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Article ; Online: Regulatory T cells: Their role in triple-negative breast cancer progression and metastasis.

Malla, Rama Rao / Vasudevaraju, Padmaraju / Vempati, Rahul Kumar / Rakshmitha, Marni / Merchant, Neha / Nagaraju, Ganji Purnachandra

Cancer

2022 Volume 128, Issue 6, Page(s) 1171–1183

Abstract: Triple-negative breast cancer (TNBC) is an aggressive and immunogenic subtype of breast cancer. This tumorigenicity is independent of hormonal or HER2 pathways because of a lack of respective receptor expression. TNBC is extremely prone to drug ... ...

Abstract	Triple-negative breast cancer (TNBC) is an aggressive and immunogenic subtype of breast cancer. This tumorigenicity is independent of hormonal or HER2 pathways because of a lack of respective receptor expression. TNBC is extremely prone to drug resistance and early recurrence because of T-regulatory cell (Treg) infiltration into the tumor microenvironment (TME) in addition to other mechanisms like genomic instability. Tumor-infiltrating Tregs interact with both tumor and stromal cells as well as extracellular matrix components in the TME and induce an immune-suppressive phenotype. Hence, treatment of TNBC with conventional therapies remains challenging. Understanding the protective mechanism of Tregs in shielding TNBC from antitumor immune responses in the TME will pave the way for developing novel, immune-based therapeutics. The current review focuses on the role of tumor-infiltrating Tregs in tumor progression and metabolic reprogramming of the TME. The authors have extended their focus to oncotargeting Treg-mediated immune suppression in breast cancer. Because of its potential role in the TME, modulating Treg activity may provide a novel strategic intervention to combat TNBC. Both under laboratory conditions and in clinical trials, currently available anticancer drugs and natural therapeutics as potential agents for targeting Tregs are explored.
MeSH term(s)	Humans ; T-Lymphocytes, Regulatory ; Triple Negative Breast Neoplasms/pathology ; Tumor Microenvironment
Language	English
Publishing date	2022-01-06
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1429-1
ISSN	1097-0142 ; 0008-543X ; 1934-662X
ISSN (online)	1097-0142
ISSN	0008-543X ; 1934-662X
DOI	10.1002/cncr.34084
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Article ; Online: DNA induced folding/fibrillation of alpha-synuclein: new insights in Parkinson's disease.

Hegde, Muralidhar L / Vasudevaraju, Padmaraju / Rao, Kosagisharaf Jagannatha

Frontiers in bioscience (Landmark edition)

2010 Volume 15, Issue 2, Page(s) 418–436

Abstract: Emerging evidences on the nuclear localization of alpha-Synuclein in neurons and a close look in to its primary sequence/structural organization led us to examine its DNA binding ability. Subsequently, we first time demonstrated the interaction of DNA ... ...

Abstract	Emerging evidences on the nuclear localization of alpha-Synuclein in neurons and a close look in to its primary sequence/structural organization led us to examine its DNA binding ability. Subsequently, we first time demonstrated the interaction of DNA with alpha-Synuclein which was also confirmed by others. We recently showed that double-stranded oligos induce partial folding in alpha-Synuclein and promote its aggregation, where as single-strand circular DNA and supercoiled plasmid DNA induced a helix-rich conformation and protected the protein from fibrillation. In turn, alpha-Synuclein modulates DNA conformation from B- to an altered B-form, which may affect DNA transactions. Interestingly, amyloid-beta peptides and prion proteins implicated in Alzheimer's disease and Prion diseases respectively, were also shown to have DNA binding activity which suggests that DNA binding may be a common property of many amyloidogenic proteins associated with various neurodegenerative disorders. In this review, we debate the biological significance of DNA-alpha-Synuclein interactions; it's beneficial vs. toxic role in relevance to Parkinson's disease.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; Humans ; Models, Biological ; Nucleic Acid Conformation ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Protein Binding ; Protein Folding ; alpha-Synuclein/chemistry ; alpha-Synuclein/metabolism
Chemical Substances	alpha-Synuclein ; DNA (9007-49-2)
Language	English
Publishing date	2010-01-01
Publishing country	Singapore
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2704569-9
ISSN	2768-6698 ; 1093-9946
ISSN (online)	2768-6698
ISSN	1093-9946
DOI	10.2741/3628
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Article ; Online: Protection of DNA and erythrocytes from free radical induced oxidative damage by black gram (Vigna mungo L.) husk extract.

Girish, Talakatta K / Vasudevaraju, Padmaraju / Prasada Rao, Ummiti J S

Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association

2012 Volume 50, Issue 5, Page(s) 1690–1696

Abstract: Antioxidants present in various plant tissues exhibit health benefits by scavenging reactive oxygen species generated under various pathophysiological conditions. In the present study, bioactive compounds from black gram husk were extracted with water ... ...

Abstract	Antioxidants present in various plant tissues exhibit health benefits by scavenging reactive oxygen species generated under various pathophysiological conditions. In the present study, bioactive compounds from black gram husk were extracted with water and the protection of black gram husk (BGH) extract against oxidative damage in DNA and erythrocytes were studied. BGH extract had total polyphenol content of 59 mg of gallic acid equivalents (GAE). The phenolic acids identified in the extract using RP-HPLC were gallic, protocatechuic, gentisic and ferulic acids. The extract showed good antioxidant properties. The IC(50) value for DPPH radical scavenging activity was found to be 3.92 μg of GAE. The BGH extract also showed α-glucosidase inhibition and the IC(50) value was found to be 2.78 μg of GAE. The oxidative hemolysis caused by hydrogen peroxide in rat erythrocytes was inhibited by BGH extract in a dose dependent manner. The IC(50) values for BGH extract and BHA for hemolysis were 11.5 and 14 μg of GAE, respectively. Morphological changes in erythrocyte membrane caused by hydrogen peroxide were protected by BGH extract. As BGH extract exhibited various antioxidant properties in different systems, it could be used as a functional food or nutraceutical product for health benefits.
MeSH term(s)	Animals ; Antioxidants/pharmacology ; DNA/drug effects ; DNA Damage ; Electrophoresis, Agar Gel ; Electrophoresis, Polyacrylamide Gel ; Erythrocytes/drug effects ; Erythrocytes/ultrastructure ; Fabaceae/chemistry ; Free Radicals ; Hemolysis/drug effects ; Microscopy, Electron, Scanning ; Oxidative Stress/drug effects ; Plant Extracts/pharmacology ; Rats
Chemical Substances	Antioxidants ; Free Radicals ; Plant Extracts ; DNA (9007-49-2)
Language	English
Publishing date	2012-05
Publishing country	England
Document type	Journal Article
ZDB-ID	782617-5
ISSN	1873-6351 ; 0278-6915
ISSN (online)	1873-6351
ISSN	0278-6915
DOI	10.1016/j.fct.2012.01.043
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Article ; Online: In vitro evidence that an aqueous extract of Centella asiatica modulates α-synuclein aggregation dynamics.

Berrocal, Ruben / Vasudevaraju, Padmaraju / Indi, Shantinath Satappa / Sambasiva Rao, Krothapalli Raja Surya / Rao, K S

Journal of Alzheimer's disease : JAD

2014 Volume 39, Issue 2, Page(s) 457–465

Abstract: α-Synuclein aggregation is one of the major etiological factors implicated in Parkinson's disease (PD). The prevention of aggregation of α-synuclein is a potential therapeutic intervention for preventing PD. The discovery of natural products as ... ...

Abstract	α-Synuclein aggregation is one of the major etiological factors implicated in Parkinson's disease (PD). The prevention of aggregation of α-synuclein is a potential therapeutic intervention for preventing PD. The discovery of natural products as alternative drugs to treat PD and related disorders is a current trend. The aqueous extract of Centella asiatica (CA) is traditionally used as a brain tonic and CA is known to improve cognition and memory. There are limited data on the role of CA in modulating amyloid-β (Aβ) levels in the brain and in Aβ aggregation. Our study focuses on CA as a modulator of the α-synuclein aggregation pattern in vitro. Our investigation is focused on: (i) whether the CA leaf aqueous extract prevents the formation of aggregates from monomers (Phase I: α-synuclein + extract co-incubation); (ii) whether the CA aqueous extract prevents the formation of fibrils from oligomers (Phase II: extract added after oligomers formation); and (iii) whether the CA aqueous extract disintegrates the pre-formed fibrils (Phase III: extract added to mature fibrils and incubated for 9 days). The aggregation kinetics are studied using a thioflavin-T assay, circular dichroism, and transmission electron microscopy. The results showed that the CA aqueous extract completely inhibited the α-synuclein aggregation from monomers. Further, CA extract significantly inhibited the formation of oligomer to aggregates and favored the disintegration of the preformed fibrils. The study provides an insight in finding new natural products for future PD therapeutics.
MeSH term(s)	Antiparkinson Agents/chemistry ; Antiparkinson Agents/pharmacology ; Circular Dichroism ; Electrophoresis, Polyacrylamide Gel ; Fluorescence ; Kinetics ; Microscopy, Electron, Transmission ; Plant Extracts/chemistry ; Plant Extracts/pharmacology ; Polyphenols/chemistry ; Protein Multimerization/drug effects ; Thiazoles ; Triterpenes/chemistry ; Triterpenes/pharmacology ; Water/chemistry ; alpha-Synuclein/chemistry
Chemical Substances	Antiparkinson Agents ; Centella asiatica extract ; Plant Extracts ; Polyphenols ; Thiazoles ; Triterpenes ; alpha-Synuclein ; Water (059QF0KO0R) ; thioflavin T (2390-54-7)
Language	English
Publishing date	2014
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-131187
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Article: Protection of DNA and erythrocytes from free radical induced oxidative damage by black gram (Vigna mungo L.) husk extract

Girish, T. K. / Vasudevaraju, P. / Rao, U. J. S. Prasada

Food and chemical toxicology

2012 Volume 50, Issue 5, Page(s) 1690–1696

Language	English
Document type	Article
ZDB-ID	782617-5
ISSN	0278-6915
Database	Current Contents Nutrition, Environment, Agriculture

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Article ; Online: Recent advances in α-synuclein functions, advanced glycation, and toxicity: implications for Parkinson's disease.

Guerrero, Erika / Vasudevaraju, P / Hegde, Muralidhar L / Britton, G B / Rao, K S

Molecular neurobiology

2012 Volume 47, Issue 2, Page(s) 525–536

Abstract: The toxicity of α-synuclein in the neuropathology of Parkinson's disease which includes its hallmark aggregation has been studied scrupulously in the last decade. Although little is known regarding the normal functions of α-synuclein, its association ... ...

Abstract	The toxicity of α-synuclein in the neuropathology of Parkinson's disease which includes its hallmark aggregation has been studied scrupulously in the last decade. Although little is known regarding the normal functions of α-synuclein, its association with membrane phospholipids suggests its potential role in signaling pathways. Following extensive evidences for its nuclear localization, we and others recently demonstrated DNA binding activity of α-synuclein that modulates its conformation as well as aggregation properties. Furthermore, we also underscored the similarities among various amyloidogenic proteins involved in neurodegenerative diseases including amyloid beta peptides and tau. Our more recent studies show that α-synuclein is glycated and glycosylated both in vitro and in neurons, significantly affecting its folding, oligomeric, and DNA binding properties. Glycated α-synuclein causes increased genome damage both via its direct interaction with DNA and by increased generation of reactive oxygen species as glycation byproduct. In this review, we discuss the mechanisms of glycation and other posttranslational modifications of α-synuclein, including phosphorylation and nitration, and their role in neuronal death in Parkinson's disease.
MeSH term(s)	Animals ; Cell Death/physiology ; Glycation End Products, Advanced/metabolism ; Glycosylation ; Humans ; Parkinson Disease/metabolism ; Parkinson Disease/pathology ; Phosphorylation/physiology ; Protein Binding/physiology ; Protein Folding ; alpha-Synuclein/adverse effects ; alpha-Synuclein/physiology ; alpha-Synuclein/toxicity
Chemical Substances	Glycation End Products, Advanced ; alpha-Synuclein
Language	English
Publishing date	2012-08-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	645020-9
ISSN	1559-1182 ; 0893-7648
ISSN (online)	1559-1182
ISSN	0893-7648
DOI	10.1007/s12035-012-8328-z
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Zs.A 2411: Show issues

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Article ; Online: New evidence on α-synuclein and Tau binding to conformation and sequence specific GC* rich DNA: Relevance to neurological disorders.

Vasudevaraju, P / Guerrero, Erika / Hegde, Muralidhar L / Collen, T B / Britton, Gabrielle B / Rao, K S

Journal of pharmacy & bioallied sciences

2012 Volume 4, Issue 2, Page(s) 112–117

Abstract: Background: Deoxyribonucleic acid (DNA) topology plays a critical role in maintaining the integrity of the genome and cellular functions. Although changes in DNA conformation and structural dynamics in the brain have been associated with various ... ...

Abstract	Background: Deoxyribonucleic acid (DNA) topology plays a critical role in maintaining the integrity of the genome and cellular functions. Although changes in DNA conformation and structural dynamics in the brain have been associated with various neurological disorders, its precise role in the pathogenesis is still unclear. Previous studies from our laboratory have shown that there is a conformational change in the genomic DNA of Parkinson's disease (PD) (B to altered B-DNA) and Alzheimer's disease brain (B to Z-DNA). However, there is limited information on the mechanism on DNA dynamics changes in brain. Objective: In the present study, we have investigated the DNA conformation and sequence specific binding ability of α-Synuclein and Tau with reference to B-DNA and Z-DNA using oligonucleotide (CGCGCGCG)(2) as a novel model DNA system. This sequence is predominantly present in the promoter region of the genes of biological relevance. Materials and methods: Natively, (CGCGCGCG)(2) sequence exists in B-DNA conformation, but in the presence of high sodium concentration (4 M NaCl), the oligo converts into Z-DNA form. We used circular dichroism, melting temperature and fluorescence studies to understand protein-DNA interactions. Results: CD studies indicated that both α-Synuclein and Tau bind to B-DNA conformation of (CGCGCGCG)(2) and induce altered B-form. Further, these proteins increased the melting temperature and decreased the number of EtBr molecules bound per base pair of DNA in B-form indicating that DNA stability is favored to alter B-DNA conformation, which could be an intermediate form favoring Z-DNA conformation. Moreover, both α-Synuclein and Tau also bound to disease-linked Z-DNA conformation of (CGCGCGCG)(2) and further stabilized the Z-conformation. Conclusions: The present study provides vital mechanistic information on Synuclein and Tau binding to DNA in a conformation-specific manner causing conformational transition. Furthermore, both the proteins stabilize Z-DNA conformation. These have altered minor and major groove patterns and thus may have significant biological implications in relevance to gene expression pattern in neurodegeneration. We discuss the implications of α-Synuclein/Tau binding to DNA and stabilizing the altered conformations of DNA in neuronal cell dysfunction.
Language	English
Publishing date	2012-04-30
Publishing country	India
Document type	Journal Article
ZDB-ID	2573569-X
ISSN	0975-7406 ; 0975-7406
ISSN (online)	0975-7406
ISSN	0975-7406
DOI	10.4103/0975-7406.94811
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Article ; Online: The biochemistry of belief.

Sathyanarayana Rao, T S / Asha, M R / Jagannatha Rao, K S / Vasudevaraju, P

Indian journal of psychiatry

2010 Volume 51, Issue 4, Page(s) 239–241

Language	English
Publishing date	2010-01-04
Publishing country	India
Document type	Journal Article
ZDB-ID	221523-8
ISSN	1998-3794 ; 0019-5545
ISSN (online)	1998-3794
ISSN	0019-5545
DOI	10.4103/0019-5545.58285
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Article ; Online: Molecular biology research in neuropsychiatry: India's contribution.

Sathyanarayana Rao, T S / Ramesh, B N / Vasudevaraju, P / Rao, K S J

Indian journal of psychiatry

2010 Volume 52, Issue Suppl 1, Page(s) S120–7

Abstract: Neuropsychiatric disorders represent the second largest cause of morbidity worldwide. These disorders have complex etiology and patho-physiology. The major lacunae in the biology of the psychiatric disorders include genomics, biomarkers and drug ... ...

Abstract	Neuropsychiatric disorders represent the second largest cause of morbidity worldwide. These disorders have complex etiology and patho-physiology. The major lacunae in the biology of the psychiatric disorders include genomics, biomarkers and drug discovery, for the early detection of the disease, and have great application in the clinical management of disease. Indian psychiatrists and scientists played a significant role in filling the gaps. The present annotation provides in depth information related to research contributions on the molecular biology research in neuropsychiatric disorders in India. There is a great need for further research in this direction as to understand the genetic association of the neuropsychiatric disorders; molecular biology has a tremendous role to play. The alterations in gene expression are implicated in the pathogenesis of several neuropsychiatric disorders, including drug addiction and depression. The development of transgenic neuropsychiatric animal models is of great thrust areas. No studies from India in this direction. Biomarkers in neuropsychiatric disorders are of great help to the clinicians for the early diagnosis of the disorders. The studies related to gene-environment interactions, DNA instability, oxidative stress are less studied in neuropsychiatric disorders and making efforts in this direction will lead to pioneers in these areas of research in India. In conclusion, we provided an insight for future research direction in molecular understanding of neuropsychiatry disorders.
Language	English
Publishing date	2010-09-21
Publishing country	India
Document type	Journal Article
ZDB-ID	221523-8
ISSN	1998-3794 ; 0019-5545
ISSN (online)	1998-3794
ISSN	0019-5545
DOI	10.4103/0019-5545.69223
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Article: Molecular toxicity of aluminium in relation to neurodegeneration.

Vasudevaraju, P / Govindaraju, M / Palanisamy, A P / Sambamurti, K / Rao, K S J

The Indian journal of medical research

2008 Volume 128, Issue 4, Page(s) 545–556

Abstract: Exposure to high levels of aluminium (Al) leads to neurofibrillary degeneration and that Al concentration is increased in degenerating neurons in Alzheimer's disease (AD). Nevertheless, the role of Al in AD remains controversial and there is little proof ...

Abstract	Exposure to high levels of aluminium (Al) leads to neurofibrillary degeneration and that Al concentration is increased in degenerating neurons in Alzheimer's disease (AD). Nevertheless, the role of Al in AD remains controversial and there is little proof directly interlinking Al to AD. The major problem in understanding Al toxicity is the complex Al speciation chemistry in biological systems. A new dimension is provided to show that Al-maltolate treated aged rabbits can be used as a suitable animal model for understanding the pathology in AD. The intracisternal injection of Al-maltolate into aged New Zealand white rabbits results in pathology that mimics several of the neuropathological, biochemical and behavioural changes as observed in AD. The neurodegenerative effects include the formation of intraneuronal neurofilamentous aggregates that are tau positive, oxidative stress and apoptosis. The present review discusses the role of Al and use of Al-treated aged rabbit as a suitable animal model to understand AD pathogenesis.
MeSH term(s)	Aluminum/toxicity ; Alzheimer Disease/chemically induced ; Animals ; Disease Models, Animal ; Rabbits
Chemical Substances	Aluminum (CPD4NFA903)
Language	English
Publishing date	2008-10
Publishing country	India
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	390883-5
ISSN	0971-5916 ; 0019-5340
ISSN	0971-5916 ; 0019-5340
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