scholarly journals Succinylation Is a Gain-of-Function Modification in Human Lens αB-Crystallin

Biochemistry ◽  
2019 ◽  
Vol 58 (9) ◽  
pp. 1260-1274 ◽  
Author(s):  
Sandip K. Nandi ◽  
Stefan Rakete ◽  
Rooban B. Nahomi ◽  
Cole Michel ◽  
Alexandra Dunbar ◽  
...  
Keyword(s):  
Human Lens ◽  
Gain Of Function ◽  
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

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.

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 Glycation-mediated inter-protein cross-linking is promoted by chaperone–client complexes of α-crystallin: Implications for lens aging and presbyopia

2020 ◽  
Vol 295 (17) ◽  
pp. 5701-5716 ◽  
Author(s):  
Sandip K. Nandi ◽  
Rooban B. Nahomi ◽  
Johanna Rankenberg ◽  
Marcus A. Glomb ◽  
Ram H. Nagaraj
Keyword(s):  
Thermal Stress ◽  
Citrate Synthase ◽  
Lens Epithelial Cell ◽  
Human Lens ◽  
Cross Linking ◽  
Human Lens Epithelial Cell ◽  
Human Lenses ◽  
Αb Crystallin ◽  
The Stability ◽  
Protein Cross Linking

Lens proteins become increasingly cross-linked through nondisulfide linkages during aging and cataract formation. One mechanism that has been implicated in this cross-linking is glycation through formation of advanced glycation end products (AGEs). Here, we found an age-associated increase in stiffness in human lenses that was directly correlated with levels of protein–cross-linking AGEs. α-Crystallin in the lens binds to other proteins and prevents their denaturation and aggregation through its chaperone-like activity. Using a FRET-based assay, we examined the stability of the αA-crystallin–γD-crystallin complex for up to 12 days and observed that this complex is stable in PBS and upon incubation with human lens–epithelial cell lysate or lens homogenate. Addition of 2 mm ATP to the lysate or homogenate did not decrease the stability of the complex. We also generated complexes of human αA-crystallin or αB-crystallin with alcohol dehydrogenase or citrate synthase by applying thermal stress. Upon glycation under physiological conditions, the chaperone–client complexes underwent greater extents of cross-linking than did uncomplexed protein mixtures. LC-MS/MS analyses revealed that the levels of cross-linking AGEs were significantly higher in the glycated chaperone–client complexes than in glycated but uncomplexed protein mixtures. Mouse lenses subjected to thermal stress followed by glycation lost resilience more extensively than lenses subjected to thermal stress or glycation alone, and this loss was accompanied by higher protein cross-linking and higher cross-linking AGE levels. These results uncover a protein cross-linking mechanism in the lens and suggest that AGE-mediated cross-linking of α-crystallin–client complexes could contribute to lens aging and presbyopia.

Expression of Neovascular Associated Factors PEDF and αB-crystallin in Human Lens Epithelial Cells

2020 ◽  
Vol 45 (11) ◽  
pp. 1385-1389
Author(s):  
Xinying Hu ◽  
Yuzhi Ding ◽  
Zhirong Wang ◽  
Juan Hu ◽  
Xuelian Liu ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Associated Factors ◽  
Human Lens ◽  
Lens Epithelial Cells ◽  
Human Lens Epithelial Cells ◽  
Αb Crystallin

scholarly journals Conformational and Functional Differences between Recombinant Human Lens αA- and αB-Crystallin

1997 ◽  
Vol 272 (10) ◽  
pp. 6220-6225 ◽  
Author(s):  
Tian-Xiao Sun ◽  
Biplab K. Das ◽  
Jack J.-N. Liang
Keyword(s):  
Human Lens ◽  
Functional Differences ◽  
Αb Crystallin

Simultaneous racemization and isomerization at specific aspartic acid residues in αB-crystallin from the aged human lens

1994 ◽  
Vol 1204 (2) ◽  
pp. 157-163 ◽  
Author(s):  
Norko Fujii ◽  
Yoshihiro Ishibashi ◽  
Kenshi Satoh ◽  
Masahiko Fujino ◽  
Kaoru Harada
Keyword(s):  
Aspartic Acid ◽  
Human Lens ◽  
Αb Crystallin
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