Article
Biochemistry & Molecular Biology
Abu-Hussien, Guru Krishnakumar Viswanathan, Luba Simhaev, Ashim Paul, Hamutal Engel, Ehud Gazit, Daniel Segal
Summary: The specific residues of the human gamma D-crystallin protein were found to play an important role in the amyloidogenicity of GDC6, facilitating peptide-peptide interactions. By validating the amyloidogenic propensity of peptide variants, it was revealed that these specific residues are crucial for the amyloidogenicity of GDC6.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Biology
Eugene Serebryany, Sourav Chowdhury, Christopher N. Woods, David C. Thorn, Nicki E. Watson, Arthur A. McClelland, Rachel E. Klevit, Eugene Shakhnovich
Summary: Cataract, a protein aggregation disorder, is a common cause of vision loss worldwide. Researchers have discovered that myo-inositol, an abundant lens metabolite, can suppress the aggregation of lens crystallins, suggesting it as a potential strategy to prevent or delay age-onset cataracts.
Article
Cell Biology
Yuan Xiao, Jia-Wen Xiang, Qian Gao, Yue-Yue Bai, Zhao-Xia Huang, Xiao-Hui Hu, Ling Wang, David Wan-Cheng Li
Summary: Research has shown that Mab21L1 promotes survival of lens epithelial cells by regulating the expression of αB-crystallin and suppressing the ATR/CHK1/p53 pathway. This finding contributes to a better understanding of the functional mechanism of Mab21L1.
Article
Biochemistry & Molecular Biology
Susanne Weininger, Malte Neudorf, Stefan Groeger, Eric Plato, Robert Broneske, Kay Saalwaechter, Ulrich Weininger, Jochen Balbach
Summary: Crystallin proteins in the human eye lenses play a role in maintaining transparency, light refraction, and UV light protection. Imbalance in the interaction between alpha-, beta-, and gamma-crystallin can lead to cataracts. The research looks into the effects of UV-B radiation on gamma D-crystallin, specifically observing changes in the N-terminal domain. It is found that some photoprotective properties remain in extracts from cataract patients. Additionally, a genetic mutation in the eye lens core of infants with cataracts increases sensitivity to UV-B irradiation.
MACROMOLECULAR BIOSCIENCE
(2023)
Article
Multidisciplinary Sciences
Roy Joseph, Michael L. L. Robinson, Laura Lambert, Om P. P. Srivastava
Summary: The beta A3/A1-crystallin protein is important in maintaining lens transparency and the loss of its function leads to congenital cataract in mice. The activation of calpain 3 results in degradation of beta-tubulin and other lens proteins, causing protein accumulation and disruption of cellular microtubular structure, which contributes to the development of cataract in beta A3/A1cKO mice.
Article
Ophthalmology
Guowei Zhang, Min Zhang, Jianfeng Yu, Lihua Kang, Huaijin Guan
Summary: The study demonstrated that Rg1 could effectively prevent lens opacification induced by H2O2, increase antioxidant levels, reduce oxidative damage, and enhance cell viability. Additionally, Rg1 was found to protect the lens against cataracts by locally administering, suggesting its potential therapeutic application in preventing oxidative stress-induced cataracts.
CURRENT EYE RESEARCH
(2021)
Article
Cell Biology
Xiang-Jia Zhu, Ke-Ke Zhang, Wen-Wen He, Jiao Qi, Yi Lu
Summary: Compared to age-related cataracts, diabetic cataracts exhibit a distinct pattern of protein racemization, which may influence the progression of the disease over time.
Article
Biochemistry & Molecular Biology
Amber D. Rolland, Takumi Takata, Micah T. Donor, Kirsten J. Lampi, James S. Prell
Summary: This study investigates the interactions and oligomerization kinetics of β-crystallin in the lens using native ion mobility-mass spectrometry, revealing compact ring-like topologies of the observed oligomers.
Article
Chemistry, Analytical
Jia Kong, Jinyao Hu, Jia Li, Jiaxing Zhang, Yuhe Shen, Tianli Yue, Xihui Shen, Yuefei Wang, Zhonghong Li, Yinqiang Xia
Summary: Reconstructing miniaturized peptides to mimic specific protein functions is appealing but challenging. In this study, we propose a practical approach to construct a mimetic peptide of redox-sensitive green fluorescent protein-2 (roGFP2) by rethreading aromatic residues adjacent to the chromophore fragment. By fine-tuning the residues, we designed a mini tetrapeptide (Cys-Phe-Phe-His) that acts as a hydrogen peroxide sensor using ratiometric fluorescence. The roGFP2 mimetic tetrapeptide, with its assembly-induced emissions, is biocompatible, photostable, and exhibits competitive fluorescent properties compared to roGFP2. We demonstrated the ability of the ratiometric tetrapeptide to sense hydrogen peroxide in acidic chambers, providing a promising approach for artificially designing miniaturized peptides with desired functions.
ANALYTICAL CHEMISTRY
(2023)
Article
Biochemistry & Molecular Biology
Malak Abu-Hussien, Guru Krishnakumar Viswanathan, Lia Borisover, Michael Mimouni, Hamutal Engel, Shiri Zayit-Soudry, Ehud Gazit, Daniel Segal
Summary: Gamma D-crystallin is essential in maintaining the transparency of the human eye lens, with its aggregation leading to cataract formation. The study found that cochineal Carmine could effectively reduce aggregation of gamma D-crystallin, showing potential for developing new therapeutics for cataract treatment.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemistry & Molecular Biology
Ajamaluddin Malik, Hajar Ahmed Almaharfi, Javed Masood Khan, Malik Hisamuddin, Salman Freeh Alamery, Samina Hyder Haq, Mohammad Z. Ahmed
Summary: Camel lens proteins show resistance to cataractogenesis in harsh conditions, with α-crystallin playing a key role in preventing aggregation of ζ-crystallin at high temperatures, exhibiting significant chaperone activity.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Biochemical Research Methods
Yulei Chen, Shuling Ye, Qingying Wang, Meixiao Shen, Fan Lu, Jia Qu, Dexi Zhu
Summary: Lens biomechanics has great potential for clinical applications in presbyopia and cataracts. A noncontact optical coherence elastography (OCE) method is proposed for quantitative imaging of lens elasticity. The method was validated and demonstrated consistent results with in vitro measurements. The study also investigated the effects of cold storage and microwave heating on lens elasticity.
BIOMEDICAL OPTICS EXPRESS
(2022)
Article
Biochemistry & Molecular Biology
Jian Liu, Wanyue Xu, Kaijie Wang, Fanrui Chen, Ling Ren, Jingjie Xu, Ke Yao, Xiangjun Chen
Summary: Congenital cataract, caused by abnormal aggregation of crystallin, is a common disease that leads to blindness in newborns worldwide. The L116P mutation in β B1-CRY affects the protein's structural stability, susceptibility to amyloid fibrils aggregation, and protease degradation, potentially contributing to cataract development and associated symptoms.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Ophthalmology
Frank J. Giblin, David M. G. Anderson, Jun Han, Kristie L. Rose, Zhen Wang, Kevin L. Schey
Summary: Research has shown that hyperbaric oxygen treatment accelerates the aging process of the lens in guinea pigs, leading to the development of nuclear cataracts. This treatment results in truncation of proteins such as aquaporin-0 and alpha A-crystallin, mirroring observations in age-related cataracts in humans.
EXPERIMENTAL EYE RESEARCH
(2021)
Article
Biochemistry & Molecular Biology
Maho Yagi-Utsumi, Tomohiro Tanaka, Yoko Otsubo, Akira Yamashita, Shinji Yoshimura, Motohiro Nishida, Koichi Kato
Summary: The study reveals that cold atmospheric plasma can affect the amyloidogenic protein Aβ associated with Alzheimer's disease by selectively oxidizing certain amino acid residues, inhibiting its fibril formation. This provides insights into potential novel applications of CAP.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Biochemistry & Molecular Biology
Murugesan Raju, Puttur Santhoshkumar, K. Krishna Sharma
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
(2016)
Article
Biochemistry & Molecular Biology
Puttur Santhoshkumar, Srabani Karmakar, Krishna K. Sharma
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
(2016)
Article
Ophthalmology
Ashutosh S. Phadte, Puttur Santhoshkumar, K. Krishna Sharma
EXPERIMENTAL EYE RESEARCH
(2018)
Article
Biochemistry & Molecular Biology
Murugesan Raju, Puttur Santhoshkumar, Leike Xie, K. Krishna Sharma
Correction
Biochemistry & Molecular Biology
Murugesan Raju, Puttur Santhoshkumar, Leike Xie, K. Krishna Sharma
Article
Biochemistry & Molecular Biology
Puttur Santhoshkumar, Leike Xie, Murugesan Raju, Lixing Reneker, K. Krishna Sharma
JOURNAL OF BIOLOGICAL CHEMISTRY
(2014)
Article
Multidisciplinary Sciences
Damian M. Daszynski, Puttur Santhoshkumar, Ashutosh S. Phadte, K. Krishna Sharma, Haizhen A. Zhong, Marjorie F. Lou, Peter F. Kador
SCIENTIFIC REPORTS
(2019)
Article
Biochemistry & Molecular Biology
Ashutosh S. Phadte, Sundararajan Mahalingam, Puttur Santhoshkumar, Krishna K. Sharma
Article
Biochemistry & Molecular Biology
Sundararajan Mahalingam, Goutham Shankar, Brian P. Mooney, Kamal Singh, Puttur Santhoshkumar, Krishna K. Sharma
Summary: This study demonstrates that specific mutations at certain residue positions in the N-terminal domain of α B-crystallin can reduce oligomer size and enhance chaperone function, indicating the importance of these residues in oligomerization and chaperone activity.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Sundararajan Mahalingam, Srabani Karmakar, Puttur Santhoshkumar, Krishna K. Sharma
Summary: The deletion of residues 54-61 from alpha B-crystallin results in increased chaperone activity and altered oligomeric assembly, with a different subunit organization observed in the mutant protein. The mutant protein shows more significant interaction with substrates and increased binding of the unfolding proteins compared to the wild-type protein. Additionally, the mutant exhibits enhanced anti-apoptotic activity, supported by reduced caspase activation and normalization of apoptotic cascade components in cells.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Biochemistry & Molecular Biology
Puttur Santhoshkumar, Krishna K. Sharma
Summary: The G98R mutation in alpha A-crystallin is associated with presenile cataract development in humans. The mutant protein initially gets stabilized upon interaction with substrate proteins, but the resulting complexes continue to increase in size over time, leading to cataract formation. The stability and chaperone activity of the mutant protein can be improved by modifying it with low concentrations of methylglyoxal (MGO).
FRONTIERS IN MOLECULAR BIOSCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Ashutosh S. Phadte, Puttur Santhoshkumar, K. Krishna Sharma
Article
Ophthalmology
Leike Xie, Puttur Santhoshkumar, Lixing W. Reneker, K. Krishna Sharma
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE
(2014)
Article
Materials Science, Biomaterials
Murugesan Raju, Puttur Santhoshkumar, K. Krishna Sharma
ADVANCED BIOSYSTEMS
(2018)