School of Life Sciences
Jawaharlal Nehru University
New Delhi -110067, India.
Room No.      : 220, 217
Off. Phone    : 26704115
Residence     : 26197230
E-mail :


  1. Ph.D., Biochemistry (1979-1984), University of Calcutta.
  2. M.Sc., Biochemistry (1976-1978), University of Calcutta.


  1. Professor, School of Life Sciences, Jawaharlal Nehru University (2006-).
  2. Associate Professor, School of Life Sciences, Jawaharlal Nehru University (1998-2006).
  3. Research Assistant Professor, Department of Anatomy and Cell Biology, State University of New York-Health Science Centre at Brooklyn, New York, USA (1993-1998).
  4. Research Instructor, Department of Anatomy and Cell Biology, State University of New York Health Science Center at Brooklyn, New York, USA (1990-1992).
  5. Post Doctoral Research Associate, Department of Microbiology and Immunology, State University of New York Health Science Centre at Brooklyn, New York, USA (1986-1989).
  6. Senior Research Fellow, Department of Biochemistry, University of Calcutta, India (1982-85).
  7. Junior Research Fellow, Department of Biochemistry, University of Calcutta, India (1979-81).

Area of Research

  1. Cell signaling and Gene Expression in Cardiovascular System.
  2. Transcription Control of Cardiovascular Development and Diseases.
  3. Redox biology of cardiovascular diseases.

Research Funding

  1. Development of a database on transcription factor binding sites from developing chick heart, CSIR, 1999-2003.
  2. Role of AP-1 and its associate proteins in cardiac muscle gene expression, DBT, 2000- 2003.
  3. Identification of Novel Gene Expression Pathways in Cardiac Diseases, UGC-UPOE, 2002-2007.
  4. Identification and characterization of novel transcriptional regulators from developing heart, CSIR, 2004-2006.
  5. Biochemical and Molecular Analysis of Redox Signaling in Cardiac Myocytes under Adrenergic Stress, DBT, 2007-2010
  6. Identification and Functional Characterization of the Splice Variants of the Tumor Antigen SG2NA, DBT, 2007-2011.
  7. Indo-US Joint Centre for cardiovascular Biology, Indo-US Science and Technology Forum, 2010-2011.
  8. Analysis of intracellular redox dynamics in H9C2 cardiac myoblasts under adrenergic stress: a tool for studying the biology of heart failure. CSIR, 2011-2014.
  9. The role of SG2NA in Tissue Differentiation during Chick Development, DST, 2011-2013.
  10. Proteomic and transcriptomic evaluation of the anti-hypertrophic and -heart failure properties of Terminali. arjuna extract, Pending with DST, 2013-2016.
  11. Mapping the redox-kinase pathway activating fosB and fra-1 expression in cardiac myocytes under adrenergic stress, DBT, 2013-2016.
  12. Analysis of cross-talk between adrenergic and NOX Signaling in Cardiac Muscle, DST, 2017-2020

 Research Details

  1. Analysis of cross-talk between adrenergic and NOX Signaling in Cardiac Muscle

    Cellular redox system has key roles in cell functions like cell division, cell-cell communication, signaling and gene expression. At the organismal level, reactive oxygen species (ROS) has long been attributed to both physiological processes like embryonic development, immune response, growth factor signaling etc, as well as pathological responses like tumorigenesis, neurological and metabolic disorders etc. Among the various sources of cellular ROS, NADPH oxidase family (Nox family) has emerged as a major player in cell/tissue function in past ten years. Nox enzymes are low abundant and function as redox-modulators. Nox-derived ROS regulate cellular responses like growth factor signaling and the onset and control of pathological conditions. The role of Nox derived ROS in the cardiovascular system has drawn considerable attention in the past decade.

    We have been investigating the role of ROS in modulating adrenergic signaling in cardiac myocytes. Based on our previous publications (Gupta et al., 2006; Jindal et al., 2011), we had hypothesized that upon stimulation of adrenergic receptors; cardiac myoblasts generate multiple reactive oxygen/nitrogen species (RO/NS). Thereafter, we had demonstrated that dynamic regulation of RO/NS in norepinephrine (NE) treated cardiac myoblasts ultimately determines its fates viz., hypertrophy or apoptosis two essential arms of heart failure (Thakur et al, 2015).

    Our subsequent study (details given in the preliminary results) suggests that ROS generated upon stimulation of adrenergic receptors create a feedback loop regulating ß-adrenergic receptor (ß-AR) phosphorylation-internalization-degradation or dephosphorylation, two key modulators of receptor desensitization in heart failure patients. Such role of ROS in ß-AR sensitization/desensitization is novel and has not been reported by any other group till date.

    Our preliminary studies also suggest that the detrimental effects of ROS on ßAR function is more due to the alteration of redox network than increased generation of certain reactive species. A better understanding of modulation of ß-AR function by ROS will therefore enhance our understanding of the redox biology of ß adrenergic receptor function. Based upon this overall hypothesis, we would like to investigate specific role(s) of ROS in ß-AR desentization-resensitization pathway. We also would like to investigate the mechanisms of modulation of ß-AR function by ROS . 

  1. Functional characterization of SG2NA variants.

    Striatin, SG2NA, and zinedin constitute a three-member subfamily of WD-40 repeat protein superfamily, with striatin as the prototype. Apart from WD-40 repeats, they have a caveolin-binding motif, a coiled-coil structure, and a calmodulin-binding domain. They also share a number of smaller motifs, suggesting a conservation of function(s). In agreement, supramolecular signalling complex(s) named STRIPAK (Striatin-interacting phosphatase and kinase) assembled around striatin and containing both kinases and phosphatises have been described. Recent studies suggest that STRIPAK complexes regulate several nodal signaling pathways involved in cell proliferation, differentiation, polarity, apoptosis and metabolism. Impairment in its function has been linked with diseases like autism, cancer, diabetes, cerebral cavernous malformation etc. 

    SG2NA, the second member of the family, was first characterised as an autoantigen from a cancer patient. Subsequent studies suggested that it is a nuclear protein/antigen with increased expression during S & G2 phases of cell cycle and named accordingly. We have demonstrated that it has at least six isoforms generated by alternative splicing and RNA editing. These variants are differentially expressed in mouse tissues and cultured cells. Variants of SG2NA have similar but distinctive structural characteristics and are likely to have related functions. Because of extensive conservation of various sequence motifs, variants of SG2NA are expected to have overlapping but distinct function. Down regulation of SG2NA by shRNA makes Neuro 2A cells more susceptible to oxidative stress but specific contribution by each variant are yet to be determined.

    Till date, a wide range of cellular events have been linked to striatin and SG2NA. They act as a subtype of the B subunit of serine/threonine phosphatase PP2A, determining its specificity & subcellular localization. PP2A counteracts the CDK-dependent phosphorylation of cell cycle proteins throughout cell division. Another interacting partner of SG2NA is CTTNBP2 that is involved in microtubule stability and dendritic spinogenesis. The WD-40 repeat domain of Striatin/SG2NA is involved in their interaction with several other proteins like Mob3 involved in membrane trafficking, adenomatous polyposis coli, regulating tight junctions and CCT/TRiC, a chaperonin.

    We recently have demonstrated that the expression of SG2NA is modulated during cell cycle while over- or under expression of SG2NA alters the duration of phases. Also, the stability of SG2NA is regulated by its phosphorylation by GSK3ß and ERK, while SG2NA in turn controls the levels of these kinases. Therefore, a precisely controlled feedback-feed forward mechanism integrating the kinase-phosphate signalling involving SG2NA regulates certain aspects of cell cycle progression.

Selected Publications:

  1. Buddhi P Jain, Shweta Pandey, Nikhat Saleem, Goutam K Tanti, Shalini Mishra, Shyamal K Goswami; SG2NA is a regulator of Endoplasmic Reticulum (ER) homeostasis as its depletion leads to ER stress; Cell Stress and Chaperone (in Press)
  2. Nikhat Saleem, Shyamal K Goswami; Activation of adrenergic receptor in H9c2 cardiac myoblasts co-stimulates Nox2 and the derived ROS mediate the downstream responses; Molecular and Cellular Biochemistry
  3. Santosh Kumar, Pankaj Prabhakar, Subir K. Maulik, Manish Sharma, Shyamal K. Goswami; Proteomic analysis of the protective effects of aqueous bark extract of terminalia arjuna (Roxb.) on isoproterenol-induced cardiac hypertrophy in rats, J. Ethnopharmacol. 2017;198: 98-108.
  4. Anita Thakur, Md. Jahangir Alam, Ajayakumar MR, Saroj Ghaskadbi, Manish Sharma and Shyamal K. Goswami, Norepinephrine-Induced Apoptotic And Hypertrophic Responses In H9c2 Cardiac Myoblasts are Characterized by Different Repertoire of Reactive Oxygen Species Generation, Redox Biology, Redox Biol. 2015 Aug;5:243-52.
  5. Goutam Kumar Tanti, Shweta Pandey, Shyamal K Goswami. SG2NA enhances cancer cell survival by stabilizing DJ-1 and thus activating Akt, Biochem Biophys Res Commun. 2015 Aug 7;463(4):524-31
  6. Jain BP, Chauhan P, Tanti GK, Singarapu N, Ghaskadbi S, Goswami SK.Tissue specific expression of SG2NA is regulated by differential splicing, RNA editing and differential polyadenylation. Gene. 2015 Feb 10;556 (2):119-26.
  7. Tanti GK, Goswami SK, SG2NA recruits DJ-1 and Akt into the mitochondria and membrane to protect cells from oxidative damage. Free Radic Biol Med. 2014 Oct; 75:1-13.
  8. Sangeeta Soni, Chetna Tyagi, Abhinav Grover and Shyamal K Goswami, Molecular modeling and molecular dynamics simulations based structural analysis of the SG2NA protein variants, BMC Research Notes, 2014 Jul 11;7:446.
  9. Tanti GK, Singarapu N, Muthuswami R, Goswami SK, Among the three striatin family members, SG2NA was first to arise during evolution, Front Biosci (Schol Ed). 2014 Jan 1; 6:1-15.
  10. Dutta P, Tanti GK, Sharma S, Goswami SK, Komath SS, Mayo MW, Hockensmith JW, Muthuswami R.Global epigenetic changes induced by SWI2/SNF2 inhibitors characterize neomycin-resistant mammalian cells. PLoS One. 2012; 7(11):e49822.
  11. Jindal E, Goswami S K, Norepinephrine Regulates fosB and fra-1 by Distinctive Redox signals in H9c2 Cardiac Myoblasts, Free Radical Biology and Medicine, 2011; 51(8):1512-21.
  12. Paila YD, Jindal E, Goswami SK, Chattopadhyay A. Cholesterol depletion enhances adrenergic signaling in cardiac myocytes, Biochim Biophys Acta. 2011; 1808:461-465.
  13. Mukherjee S, Lekli I, Goswami S, Das DK. Freshly crushed garlic is a superior cardioprotective agent than processed garlic. J Agric Food Chem. 2009; 57:7137-44.
  14. Goswami SK, Das DK., Resveratrol and chemoprevention, Cancer Lett. 2009; 284:1-6.
  15. Gurusamy N, Goswami S, Malik G, Das DK., Oxidative injury induces selective rather than global inhibition of proteasomal activity. J Mol Cell Cardiol. 2008; 44(2):419-28.
  16. Sanghamitra M, Talukder I, Singarapu N, Sindhu KV, Kateriya S, Goswami S.K. WD-40 repeat protein SG2NA has multiple splice variants with tissue restricted and growth responsive properties.Gene. 2008 May 6.
  17. Gurusamy N, Goswami S.K., Malik G, Das DK. Oxidative injury induces selective rather than global inhibition of proteasomal activity. J Mol Cell Cardiol. 2008 Feb; 44(2): 419-428.
  18. Gupta MK, Neelakantan TV, Sanghamitra M, Tyagi RK, Dinda A, Maulik S, Mukhopadhyay CK, Goswami S.K. An assessment of the role of reactive oxygen species and redox signaling in norepinephrine-induced apoptosis and hypertrophy of H9c2 cardiac myoblasts. Antioxid Redox Signal. 2006 May-Jun; 8(5-6): 1081-1093.
  19. Goswami, S.K., (2004) ‘Molecular Biology’ in ‘Biotechnology’ edited by Prof H K Das and published by Wiley DreamTech, India.
  20. Karnani, N., Gaur, N.A., Jha, S., Puri, N., Krishnamurthy, S., Goswami, S.K., Mukhopadhyay, G., and Prasad, R., (2004) SRE1 and SRE2 are two specific steroid-responsive modules of Candida drug resistance gene 1 (CDR1) promoter. Yeast21219-39.
  21. Gaur, N.A., Puri, N., Karnani, N., Mukhopadhyay, G., Goswami, S.K.and Prasad, R., (2004). Identification of a negative regulatory element, which regulates basal transcription of a multidrug resistance gene CDR1 of Candida albicans. FEMS Yeast Res4389-99.
  22. Sindhu, K.V., Rani, V., Gupta, M.K., Ghaskadbi, S., Choudhury, D., and Goswami, S.K., (2004). Isolation of a library of   target-sites for sequence specific DNA binding proteins from chick embryonic heart: a potential tool for identifying novel transcriptional regulators involved in embryonic development. BiochemBiophys Res Commun., 323912-9.
  23. Meenakshi, J., Anupama, Goswami, S.K., and Datta, K., (2003). Constitutive expression of hyaluronan binding protein 1 (HABP1/p32/gC1qR) in normal fibroblast cells perturbs its growth characteristics and induces apoptosis. BiochemBiophys Res Commun., 300686-93.
  24. Majumdar, M., Meenakshi, J., Goswami, S.K., and Datta, K., (2002). Hyaluronan binding protein 1 (HABP1)/C1QBP/p32 is an endogenous substrate for MAP kinase and is translocated to the nucleus upon mitogenic stimulation. BiochemBiophys Res Commun. , 291829-37.
  25. Nijhara R, Jana SS, Goswami SK, Rana A, Majumdar SS, Kumar V, Sarkar DP (2001). Sustained activation of mitogen-activated protein kinases and activator protein 1 by the hepatitis B virus X protein in mouse hepatocytes in vivo. J Virol. Nov; 75(21):10348-58.
  26. Nijhara R, Jana SS, Goswami SK, Kumar V, Sarkar DP (2001). An internal segment (residues 58-119) of the hepatitis B virus X protein is sufficient to activate MAP kinase pathways in mouse liver. FEBS Lett. Aug 24; 504(1-2):59-64.
  27. Goswami SK, Shafiq S, Siddiqui MA., (2001) Modulation of MLC-2v gene expression by AP-1: complex regulatory role of Jun in cardiac myocytes. Mol Cell Biochem. Jan; 217(1-2):13-20.
  28. Ghatpande S, Goswami S, Mathew S, Rong G, Cai L, Shafiq S, Siddiqui MA., (1999) Identification of a novel cardiac lineage-associated protein (cCLP-1): A candidate regulator of cardiogenesis.Dev Biol. Apr 1; 208 (1):210-21.
  29. Maulik N, Goswami S, Galang N, Das DK., (1999)Differential regulation of Bcl-2, AP-1 and NF-kappaB on cardiomyocyte apoptosis during myocardial ischemic stress adaptation. FEBS Lett. Jan 29; 443(3):331-6.
  30. Ghatpande S, Goswami S, Mascareno E, Siddiqui MA. Signal transduction and transcriptional adaptation in embryonic heart development and during myocardial hypertrophy. Mol Cell Biochem. 1999 Jun; 196(1-2):93-7.
  31. Goswami SK, Siddiqui MA. Molecular basis of cardiocyte cell specification. Ann N Y Acad Sci. 1996 Sep 30; 793:259-66. Review.
  32. Alam M, Vaynblat M, Goswami SK, Baig MM, Grijalva G, Chiavarelli M, Zisbrod Z, Jacobowitz IJ, Cheng W, Stein RA, Siddiqui MA. Activation of creatine kinase-B and phospholamban gene expression in transformed latissimusdorsi muscle: evaluation of mRNA by polymerase chain reaction.J Mol Cell Cardiol1996 Sep; 28(9):1901-10.
  33. Goswami SK, Siddiqui MA. Transactivation of cardiac MLC-2 promoter by MyoD in 10T1/2 fibroblast cells is independent of E-box requirement but depends upon new proteins that recognize MEF-2 site. Cell Mol Biol Res1995; 41(3):199-205.
  34. Goswami S, Qasba P, Ghatpande S, Carleton S, Deshpande AK, Baig M, Siddiqui MA. Differential expression of the myocyte enhancer factor 2 family of transcription factors in development: the cardiac factor BBF-1 is an early marker for cardiogenesis. Mol Cell Biol1994 Aug; 14 (8):5130-8.
  35. Zhou MD, Goswami SK, Martin ME, Siddiqui MA. A new serum-responsive, cardiac tissue-specific transcription factor that recognizes the MEF-2 site in the myosin light chain-2 promoter. Mol Cell Biol. 1993 Feb; 13(2):1222-31.
  36. Goswami SK, Zhao YY, Siddiqui MA, Kumar A. MyoD transactivates angiotensinogen promoter in fibroblast C3H10T1/2 cells. Cell Mol Biol Res1993; 39(2):125-30.
  37. Goswami SK, Zarraga AM, Martin ME, Morgenstern D, Siddiqui MA. fos-mediated repression of cardiac myosin light chain-2 gene transcription. Cell Mol Biol1992 Feb; 38(1):49-58.
  38. Bablanian R, Goswami SK, Esteban M, Banerjee AK, Merrick WC. Mechanism of selective translation of vaccinia virus mRNAs: differential role of poly (A) and initiation factors in the translation of viral and cellular mRNAs. J Virol1991 Aug; 65(8):4449-60.
  39. Shen RA, Goswami SK, Mascareno E, Kumar A, Siddiqui MA. Tissue-specific transcription of the cardiac myosin light-chain 2 gene is regulated by an upstream repressor element. Mol Cell Biol.1991 Mar; 11(3):1676-85.
  40. Bablanian R, Goswami SK, Esteban M, Banerjee AK. Selective inhibition of protein synthesis by synthetic and vaccinia virus-core synthesized poly (riboadenylic acids). Virology. 1987 Dec;161(2):366-73.

Student’s Profile:

Former Students:

  1. Sindhu K V (2004): Identification and Characterization of Stage/Tissue Restricted Putative Transcription Factor(s) from Developing Chick Heart.
    Present address: Department of Biochemistry, Delhi University South Campus.

  2. Vibha Rani (2004):Isolation and Characterization of Novel Transcription Factor Target Sites and Their Cognate Factors from Chick Embryonic Heart.
    Present address: Department of Biotechnology at Jaypee Institute of Information Technology

  3. Neelkantan TV (2005): Role of AP-1 and its Associated Proteins in Cardiac Muscle Gene Expression.
    Present address: Molecular cardiology, Cleveland Clinic Foundation, Cleveland, USA.

  4. Manveen K Gupta (2005): Biochemical and Molecular Analysis of Norepinephrine Mediated Apoptosis in H9c2 Cardiac Myoblasts.
    Present address: Molecular cardiology, Cleveland Clinic Foundation, Cleveland, USA.

  5. Sanghamitra Mishra (2007): An Assessment of the Role of SG2NA and FosB in hypertrophy of H9c2 cardiac myoblasts.
    Present address:National institute of Health, Bethesda, USA.

  6. Nandini Singarapu (2008):Analysis of the Regulation of Vigilin and SG2NA during Chick Cardiac Development
    Present address: MD Anderson Cancer Centre, Texas, USA.

  7. Anita Thakur (2010): Elucidation of the Mechanism(s) of Redox signaling Leading to Cardiac Hypertrophy and Apoptosis Under Adrenergic Stress.
    Present Address: Technion - Israel Institute of Technology, Haifa, Israel

  8. Ekta Jindal (submitted in 2011): Biochemical and Molecular Analysis of Redox Signaling in Cardiac Myocytes under Adrenergic Stress.
    Present Address: The Mount Sinai Hospital, New York

  9. Indrani Talukder (submitted in 2011): Functional Characterization of SG2NA variants in cell proliferation and differentiation.

  10. Pooja Chauhan (2006): Characterization of Variants of mouse SG2NA.

  11. Goutam K Tanti (2007): Functional Characterization of SG2NA Variants and DJ-1: Implications in Cancer and Neurodegenerative Diseases.
    Present address: Technische Universität München, Munich

  12. Santosh Kumar (2007): Analysis of adrenergic signaling in cardiac myocytes and assessing the effect of Tarminalia arujuna

  13. Sangeeta Soni (2008): Biophysical characterization of SG2NA variants.

  14. Md. Jahangir Alam (2009): Analysis of Intracellular Redox Dynamics in H9c2 Cardiac Myoblasts under Adrenergic Stress.

  15. Buddhi P Jain (2011), Regulation of Expression of Variants of SG2NA and its Associated Kinase Network.

Present Students:

  1. Nikhat Saleem (2010): Redox Biology of Heart Failure.
  2. Shweta Pandey (2010): Biochemical and Cell Biological Characterization of SG2NA Variants
  3. Anamika: Redox signalling in heart failure.
  4. Richa Gupta: Characterization of variants of SG2NA
  5. Padmini Bishoyi: Role of SG2NA in cancer development.