, Usha P

PloS one

2020 Volume 15, Issue 8, Page(s) e0238081

Abstract: Cataracts are a major cause of blindness worldwide and commonly occur in individuals over 70 years old. Cataracts can also appear earlier in life due to genetic mutations. The lens proteins, αA- and αB-crystallins, are chaperone proteins that have ... ...

Abstract	Cataracts are a major cause of blindness worldwide and commonly occur in individuals over 70 years old. Cataracts can also appear earlier in life due to genetic mutations. The lens proteins, αA- and αB-crystallins, are chaperone proteins that have important roles maintaining protein solubility to prevent cataract formation. Mutations in the CRYAA and CRYAB crystallin genes are associated with autosomal dominant early onset human cataracts. Although studies about the proteomic and genomic changes that occur in cataracts have been reported, metabolomics studies are very limited. Here, we directly investigated cataract metabolism using gas-chromatography-mass spectrometry (GC-MS) to analyze the metabolites in adult Cryaa-R49C and Cryab-R120G knock-in mouse lenses. The most abundant metabolites were myo-inositol, L-(+)-lactic acid, cholesterol, phosphate, glycerol phosphate, palmitic and 9-octadecenoic acids, α-D-mannopyranose, and β-D-glucopyranose. Cryaa-R49C knock-in mouse lenses had a significant decrease in the number of sugars and minor sterols, which occurred in concert with an increase in lactic acid. Cholesterol composition was unchanged. In contrast, Cryab-R120G knock-in lenses exhibited increased total amino acid content including valine, alanine, serine, leucine, isoleucine, glycine, and aspartic acid. Minor sterols, including cholest-7-en-3-ol and glycerol phosphate were decreased. These studies indicate that lenses from Cryaa-R49C and Cryab-R120G knock-in mice, which are models for human cataracts, have unique amino acid and metabolite profiles.
MeSH term(s)	Animals ; Cataract/genetics ; Cataract/metabolism ; Disease Models, Animal ; Humans ; Lens, Crystalline/metabolism ; Metabolomics ; Mice ; Mice, Inbred C57BL ; Mutation ; alpha-Crystallins/genetics
Chemical Substances	alpha-Crystallins
Language	English
Publishing date	2020-08-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0238081
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Article ; Online: Changes in relative histone abundance and heterochromatin in αA-crystallin and αB-crystallin knock-in mutant mouse lenses.

Andley, Usha P / Naumann, Brittney N / Hamilton, Paul D / Bozeman, Stephanie L

BMC research notes

2020 Volume 13, Issue 1, Page(s) 315

Abstract: Objective: Understanding the mechanisms of cataract formation is important for age-related and hereditary cataracts caused by mutations in lens protein genes. Lens proteins of the crystallin gene families α-, β-, and γ-crystallin are the most abundant ... ...

Abstract	Objective: Understanding the mechanisms of cataract formation is important for age-related and hereditary cataracts caused by mutations in lens protein genes. Lens proteins of the crystallin gene families α-, β-, and γ-crystallin are the most abundant proteins in the lens. Single point mutations in crystallin genes cause autosomal dominant cataracts in multigenerational families. Our previous proteomic and RNAseq studies identified genes and proteins altered in the early stages of cataract formation in mouse models. Histones H2A, H2B, and H4 increase in abundance in αA- and αB-crystallin mutant mouse lenses and in cultured cells expressing the mutant form of αA-crystallin linked with hereditary cataracts. Results: In this study of histones in mutant lenses, we extracted histones from adult mouse lenses from cryaa-R49C and cryab-R120G mutant knock-in mice. We characterized the histones using matrix-assisted laser desorption/ionization time of flight (MALDI-TOF)-mass spectrometric analysis and gel electrophoresis and characterized the lens nucleus morphology using electron microscopy (EM). The relative abundance of histone H3 protein decreased in lenses from cryaa-R49C mutant mice and the relative abundance of histone H2 increased in these lenses. Electron microscopy of nuclei from cryaa-R49C-homozygous mutant mouse lenses revealed a pronounced alteration in the distribution of heterochromatin.
MeSH term(s)	Animals ; Cataract/genetics ; Cataract/metabolism ; Gene Knock-In Techniques ; Heterochromatin/ultrastructure ; Histones/metabolism ; Lens, Crystalline/metabolism ; Lens, Crystalline/ultrastructure ; Mice ; Mutation ; alpha-Crystallin A Chain/genetics ; alpha-Crystallin B Chain/genetics
Chemical Substances	Heterochromatin ; Histones ; alpha-Crystallin A Chain ; alpha-Crystallin B Chain
Language	English
Publishing date	2020-07-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2413336-X
ISSN	1756-0500 ; 1756-0500
ISSN (online)	1756-0500
ISSN	1756-0500
DOI	10.1186/s13104-020-05154-7
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Article: Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataracts.

Andley, Usha P / Goldman, Joshua W

Biochimica et biophysica acta

2016 Volume 1860, Issue 1 Pt B, Page(s) 234–239

Abstract: Background: Knock-in mice provide useful models of congenital and age-related cataracts caused by α-crystallin mutations. R49C αA-crystallin and R120G αB-crystallin mutations are linked with hereditary cataracts. Knock-in αA-R49C+/- heterozygotes ... ...

Abstract	Background: Knock-in mice provide useful models of congenital and age-related cataracts caused by α-crystallin mutations. R49C αA-crystallin and R120G αB-crystallin mutations are linked with hereditary cataracts. Knock-in αA-R49C+/- heterozygotes develop cataracts by 1-2months, whereas homozygote mice have cataracts at birth. The R49C mutation drastically reduces lens protein water solubility and causes cell death in knock-in mouse lenses. Mutant crystallin cannot function as a chaperone, which leads to protein aggregation and lens opacity. Protein aggregation disrupts the lens fiber cell structure and normal development and causes cell death in epithelial and fiber cells. We determined what aspects of the wild-type phenotype are age-dependently altered in the mutant lens. Methods: Wild-type, heterozygote (αA-R49C+/-), and homozygote (αA-R49C+/+) mouse lenses were assessed pre- and postnatally for lens morphology (electron microscopy, immunohistochemistry), and autophagy or unfolded protein response markers (immunoblotting). Results: Morphology was altered by embryonic day 17 in R49C+/+ lenses; R49C+/- lens morphology was unaffected at this stage. Active autophagy in the lens epithelium of mutant lenses was indicated by the presence of autophagosomes using electron microscopy. Protein p62 levels, which are degraded specifically by autophagy, increased in αA-R49C mutant versus wild-type lenses, suggesting autophagy inhibition in the mutant lenses. The unfolded protein response marker XBP-1 was upregulated in adult lenses of αB-R120G+/+ mice, suggesting its role in lens opacification. Conclusions: Mutated crystallins alter lens morphology, autophagy, and stress responses. General significance: Therapeutic modulation of autophagic pathways may improve protein degradation in cataractous lenses and reduce lens opacity. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.
MeSH term(s)	Aging/genetics ; Animals ; Autophagy/genetics ; Cataract/genetics ; Cataract/pathology ; Crystallins/genetics ; Disease Models, Animal ; Gene Knock-In Techniques ; Lens, Crystalline/metabolism ; Lens, Crystalline/pathology ; Mice ; Mutation ; Unfolded Protein Response/genetics
Chemical Substances	CRYAA protein, human ; Crystallins
Language	English
Publishing date	2016-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2015.06.001
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Article ; Online: Creatine kinase/α-crystallin interaction functions in cataract development

Paul D. Hamilton / Stephanie L. Bozeman / Usha P. Andley

Biochemistry and Biophysics Reports, Vol 22, Iss , Pp - (2020)

2020

Abstract	Creatine kinase (CK) is an energy storage enzyme that plays an important role in energy metabolism. CK/phosphocreatine functions as an energy buffer and links ATP production sites with ATP utilization sites. Several key mutations in the αA-crystallin (cryaa) and αB-crystallin (cryab) genes have been linked with autosomal-dominant, hereditary human cataracts. The cryaa-R49C mutation was identified in a four-generation Caucasian family. We previously identified an increase in the quantity of CK complexed with α-crystallin in the lenses of knock-in mice expressing the cryaa-R49C mutation using proteomic analyses. Increased levels of CK in postnatal cataractous lenses may indicate increased ATP requirements during early cataract development. To gain a further understanding of the relationship between CK and α-crystallin, we investigated whether α-crystallin interacts with and forms complexes with CK, in vitro. Isothermal titration calorimetry (ITC) showed that each CK dimer bound to 28 α-crystallin subunits, with a Kd of 3.3 × 10−7 M, and that the interaction between α-crystallin and CK was endothermic, thermodynamically favorable, and entropy-driven. High-salt concentrations did not affect the interaction between CK and α-crystallin, suggesting that the interaction between CK and α-crystallin is primarily hydrophobic. Gel permeation chromatography (GPC) detected water-soluble α-crystallin and CK complexes, as determined by increased light scattering after complex formation. In addition, CK and α-crystallin formed partially-water-insoluble, high-molecular-mass complexes. Enzyme-linked immunosorbent assay (ELISA)-based enzymatic activity analyses of lens homogenates showed a 17-fold increase in CK activity in the postnatal lenses of cryaa-R49C knock-in mice. These studies indicate that the interaction between α-crystallin and CK is functionally important and that increased CK levels may be necessary to meet the increased ATP demands of ATP-dependent functions in cataractous lenses. Keywords: Creatine kinase, α-Crystallin, Cataract, Complex formation, Mouse model
Keywords	Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Subject code	570
Language	English
Publishing date	2020-07-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Effects of alpha-crystallin on lens cell function and cataract pathology.

Andley, Usha P

Current molecular medicine

2009 Volume 9, Issue 7, Page(s) 887–892

Abstract: The development of cataracts is a debilitating eye condition which is common in elderly patients and afflicts millions worldwide. Cataracts result from the deposition of aggregated proteins in the eye which causes clouding of the lens, light scattering, ... ...

Abstract	The development of cataracts is a debilitating eye condition which is common in elderly patients and afflicts millions worldwide. Cataracts result from the deposition of aggregated proteins in the eye which causes clouding of the lens, light scattering, and obstruction of vision. Non-syndromic, hereditary human cataract development is linked to point mutations in the CRYAA and CRYAB genes which encode alphaA and alphaB-crystallin. The alpha-crystallins are small heat shock proteins which play central roles in maintaining lens transparency and refractive properties. The discovery in 1992 that these proteins possess chaperone-like activity has led most researchers to focus on the ability of alpha-crystallins to prevent protein aggregation in vitro. While the ability of alpha-crystallins to efficiently trap aggregation-prone denatured proteins in vitro is thought to delay the development of age-related cataracts in vivo, alpha-crystallins have additional functions which may also contribute to cataract pathology. In addition to chaperone activity, alpha-crystallins are known to protect cells from stress-induced apoptosis, regulate cell growth, and enhance genomic stability. They also physically and functionally interact with both the cell membrane and cytoskeleton. Functional changes in alpha-crystallin have been shown to modify membrane and cell-cell interactions and lead to lens cell pathology in vivo. This article focuses on the multiple diverse roles of alphaA-crystallin in the maintenance of lens function and cataract development in vivo.
MeSH term(s)	Animals ; Cataract/genetics ; Cataract/metabolism ; Cataract/pathology ; Cell Survival ; Genomic Instability ; Humans ; Lens, Crystalline/cytology ; Lens, Crystalline/metabolism ; Lens, Crystalline/pathology ; Point Mutation ; Protein Conformation ; Protein Processing, Post-Translational ; alpha-Crystallin A Chain/chemistry ; alpha-Crystallin A Chain/genetics ; alpha-Crystallin A Chain/metabolism ; alpha-Crystallin B Chain/chemistry ; alpha-Crystallin B Chain/genetics ; alpha-Crystallin B Chain/metabolism
Chemical Substances	alpha-Crystallin A Chain ; alpha-Crystallin B Chain
Language	English
Publishing date	2009-09-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2064873-X
ISSN	1875-5666 ; 1566-5240
ISSN (online)	1875-5666
ISSN	1566-5240
DOI	10.2174/156652409789105598
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Article ; Online: AlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice.

Andley, Usha P

BMC ophthalmology

2009 Volume 9, Page(s) 4

Abstract: Background: AlphaA-crystallin (CRYAA/HSPB4), a major component of all vertebrate eye lenses, is a small heat shock protein responsible for maintaining lens transparency. The R49C mutation in the alphaA-crystallin protein is linked with non-syndromic, ... ...

Abstract	Background: AlphaA-crystallin (CRYAA/HSPB4), a major component of all vertebrate eye lenses, is a small heat shock protein responsible for maintaining lens transparency. The R49C mutation in the alphaA-crystallin protein is linked with non-syndromic, hereditary human cataracts in a four-generation Caucasian family. Methods: This study describes a mouse cataract model generated by insertion of a neomycin-resistant (neor) gene into an intron of the gene encoding mutant R49C alphaA-crystallin. Mice carrying the neor gene and wild-type Cryaa were also generated as controls. Heterozygous knock-in mice containing one wild type gene and one mutated gene for alphaA-crystallin (WT/R49Cneo) and homozygous knock-in mice containing two mutated genes (R49Cneo/R49Cneo) were compared. Results: By 3 weeks, WT/R49Cneo mice exhibited large vacuoles in the cortical region 100 mum from the lens surface, and by 3 months posterior and nuclear cataracts had developed. WT/R49Cneo mice demonstrated severe posterior cataracts at 9 months of age, with considerable posterior nuclear migration evident in histological sections. R49Cneo/R49Cneo mice demonstrated nearly complete lens opacities by 5 months of age. In contrast, R49C mice in which the neor gene was deleted by breeding with CreEIIa mice developed lens abnormalities at birth, suggesting that the neor gene may suppress expression of mutant R49C alphaA-crystallin protein. Conclusion: It is apparent that modification of membrane and cell-cell interactions occurs in the presence of the alphaA-crystallin mutation and rapidly leads to lens cell pathology in vivo.
MeSH term(s)	Amino Acid Substitution ; Animals ; Cataract/genetics ; Cataract/metabolism ; Cataract/pathology ; Cell Membrane/pathology ; Cell Membrane/ultrastructure ; Epithelial Cells/metabolism ; Epithelial Cells/pathology ; Epithelial Cells/ultrastructure ; Gene Dosage ; Gene Knock-In Techniques ; Lens Capsule, Crystalline/metabolism ; Lens Capsule, Crystalline/pathology ; Lens Capsule, Crystalline/ultrastructure ; Lens Cortex, Crystalline/metabolism ; Lens Cortex, Crystalline/pathology ; Lens Cortex, Crystalline/ultrastructure ; Lens Nucleus, Crystalline/metabolism ; Lens Nucleus, Crystalline/pathology ; Lens Nucleus, Crystalline/ultrastructure ; Mice ; Models, Animal ; Mutation ; alpha-Crystallin A Chain/genetics ; alpha-Crystallin A Chain/metabolism
Chemical Substances	alpha-Crystallin A Chain
Language	English
Publishing date	2009-07-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2050436-6
ISSN	1471-2415 ; 1471-2415
ISSN (online)	1471-2415
ISSN	1471-2415
DOI	10.1186/1471-2415-9-4
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Article ; Online: In vitro interactions of histones and α-crystallin

Paul D. Hamilton / Usha P. Andley

Biochemistry and Biophysics Reports, Vol 15, Iss , Pp 7-

2018 Volume 12

Abstract	The aggregation of crystallins in lenses is associated with cataract formation. We previously reported that mutant crystallins are associated with an increased abundance of histones in knock-in and knockout mouse models. However, very little is known about the specific interactions between lens crystallins and histones. Here, we performed in vitro analyses to determine whether α-crystallin interacts with histones directly. Isothermal titration calorimetry revealed a strong histone–α-crystallin binding with a Kd of 4 × 10−7 M, and the thermodynamic parameters suggested that the interaction was both entropy and enthalpy driven. Size-exclusion chromatography further showed that histone–α-crystallin complexes are water soluble but become water insoluble as the concentration of histones is increased. Right-angle light scattering measurements of the water-soluble fractions of histone–α-crystallin mixtures showed a decrease in the oligomeric molecular weight of α-crystallin, indicating that histones alter the oligomerization of α-crystallin. Taken together, these findings reveal for the first time that histones interact with and affect the solubility and aggregation of α-crystallin, indicating that the interaction between α-crystallin and histones in the lens is functionally important. Keywords: Histone, Complex formation, Cataract, Crystallin
Keywords	Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Language	English
Publishing date	2018-09-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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