In Vivo Modification of the C-Terminal Lysine of Human Lens αB-Crystallin

1997 ◽  
Vol 65 (5) ◽  
pp. 673-680 ◽  
Author(s):  
PEIPING LIN ◽  
DAVID L SMITH ◽  
JEAN B SMITH
Keyword(s):  
Human Lens ◽  
Αb Crystallin

scholarly journals In vivo carbamylation and acetylation of water-soluble human lens αB-crystallin lysine 92

2001 ◽  
Vol 10 (6) ◽  
pp. 1130-1136 ◽  
Author(s):  
Veniamin N. Lapko ◽  
David L. Smith ◽  
Jean B. Smith
Keyword(s):  
Water Soluble ◽  
Human Lens ◽  
Αb Crystallin

Assigning in vivo carbamylation and acetylation in human lens proteins using tandem mass spectrometry and database searching

2007 ◽  
Vol 259 (1-3) ◽  
pp. 161-173 ◽  
Author(s):  
Zee-Yong Park ◽  
Rovshan Sadygov ◽  
Judy M. Clark ◽  
John I. Clark ◽  
John R. Yates
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Human Lens ◽  
Database Searching ◽  
Tandem Mass ◽  
Lens Proteins

In Vivo Measurements On Human Lens Using Quasielastic Light Scattering

1987 ◽  
Author(s):  
Peter C. Magnante ◽  
Leo T. Chylack ◽  
George B. Benedek ◽  
Teodosio Libondi ◽  
Stephen N. Joffe ◽  
...  
Keyword(s):  
Light Scattering ◽  
Human Lens ◽  
Quasielastic Light Scattering ◽  
In Vivo Measurements

scholarly journals The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27

2021 ◽  
Vol 22 (7) ◽  
pp. 3700
Author(s):  
Junna Hayashi ◽  
Jennifer Ton ◽  
Sparsh Negi ◽  
Daniel E. K. M. Stephens ◽  
Dean L. Pountney ◽  
...  
Keyword(s):  
Heat Shock ◽  
Protein Aggregation ◽  
Molecular Chaperone ◽  
Cross Linking ◽  
Αb Crystallin ◽  
The Cross ◽  
Shock Proteins ◽  
And Function

Oxidation of the neurotransmitter, dopamine (DA), is a pathological hallmark of Parkinson’s disease (PD). Oxidized DA forms adducts with proteins which can alter their functionality. αB-crystallin and Hsp27 are intracellular, small heat-shock molecular chaperone proteins (sHsps) which form the first line of defense to prevent protein aggregation under conditions of cellular stress. In vitro, the effects of oxidized DA on the structure and function of αB-crystallin and Hsp27 were investigated. Oxidized DA promoted the cross-linking of αB-crystallin and Hsp27 to form well-defined dimer, trimer, tetramer, etc., species, as monitored by SDS-PAGE. Lysine residues were involved in the cross-links. The secondary structure of the sHsps was not altered significantly upon cross-linking with oxidized DA but their oligomeric size was increased. When modified with a molar equivalent of DA, sHsp chaperone functionality was largely retained in preventing both amorphous and amyloid fibrillar aggregation, including fibril formation of mutant (A53T) α-synuclein, a protein whose aggregation is associated with autosomal PD. In the main, higher levels of sHsp modification with DA led to a reduction in chaperone effectiveness. In vivo, DA is sequestered into acidic vesicles to prevent its oxidation and, intracellularly, oxidation is minimized by mM levels of the antioxidant, glutathione. In vitro, acidic pH and glutathione prevented the formation of oxidized DA-induced cross-linking of the sHsps. Oxidized DA-modified αB-crystallin and Hsp27 were not cytotoxic. In a cellular context, retention of significant chaperone functionality by mildly oxidized DA-modified sHsps would contribute to proteostasis by preventing protein aggregation (particularly of α-synuclein) that is associated with PD.

Association of αB-Crystallin, a Small Heat Shock Protein, with Actin: Role in Modulating Actin Filament Dynamics in Vivo

2007 ◽  
Vol 366 (3) ◽  
pp. 756-767 ◽  
Author(s):  
Bhairab N. Singh ◽  
K. Sridhar Rao ◽  
Tangirala Ramakrishna ◽  
Nandini Rangaraj ◽  
Ch. Mohan Rao
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Actin Filament ◽  
Small Heat Shock Protein ◽  
Filament Dynamics ◽  
Αb Crystallin

Surface plasmon resonance study of the interaction of 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) and adenosine triphosphate (ATP) with oligomeric recombinant human lens αA-crystallin

2019 ◽  
Vol 97 (6) ◽  
pp. 504-511
Author(s):  
Srabani Karmakar ◽  
Shrutidhara Biswas ◽  
Kali P. Das ◽  
Umakanta Tripathy
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Age Related Macular Degeneration ◽  
Disulfonic Acid ◽  
Human Lens ◽  
Lens Protein ◽  
Retinal Diseases ◽  
Dipotassium Salt ◽  
Αb Crystallin

α-Crystallin, an abundant mammalian lens protein made up of two subunits (αA- and αB-crystallin), is involved in the maintenance of the optimal refractive index in the lens. The protein is implicated in the pathophysiology of a large number of retinal diseases including cataract, age-related macular degeneration, diabetic retinopathy, and uveitis. α-Crystallin belongs to the small heat shock protein (sHSP) family, forms large oligomeric structures, and functions as a molecular chaperone appearing very early during embryonic development. To gain mechanistic insight into the structural and functional role of α-crystallin and its alterations in various retinal diseases, it is important to study the interaction chemistry with its known partners. The hydrophobic sites in α-crystallin have been studied extensively using environmentally sensitive fluorescent probes such as 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) that interacts with both subunits of α-cystallin in 1:1 stoichiometry at 37 °C and diminishes the chaperone-like activity of the protein. Furthermore, it has been shown that ATP plays a crucial role in the association of α-crystallin with substrate proteins. We use surface plasmon resonance (SPR) to monitor the interactions of immobilized oligomeric recombinant αA subunit of human α-crystallin protein with bis-ANS and ATP. We assess the thermodynamic parameters and kinetics of such interactions at various temperatures. Our results indicate that bis-ANS binds to αA-crystallin with higher affinity when compared with ATP, although both αA-crystallin and αB-crystallin display fast interaction kinetics.

scholarly journals In Vivo Quasi-Elastic Light Scattering Eye Scanner Detects Molecular Aging in Humans

2020 ◽  
Vol 75 (9) ◽  
pp. e53-e62
Author(s):  
Olga Minaeva ◽  
Srikant Sarangi ◽  
Danielle M Ledoux ◽  
Juliet A Moncaster ◽  
Douglas S Parsons ◽  
...  
Keyword(s):  
Light Scattering ◽  
Human Lens ◽  
Fetal Life ◽  
Healthy Human ◽  
Elastic Light Scattering ◽  
Lens Proteins ◽  
Age Dependent ◽  
Molecular Aging

Abstract The absence of clinical tools to evaluate individual variation in the pace of aging represents a major impediment to understanding aging and maximizing health throughout life. The human lens is an ideal tissue for quantitative assessment of molecular aging in vivo. Long-lived proteins in lens fiber cells are expressed during fetal life, do not undergo turnover, accumulate molecular alterations throughout life, and are optically accessible in vivo. We used quasi-elastic light scattering (QLS) to measure age-dependent signals in lenses of healthy human subjects. Age-dependent QLS signal changes detected in vivo recapitulated time-dependent changes in hydrodynamic radius, protein polydispersity, and supramolecular order of human lens proteins during long-term incubation (~1 year) and in response to sustained oxidation (~2.5 months) in vitro. Our findings demonstrate that QLS analysis of human lens proteins provides a practical technique for noninvasive assessment of molecular aging in vivo.

scholarly journals In vivo acetylation identified at lysine 70 of human lens αA-crystallin

1998 ◽  
Vol 7 (6) ◽  
pp. 1451-1457 ◽  
Author(s):  
Peiping P. Lin ◽  
Richard C. Barry ◽  
David L. Smith ◽  
Jean B. Smith
Keyword(s):  
Human Lens
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