Time filter

Source Type

Vaid S.,Grant Medical Foundation | Manikoth M.,Dr Manojs Superspeciality ENT Institute
Cochlear Implants International | Year: 2013

One of the most dreaded complications after cochlear implantation is infection. These infections are a challenge due to lack of any data regarding optimal methods of investigation and management. More often than not, these patients have to undergo explantation and revision surgery. This paper presents a case report and literature review which focuses on the role of antibiotics and the need for early explantation in most biofilm-related infections of cochlear implants. © W. S. Maney & Son Ltd 2013. Source

Vaid N.,BIG EARS | Thomas Roland J.,Otolaryngology and Neurosurgery | Thomas Roland J.,Cochlear Implant Center | Vaid S.,Grant Medical Foundation
Cochlear Implants International | Year: 2011

Extra-cochlear electrode extrusion is a potentially under-recognized complication of cochlear implantation. As the age of implantation becomes younger, electrode extrusion is of concern due to future skull growth. Extrusion of several electrodes may compromise performance and thus require surgical reinsertion of the electrodes. Almost 60% of patients with electrode extrusion have required revision surgery. This paper presents a case report and literature review which discusses factors which contribute to electrode extrusion and emphasizes the need for a high degree of suspicion in certain situations. Surgical steps such as electrode fixation techniques are highlighted in order to attempt to reduce the occurrence of this complication. © W.S. Maney & Son Ltd. 2011. Source

Kumar V.,National Center for Cell Science | Behera R.,National Center for Cell Science | Lohite K.,Grant Medical Foundation | Karnik S.,Grant Medical Foundation | Kundu G.C.,National Center for Cell Science
Cancer Research | Year: 2010

p38 kinases activated by growth factors, hormones, and environmental stresses exert diverse functions in regulating normal and malignant cell pathophysiology. Enhanced levels of activated p38 isoforms have been linked with poor prognosis in breast cancer, although the mechanistic basis for this association is poorly understood. In this study, we report that p38 activation in cervical cancer cells is driven by osteopontin (OPN), an extracellular matrix-associated cytokine that drives invasive progression. OPN regulates CD44-mediated p38 phosphorylation that induces NF-κB activation and NF-κB-dependent expression of furin, an extracellular protease implicated in human papilloma virus (HPV) processing that enhances cervical cancer cell motility. OPN induces CD44-mediated MKK3/6 phosphorylation which in turn phosphorylates p38 in these cells. OPN-induced furin expression and cell motility was impeded by blockades to MKK3/6, p38α/β or NF-κB signaling. In a mouse xenograft model of human cervical cancer, tumor growth was enhanced by OPN overexpression and blocked by short hairpin RNA (shRNA)-mediated OPN silencing. Furin overexpression similarly augmented tumor growth in the model, whereas blocking MKK3/6, p38, or furin reduced OPN-induced cervical tumor growth. Analysis of clinical specimens revealed that enhanced expression of OPN, phosphorylated NF-κB, p65, and furin correlated with cervical cancer progression, further strengthening the in vitro and in vivo results. In summary, our findings offer a proof of concept for targeting OPN and its downstream p38 signaling as a novel therapeutic strategy to manage cervical cancer. ©2010 AACR. Source

Vaid S.,Grant Medical Foundation | Vaid N.,KEM Hospital | Rathod S.,Grant Medical Foundation
Otology and Neurotology | Year: 2012

Objective: To highlight the importance of imaging the geniculate fossa in patients with solitary infranuclear facial palsy. Study Design: Prospective. Setting: Tertiary referral center. ELIGIBILITY CRITERIA: Patients with solitary infranuclear facial palsy sent for imaging. INTERVENTION: Diagnostic. MAIN OUTCOME MEASURE: Imaging specifics concerning high-resolution computed tomography (HRCT) and magnetic resonance imaging (MRI) are described in detail for evaluation of the intratemporal part of the facial nerve with special focus on the geniculate fossa. Results: Normal appearances of the geniculate fossa on HRCT and MRI and its normal anatomic variant, that is, dehiscence of the overlying bone are described. Imaging findings in a range of pathologies involving the geniculate fossa in a clinical setting of infranuclear facial nerve palsy is demonstrated. These include infections (tuberculosis), trauma, schwannoma, hemangioma, meningioma, and perineural spread of parotid malignancy. Conclusion: The geniculate fossa is a small bony hiatus in the temporal bone and is situated at the junction of the labyrinthine and the tympanic segments of the intratemporal facial nerve canal. It houses important neural structures and is best visualized by a combination of HRCT and high-resolution MRI examination of the temporal bone. It is therefore imperative for imaging specialists to be familiar with the normal appearance of this structure on HRCT and MRI examinations of the temporal bone as subtle imaging findings involving the geniculate fossa can be indicators of a variety of abnormalities. © 2012, Otology & Neurotology, Inc. Source

Mishra R.,Angiogenesis and Nanomedicine Research | Thorat D.,Angiogenesis and Nanomedicine Research | Soundararajan G.,Angiogenesis and Nanomedicine Research | Pradhan S.J.,Angiogenesis and Nanomedicine Research | And 4 more authors.
Oncogene | Year: 2014

Semaphorin 3A (Sema 3A), a member of semaphorin family, serves as a guidance clue during embryonic development and is known as a candidate tumor suppressor that attenuates breast tumor progression by binding with its co-receptor, neuropilin-1 (NRP-1). However, the underlying mechanism by which Sema 3A suppresses breast tumor growth is still unexplored. In this study, we report that Sema 3A regulates phosphorylation and nuclear translocation of phosphatase and tensin homolog (PTEN) and FOXO 3a. Moreover, Sema 3A controls NRP-1-mediated PTEN-dependent FOXO 3a activation. Overexpression of PTEN and FOXO 3a enhances Sema 3A-induced attenuation of breast cancer cell migration. Chromatin immunoprecipitation and electrophoretic mobility shift assay data revealed that FOXO 3a regulates MelCAM at the transcriptional level. Furthermore, Sema 3A induces NRP-1-mediated MelCAM expression through PTEN and FOXO 3a. The data also showed that vascular endothelial growth factor-induced angiogenesis is inhibited by Sema 3A. Loss of or gain in function study revealed that Sema 3A modulates phosphorylation of PTEN and FOXO 3a and expression of MelCAM, leading to suppression of tumor growth and angiogenesis using in vivo mice model. Clinical specimen analysis revealed that reduced expression of Sema 3A and p-PTEN are correlated with enhanced breast cancer progression, further strengthening our in vitro and in vivo findings. Correlation of relapse-free survival of breast cancer patients (n=2878) with expression levels of Sema 3A, NRP-1, FOXO 3a and MelCAM were studied by Kaplan-Meier analysis. Statistical analysis revealed a close association between reduced expression of Sema 3A and MelCAM with that of poor patient's survival. Our study demonstrated a novel mechanism of regulation of tumor suppression by Sema 3A in coordination with a chain of tumor-suppressor genes, which in turn inhibits breast cancer cell migration, tumor growth and angiogenesis.Oncogene advance online publication, 14 April 2014; doi:10.1038/onc.2014.79. Source

Discover hidden collaborations