Nandita Mishra
Amrita Vishwa Vidyapeetham
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Publication
Featured researches published by Nandita Mishra.
Biochemical and Biophysical Research Communications | 2010
Nandita Mishra; Rekha Kar; Prajjal K. Singha; Manjeri A. Venkatachalam; Donald G. McEwen; Pothana Saikumar
Arachidonic acid derived endogenous electrophile 15d-PGJ2 has gained much attention in recent years due to its potent anti-proliferative and anti-inflammatory actions mediated through thiol modification of cysteine residues in its target proteins. Here, we show that 15d-PGJ2 at 1 microM concentration converts normal mitochondria into large elongated and interconnected mitochondria through direct binding to mitochondrial fission protein Drp1 and partial inhibition of its GTPase activity. Mitochondrial elongation induced by 15d-PGJ2 is accompanied by increased assembly of Drp1 into large oligomeric complexes through plausible intermolecular interactions. The role of decreased GTPase activity of Drp1 in the formation of large oligomeric complexes is evident when Drp1 is incubated with a non-cleavable GTP analog, GTPgammaS or by a mutation that inactivated GTPase activity of Drp1 (K38A). The mutation of cysteine residue (Cys644) in the GTPase effector domain, a reported target for modification by reactive electrophiles, to alanine mimicked K38A mutation induced Drp1 oligomerization and mitochondrial elongation, suggesting the importance of cysteine in GED to regulate the GTPase activity and mitochondrial morphology. Interestingly, treatment of K38A and C644A mutants with 15d-PGJ2 resulted in super oligomerization of both mutant Drp1s indicating that 15d-PGJ2 may further stabilize Drp1 oligomers formed by loss of GTPase activity through covalent modification of middle domain cysteine residues. The present study documents for the first time the regulation of a mitochondrial fission activity by a prostaglandin, which will provide clues for understanding the pathological and physiological consequences of accumulation of reactive electrophiles during oxidative stress, inflammation and degeneration.
Biochemical and Biophysical Research Communications | 2010
Rekha Kar; Nandita Mishra; Prajjal K. Singha; Manjeri A. Venkatachalam; Pothana Saikumar
We showed earlier that 15 deoxy Delta(12,14) prostaglandin J2 (15d-PGJ2) inactivates Drp1 and induces mitochondrial fusion [1]. However, prolonged incubation of cells with 15d-PGJ2 resulted in remodeling of fused mitochondria into large swollen mitochondria with irregular cristae structure. While initial fusion of mitochondria by 15d-PGJ2 required the presence of both outer (Mfn1 and Mfn2) and inner (OPA1) mitochondrial membrane fusion proteins, later mitochondrial changes involved increased degradation of the fusion protein OPA1 and ubiquitination of newly synthesized OPA1 along with decreased expression of Mfn1 and Mfn2, which likely contributed to the loss of tubular rigidity, disorganization of cristae, and formation of large swollen degenerated dysfunctional mitochondria. Similar to inhibition of Drp1 by 15d-PGJ2, decreased expression of fission protein Drp1 by siRNA also resulted in the loss of fusion proteins. Prevention of 15d-PGJ2 induced mitochondrial elongation by thiol antioxidants prevented not only loss of OPA1 isoforms but also its ubiquitination. These findings provide novel insights into unforeseen complexity of molecular events that modulate mitochondrial plasticity.
RSC Advances | 2016
K Yamini Yasoda; Kondapa Naidu Bobba; Divya Nedungadi; Debabrata Dutta; M Sathish Kumar; Nikhil K. Kothurkar; Nandita Mishra; Sankarprasad Bhuniya
A water-soluble and biocompatible polymer, i.e. biotinylated poly(vinyl alcohol)-grafted graphene oxide (GO), was used as a nanocarrier for targeted delivery of anticancer drug camptothecin (CPT). The extent of CPT release in the presence of glutathione (GSH) from GO–biotinPVA–CPT was monitored by the increase in the fluorescence intensity, at λmax = 450 nm. The cell-specific (HeLa) antiproliferative activity of GO–biotinPVA–CPT makes it suitable to be used for targeted delivery of chemotherapeutics to cancerous cells.
International Journal of Polymeric Materials | 2017
C. R. Reshmi; Tara Menon; Anupama Binoy; Nandita Mishra; K. K. Elyas; A. Sujith
ABSTRACT Here we report a novel bioactive electrospun mat based on poly(L-lactide-co-caprolactone) (PLLC) and collagen for wound dressing and sustained drug delivery of gentamicin. PLLC/collagen electrospun mat loaded with 10% gentamicin showed bioactivity for 15 days against Gram-positive and Gram-negative bacteria. The in vitro cell culture of 3T3 fibroblasts confirmed that these electrospun mat provide an increased specific interface area and hydrophilicity to enhance cell attachment, proliferation, and migration. The modified PLLC/collagen mat provided an excellent enhancement in properties of antibacterial wound dressings with a minimum in vitro toxicity and high potency for promoting wound healing stages. GRAPHICAL ABSTRACT
International Journal of Biological Macromolecules | 2018
Chandni Porayath; Maneesha K. Suresh; Raja Biswas; Bipin G. Nair; Nandita Mishra; Sanjay Pal
Major autolysin (Atl) of Staphylococcus aureusis a cell surface associated peptidoglycan hydrolase with amidase and glucosaminidase domains. Atl enzymes (amidase and glucosaminidase) are known to participate in biofilm formation and also can bind with host matrices. Earlier studies demonstrated the binding of Atlwithfibronectin, thrombospondin 1, vitronectin and heat shock cognate protein Hsc70. Here, we have shown, Atl mediates attachment of S.aureus to heparin and gelatine as well. The atl mutant strain demonstrated around 2.5 fold decreased adherence with fibronectin, gelatin and heparin coated microtiter plates. The microscopic studies confirmed the reduced binding of atl mutant with them compared to its parental wild type and complemented mutant strains. Amidase and glucosaminidase were expressed as N-terminal histidine tagged proteins from Escherichia coli, purified and refolded. We found refolded amidase bind with fibronectin, gelatin and heparin; whereas refolded glucosaminidase binds with only fibronectin and heparin but not gelatin. These results reemphasize Atl as one of the crucial proteins from Staphylococcus that facilitate their binding with multiple host cellular components during colonization and infection.
Experimental Cell Research | 2018
Divya Nedungadi; Anupama Binoy; Nanjan Pandurangan; Sanjay Pal; Bipin G. Nair; Nandita Mishra
&NA; An &agr;, &bgr;‐unsaturated carbonyl compound of ginger, 6‐Shogaol (6S), induced extensive cytoplasmic vacuolation and cell death in breast cancer cell (MDA‐MB‐231) and non‐small lung cancer (A549) cells. In the presence of autophagic inhibitors the cells continued to exhibit cytoplasmic vacuolation and cell death clearly distinguishing it from the classic autophagic process. 6S induced death did not exhibit the characteristic apoptotic features like caspase cleavage, phosphatidyl serine exposure and DNA fragmentation. The immunofluorescence with the Endoplasmic Reticulum (ER) resident protein, calreticulin indicated that the vacuoles were of ER origin, typical of paraptosis. This was supported by the increase in level of microtubule associated protein light chain 3B (LC3 I and LC3 II) and polyubiquitin binding protein, p62. The level of ER stress markers like polyubiquitinated proteins, Bip and CHOP also consistently increased. We have found that 6S inhibits the 26S proteasome. The proteasomal inhibitory activity was elucidated by a) molecular docking of 6S onto the active site of &bgr;5 subunit and b) reduced fluorescence by the fluorogenic substrate of the chymotrypsin‐like subunit. In conclusion these studies demonstrate for the first time that proteasomal inhibition by 6S induces cell death via paraptosis. So 6‐shogaol may act as a template for anti‐cancer lead discovery against the apoptosis resistant cancer cells.
Journal of Photochemistry and Photobiology B-biology | 2018
Richa Rashmi; Divya Nedungadi; Arup Podder; Nandita Mishra; Sankarprasad Bhuniya
We have developed endogenous redox-responsive polymer conjugated GO-based hybrid nanomaterials (GO-PEGssFol-CPT) for delivery of anticancer drug camptothecin (CPT) to the cancer cells. The synthesized intermediate (PEGSSFol) and CPT loaded GO- PEGSSFol were characterized using Fourier transform infrared spectroscopy (FTIR) and 1H NMR. The morphological feature changes of TEM and AFM images have confirmed the loading of CPT on the nanocarrier and its release from the nanocarrier. The amount of CPT was loaded was found to be 14.2%. The extent of camptothecin (CPT) release from GO-BiotinPVA-CPT in the presence of different concentrations of glutathione (GSH) was monitored with the increase in the fluorescence intensity at λmax 438 nm and UV-Vis absorbance at 366 nm. The time-dependent camptothecin (CPT) release was monitored in the presence of GSH. It was noticed that CPT was completely released from GO-PEGssFol-CPT within 45 min. This release process is free from interference by other ubiquitous analytes in the living system. The constant fluorescence intensity of GO-PEGssFol-CPT against acidic pH indicated that CPT would not be released in the extracellular region of cancer cells. Therefore, such delivery system could be used to prevent unwanted cytotoxicity to the healthy cells. The GO-PEGssFol-CPT showed higher antiproliferative activity against cervical cancer cells compared to the CPT. Thus, GO-PEGssFol-CPT can be a new material to deliver the anticancer drug to the target tumor region.
Chemical Communications | 2017
Nithya Velusamy; Anupama Binoy; Kondapa Naidu Bobba; Divya Nedungadi; Nandita Mishra; Sankarprasad Bhuniya
Cancer Research | 2010
Prajjal K. Singha; Nandita Mishra; Rekha Kar; Srilakshmi Pandeswara; Manjeri A. Venkatachalam; Pothana Saikumar
The 39th All India Cell Biology Conference on “Cellular Organization and Dynamics", Thiruvananthapuram, Kerala, India, | 2015
Chandni P; Pradeesh Babu; N Menon; V Aishwarya; C Nadkarni; G Vijayakumar; S Sukumaran; Ajith Madhavan; Bipin G. Nair; Nandita Mishra; Sanjay Pal
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University of Texas Health Science Center at San Antonio
View shared research outputsUniversity of Texas Health Science Center at San Antonio
View shared research outputsUniversity of Texas Health Science Center at San Antonio
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