Back to Authors

Vohra, Pawan K.

Mayo Clinic

Mayo Clinic

Citations 13

Differential Expression of ErbB Receptors on Typical Pulmonary Carcinoid Cancers
Vohra, Pawan K., Sanyal, Bharati, Thomas, Charles F.

The FASEB Journal | June 21, 2021 | Volume: 20 | Issue: 4 | Pages: No page available

10.1096/fasebj.20.4.a508-d Get It

Lung cancer is the leading cause of cancer‐related death inthe United States. Pulmonary typical carcinoid (TC) cancers are part of a spectrum of neuroendocrine lung cancers which includes small cell lung cancer (SCLC). Besides surgery, there are limited treatment options available for patients with these cancers, emphasizing the need for the development of new treatments. The c‐erbB family of receptor tyrosine kinases (ErbB1‐4) mediate cellular responses to growth factors and interact with downstream signaling pathways to promote tumorigenesis through abnormal cell proliferation. ErbB1 (EGFR) has received considerable attention in NSCLC since somatic mutations in the tyrosine kinase domain correlated with responsiveness to gefitinib. In NSCLC, breast, and ovarian cancer, ErbB2/ErbB3 heterodimers have been found to be expressed and signal to downstream pathways such as ERK. ErbB4 has been shown to promote proliferation or differentiation of neural tumors (ependymoma, gliomas, and meningiomas), ovarian cancer, and osteosarcoma. We recently examined the expression of ErbB receptors on TC cancers by quantitative real‐time RT‐PCR and immunoblotting. TCs have high expression of ErbB3 with moderate expression of ErbB1 and ErbB4 and lack expression of ErbB2. This contrasts with atypical carcinoids and SCLC which have high expression of ErbB4 with minimal expression of ErbB3 and lack expression of ErbB1 and ErbB2. We believe that investigation of ErbB signaling in pulmonary carcinoids will lead to new insights into the biology of these cancers, the understanding of which could lead to the development of novel treatments. Supported by funds from Mayo Foundation.
Functional Characterization of the Pneumocystis carinii Pheromone Receptor STE2
Vohra, Pawan K., Sanyal, Bharati, Thomas, Charles F.

The FASEB Journal | April 10, 2020 | Volume: 21 | Issue: 5 | Pages: No page available

10.1096/fasebj.21.5.a620-c Get It

The cellular differentiation of Pneumocystis carinii (PC) from the trophic forms to the multinucleated cyst is critical to understand the pathogenesis of this fungus. Still the mechanism of life cycle regulation is not well known. In fungi closely related to PC, a mitogen‐activated protein kinase (MAPK) cascade regulates these processes. Conjugation between two haploid cells occurs after pheromones bind to their respective pheromone receptors on cells of opposite mating types. We previously reported a functional analysis of the PCSTE3 pheromone receptor of PC, and now we report characteristics of the cognate receptor, PCSTE2. We cloned the full‐length 1065‐bp cDNA for PCSTE2, of which the translated open‐reading frame encodes a protein of 354 amino acids with greatest homology to the fungal pheromone receptors from S. cerevisiae Ste2 and S. pombe Mam2. Computer prediction modeling of PCSTE2 reveals seven transmembrane domains characteristic of fungal pheromone receptors. Similar to the S. cerevisiae alpha factor receptor Ste2, PCSTE2 has three extracellular domains implicated in ligand binding. An antibody made against the extracellular domain of PCSTE2 identified PCSTE2 receptor expression on a subpopulation of PC organisms in infected rat lung tissue but not normal uninfected tissue. We expressed PCSTE2 in S. cerevisiae Ste2 knockout yeast for functional characterization. Our identification of both PCSTE2 and PCSTE3 pheromone receptors may help to elucidate mechanisms of PC life cycle regulation and potential new therapeutics for treating PC pneumonia through alterations of MAPK signaling. Supported by NIH grant 2R01 AI‐48409 to CFT.
Caveolin-1 knockout mice exhibit airway hyperreactivity
Aravamudan, Bharathi, VanOosten, Sarah Kay, Meuchel, Lucas W., Vohra, Pawan K., Prakash, Y. S. , Thompson, Michael A. , Sieck, Gary C. , Pabelick, Christina M. , Prakash, Y S

American Journal of Physiology-Lung Cellular and Molecular Physiology | August 24, 2012 | Volume: 303 | Issue: 8 | Pages: L669-L681

10.1152/ajplung.00018.2012 Get It

Caveolae are flask-shaped plasma membrane invaginations expressing the scaffolding caveolin proteins. Although caveolins have been found in endothelium and epithelium (where they regulate nitric oxide synthase activity), their role in smooth muscle is still under investigation. We and others have previously shown that caveolae of human airway smooth muscle (ASM), which express caveolin-1, contain Ca 2+ and force regulatory proteins and are involved in mediating the effects of inflammatory cytokines such as TNF-α on intracellular Ca 2+ concentration responses to agonist. Accordingly, we tested the hypothesis that in vivo, absence of caveolin-1 leads to reduced airway hyperresponsiveness, using a knockout (KO) (Cav1 KO) mouse and an ovalbumin-sensitized/challenged (OVA) model of allergic airway hyperresponsiveness. Surprisingly, airway responsiveness to methacholine, tested by use of a FlexiVent system, was increased in Cav1 KO control (CTL) as well as KO OVA mice, which could not be explained by a blunted immune response to OVA. In ASM of wild-type (WT) OVA mice, expression of caveolin-1, the caveolar adapter proteins cavins 1–3, and caveolae-associated Ca 2+ and force regulatory proteins such as Orai1 and RhoA were all increased, effects absent in Cav1 KO CTL and OVA mice. However, as with WT OVA, both CTL and OVA Cav1 KO airways showed signs of enhanced remodeling, with high expression of proliferation markers and increased collagen. Separately, epithelial cells from airways of all three groups displayed lower endothelial but higher inducible nitric oxide synthase and arginase expression. Arginase activity was also increased in these three groups, and the inhibitor nor-NOHA ( N-omega-nor-l-arginine) enhanced sensitivity of isolated tracheal rings to ACh, especially in Cav1 KO mice. On the basis of these data disproving our original hypothesis, we conclude that caveolin-1 has complex effects on ASM vs. epithelium, resulting in airway hyperreactivity in vivo mediated by altered airway remodeling and bronchodilation.
Revealing the role of phospholipase Cβ3 in the regulation of VEGF-induced vascular permeability
Hoeppner, Luke H. , Phoenix, Kathryn N., Clark, Karl J. , Gong, Xun , Sciuto, Tracey , Vohra, Pawan K., Suresh, Sandip , Dvořàk, Ann M., Ekker, Stephen C. , Dvorak, Harold F., Claffey, Kevin P. , Bhattacharya, Resham , Bhattacharya, Santanu , Mukhopadhyay, Debabrata , Ekker, Stephen C , Clark, Karl J , Gong, Xun

Blood | June 7, 2012 | Volume: 120 | Issue: 11 | Pages: 2167-2173

10.1182/blood-2012-03-417824 Get It

AbstractVEGF induces vascular permeability (VP) in ischemic diseases and cancer, leading to many pathophysiological consequences. The molecular mechanisms by which VEGF acts to induce hyperpermeability are poorly understood and in vivo models that easily facilitate real-time, genetic studies of VP do not exist. In the present study, we report a heat-inducible VEGF transgenic zebrafish (Danio rerio) model through which VP can be monitored in real time. Using this approach with morpholino-mediated gene knock-down and knockout mice, we describe a novel role of phospholipase Cβ3 as a negative regulator of VEGF-mediated VP by regulating intracellular Ca2+ release. Our results suggest an important effect of PLCβ3 on VP and provide a new model with which to identify genetic regulators of VP crucial to several disease processes.
NHERF-2 maintains endothelial homeostasis
Wang, Enfeng , Dutta, Shamit K., Vohra, Pawan K., Guangqi, E, Prakash, Y. S. , Bhattacharya, Resham , Mukhopadhyay, Debabrata , Prakash, Y S

Blood | February 18, 2012 | Volume: 119 | Issue: 20 | Pages: 4798-4806

10.1182/blood-2011-11-392563 Get It

AbstractThe Na+/H+ exchanger regulatory factor-2 (NHERF-2) is an integral component of almost all endothelial cells (ECs), yet its endothelial function is not known. Here, we found that NHERF-2, is a key regulator of endothelial homeostasis because NHERF-2–silenced ECs proliferate at a much higher rate even in the absence of mitogens such as VEGF compared with control ECs. We further show that the hyperproliferation phenotype of NHERF-2–silenced EC is because of an accelerated cell cycle that is probably caused by a combination of the following factors: increased cytoplasmic calcium, increased expression of c-Myc, increased expression of cyclin D1, and reduced expression of p27. Using an experimental mouse model of human hemangioma, we found that the endothelial neoplasms derived from NHERF-2–silenced cells were much larger in volume than those derived from control cells. Thus, NHERF-2 is a negative regulator of endothelial proliferation and may have important roles in endothelial homeostasis and vascular modeling.
Dopamine inhibits pulmonary edema through the VEGF-VEGFR2 axis in a murine model of acute lung injury
Vohra, Pawan K., Hoeppner, Luke H. , Sagar, Gunisha, Dutta, Shamit K., Misra, Sanjay, Hubmayr, Rolf D., Misra, Sanjay , Mukhopadhyay, Debabrata , Misra, Sanjay

American Journal of Physiology-Lung Cellular and Molecular Physiology | October 15, 2011 | Volume: 302 | Issue: 2 | Pages: L185-L192

10.1152/ajplung.00274.2010 Get It

The neurotransmitter dopamine and its dopamine receptor D2 (D2DR) agonists are known to inhibit vascular permeability factor/vascular endothelial growth factor (VEGF)-mediated angiogenesis and vascular permeability. Lung injury is a clinical syndrome associated with increased microvascular permeability. However, the effects of dopamine on pulmonary edema, a phenomenon critical to the pathophysiology of both acute and chronic lung injuries, have yet to be established. Therefore, we sought to determine the potential therapeutic effects of dopamine in a murine model of lipopolysaccharide (LPS)-induced acute lung injury (ALI). Compared with sham-treated controls, pretreatment with dopamine (50 mg/kg body wt) ameliorated LPS-mediated edema formation and lowered myeloperoxidase activity, a measure of neutrophil infiltration. Moreover, dopamine significantly increased survival rates of LPS-treated mice, from 0–75%. Mechanistically, we found that dopamine acts through the VEGF-VEGFR2 axis to reduce pulmonary edema, as dopamine pretreatment in LPS-treated mice resulted in decreased serum VEGF, VEGFR2 phosphorylation, and endothelial nitric oxide synthase phosphorylation. We used D2DR knockout mice to confirm that dopamine acts through D2DR to block vascular permeability in our lung injury model. As expected, a D2DR agonist failed to reduce pulmonary edema in D2DR−/− mice. Taken together, our results suggest that dopamine acts through D2DR to inhibit pulmonary edema-associated vascular permeability, which is mediated through VEGF-VEGFR2 signaling and conveys protective effects in an ALI model.
A Lipid-Modified Estrogen Derivative that Treats Breast Cancer Independent of Estrogen Receptor Expression through Simultaneous Induction of Autophagy and Apoptosis
Roy, Sayantani , Reddy, Bathula Surendar , Pal, Krishnendu , Sudhakar, Godeshala, Dutta, Shamit K., Wang, Enfeng , Vohra, Pawan K., Roy, Karnati R., Banerjee‬‬‬‬‬‬‬‬‬, Rintu , Godeshala, Sudhakar , Sinha, Sutapa , Iyer, Seethalakshmi , Reddanna, Pallu , Mukhopadhyay, Debabrata , Pal, Krishnendu , Banerjee, Rajkumar

Molecular Cancer Research | February 2, 2011 | Volume: 9 | Issue: 3 | Pages: 364-374

10.1158/1541-7786.mcr-10-0526 Get It

Abstract It is a challenge to develop a universal single drug that can treat breast cancer at single- or multiple-stage complications, yet remains nontoxic to normal cells. The challenge is even greater when breast cancer–specific, estrogen-based drugs are being developed that cannot act against multistaged breast cancer complications owing to the cells differential estrogen receptor (ER) expression status and their possession of drug-resistant and metastatic phenotypes. We report here the development of a first cationic lipid-conjugated estrogenic derivative (ESC8) that kills breast cancer cells independent of their ER expression status. This ESC8 molecule apparently is nontoxic to normal breast epithelial cells, as well as to other noncancer cells. ESC8 induces apoptosis through an intrinsic pathway in ER-negative MDA-MB-231 cells. In addition, ESC8 treatment induces autophagy in these cells by interfering with the mTOR activity. This is the first example of an estrogen structure–based molecule that coinduces apoptosis and autophagy in breast cancer cells. Further in vivo study confirms the role of this molecule in tumor regression. Together, our results open new perspective of breast cancer chemotherapy through a single agent, which could provide the therapeutic benefit across all stages of breast cancer. Mol Cancer Res; 9(3); 364–74. ©2011 AACR.
RGS-GAIP–Interacting Protein Controls Breast Cancer Progression
Wang, Ling , Lau, Julie S., Patra, Chitta Ranjan , Cao, Ying , Dutta, Shamit K., Nandy, Debashis, Wang, Enfeng , Rupasinghe, Chamila N., Vohra, Pawan K., Spaller, Mark R., Bhattacharya, Santanu , Mukhopadhyay, Debabrata

Molecular Cancer Research | October 28, 2010 | Volume: 8 | Issue: 12 | Pages: 1591-1600

10.1158/1541-7786.mcr-10-0209 Get It

Abstract Although the importance of RGS-GAIP–interacting protein (GIPC) in the biology of malignant cells is well known, the molecular mechanism of GIPC in the inhibition of tumor progression has not been identified. This study focused on elucidating the molecular role of GIPC in breast cancer progression. By using a human breast tumor specimen, an in vivo mouse model, and breast cancer cell lines, we showed for the first time that GIPC is involved in breast cancer progression through regulation of breast cancer cell proliferation, survival, and invasion. Furthermore, we found that the Akt/Mdm2/p53 axis, insulin-like growth factor-1 receptor, matrix metalloproteinase-9, and Cdc42 were downstream of GIPC signaling in breast cancer cells. Moreover, we showed that wild-type p53 reduced GIPC-induced breast cancer cell survival, whereas mutant p53 inhibited GIPC-induced cell invasion. Finally, we demonstrated that an N-myristoylated GIPC peptide (CR1023, N-myristoyl-PSQSSSEA) capable of blocking the PDZ domain of GIPC successfully inhibited MDA-MB-231 cell proliferation, survival, and further in vivo tumor growth. Taken together, these findings demonstrate the importance of GIPC in breast tumor progression, which has a potentially significant impact on the development of therapies against many common cancers expressing GIPC, including breast and renal cancer. Mol Cancer Res; 8(12); 1591–600. ©2010 AACR.
Dopamine regulates phosphorylation of VEGF receptor 2 by engaging Src-homology-2-domain-containing protein tyrosine phosphatase 2
Vohra, Pawan K., Dutta, Shamit K., Sinha, Shirshendu , Sinha, Sutapa , Bhattacharya, Resham , Mukhopadhyay, Debabrata

Journal of Cell Science | August 26, 2009 | Volume: 122 | Issue: 18 | Pages: 3385-3392

10.1242/jcs.053124 Get It

Vascular endothelial growth factor (VEGF)-induced receptor phosphorylation is the crucial step for initiating downstream signaling pathways that lead to angiogenesis or related pathophysiological outcomes. Our previous studies have shown that the neurotransmitter dopamine could inhibit VEGF-induced phosphorylation of VEGF receptor 2 (VEGFR-2), endothelial cell proliferation, migration, microvascular permeability, and thus, angiogenesis. In this study, we address the mechanism by which VEGFR-2 phosphorylation is regulated by dopamine. Here, we demonstrate that D2 dopamine receptor (D2DR) colocalizes with VEGFR-2 at the cell surface. Dopamine pretreatment increases the translocation and colocalization of Src-homology-2-domain-containing protein tyrosine phosphatase (SHP-2) with D2DR at the cell surface. Dopamine administration leads to increased VEGF-induced phosphorylation of SHP-2 and this increased phosphorylation parallels the increased phosphatase activity of SHP-2. Active SHP-2 then dephosphorylates VEGFR-2 at Y951, Y996 and Y1059, but not Y1175. We also observe that SHP-2 knockdown impairs the dopamine-regulated inhibition of VEGF-induced phosphorylation of VEGFR-2 and, subsequently, Src phosphorylation and migration. Our data establish a novel role for SHP-2 phosphatase in the dopamine-mediated regulation of VEGFR-2 phosphorylation.
Targeting GIPC/Synectin in Pancreatic Cancer Inhibits Tumor Growth
Muders, Michael H. , Vohra, Pawan K., Dutta, Shamit K., Wang, Enfeng , Ikeda, Yasuhiro , Wang, Xuan , Udugamasooriya, D. Gomika , Rupashinghe, Chamila N., Baretton, Gustavo , Langer, Silke, Datta, Kaustubh , Simons, Michael , Spaller, Mark R., Memić, Adnan , Aust, Daniela Ellen , Mukhopadhyay, Debabrata , Simons, Michael

Clinical Cancer Research | June 15, 2009 | Volume: 15 | Issue: 12 | Pages: 4095-4103

10.1158/1078-0432.ccr-08-2837 Get It

Abstract Purpose: Various studies have shown the importance of the GAIP interacting protein, COOH-terminus (GIPC, also known as Synectin) as a central adaptor molecule in different signaling pathways and as an important mediator of receptor stability. GIPC/Synectin is associated with different growth-promoting receptors such as insulin-like growth factor receptor I (IGF-IR) and integrins. These interactions were mediated through its PDZ domain. GIPC/Synectin has been shown to be overexpressed in pancreatic and breast cancer. The goal of this study was to show the importance of GIPC/Synectin in pancreatic cancer growth and to evaluate a possible therapeutic strategy by using a GIPC-PDZ domain inhibitor. Furthermore, the effect of targeting GIPC on the IGF-I receptor as one of its associated receptors was tested. Experimental Design: The in vivo effects of GIPC/Synectin knockdown were studied after lentiviral transduction of luciferase-expressing pancreatic cancer cells with short hairpin RNA against GIPC/Synectin. Additionally, a GIPC-PDZ–targeting peptide was designed. This peptide was tested for its influence on pancreatic cancer growth in vitro and in vivo. Results: Knockdown of GIPC/Synectin led to a significant inhibition of pancreatic adenocarcinoma growth in an orthotopic mouse model. Additionally, a cell-permeable GIPC-PDZ inhibitor was able to block tumor growth significantly without showing toxicity in a mouse model. Targeting GIPC was accompanied by a significant reduction in IGF-IR expression in pancreatic cancer cells. Conclusions: Our findings show that targeting GIPC/Synectin and its PDZ domain inhibits pancreatic carcinoma growth and is a potential strategy for therapeutic intervention of pancreatic cancer.