Dr. Manni L Guptasarma
Designation : Professor
Department : IMMUNOPATHOLOGY
guptasarma.manni@pgimer.edu.in

 

 
 :: Contact Details
  Phone No.    :   7087008196
  Ext No.        :   5196
 :: Educational Qualification
  Graduation :   --
  Post Graduation :   M.Sc
  Other Qualification.(1)      :   Ph.D (Biochemistry)
     
 :: Area of Interest
       Area Of Interest       :
Protein misfolding-related diseases; ocular pathology; antibody engineering;  DNA-based (molecular) diagnostics
     
 :: Research & Projects
      Research In
      Progress      
:
Research Projects
1. Understanding the association of Ankylosing Spondylitis (AS) with misfolding of HLA-B27
2. Examination of structural aspects of the intermolecular interactions among crystallins in the lens
3. Establishment of a DNA-based HLA typing laboratory at PGIMER, Chandigarh
4. Modulation of activity of matrix metalloproteases (MMPs) in the extracellular matrix surrounding cultured retinal pigment epithelial (RPE) cells derived from proliferative vitreoretinopathy (PVR) patients
5. Evaluation of Platelet Activation and GPIIb/IIIa Conformational Status in ITP
6. Molecular and morphological monitoring of neuronal transdifferentiation of retinal pigment epithelial cells in culture system by combinations of growth factors
7. Protein engineering-based strategies to target posterior capsular opacification 
      Area Of
      Specialization      
:
Protein Science/Engineering; Biophysics; Cell and Molecular Biology
     
 :: Publications(In Vancouver Style)
1. Sharma,R., Vasishta, R.K.,  Sen, R.K., Luthra-Guptasarma, M. (2007). Refolding of HLA-B27 heavy chains in the absence of 2m yields stable high molecular weight (HMW) protein forms displaying native-like as well as non-native-like conformational features: Implications for autoimmune disease. Biochem. Biophys. Acta (Molecular Basis of Disease) 1772, 1258-1269.
2. Verma, A., Sharma, S., Ganguly, N.K., Majumdar, S., Guptasarma, P., Luthra-Guptasarma, M. (2008). Identification and characterization of a spontaneously aggregating amyloid-forming variant of human PrP(90-231) through phage-display screening of variants randomized between residues 101-112. Int. J. Biochem. Cell Biol. 40, 663-676.
3. Sharma, M., Luthra-Guptasarma, M. (2009) Degradation of proteins upon storage at near-neutral pH : Indications of a proteolytic/gelatinolytic activity associated with aggregates. Biochem. Biophys. Acta : General Subjects 1790, 1282-1294.
4. Luthra-Guptasarma, M., Guptasarma, P. (2010) Metal-catalyzed proteolysis, conformational antigenicity, photosensitized oxidation, and electrical dysfunction explain the pathogenicity of protein aggregates. Medical Hypotheses 75, 294-298.
5. Arora, S.K., Sharma, R., Kaur, G., Bhoria, P., Sharma, M., Luthra-Guptasarma, M. (2010) Towards an indirect screening technique facilitating detection of cellular populations bearing specific cell-surface markers. Biotech Progress 26,1544-1550.
6. Khera, S., Tiwari, A., Srinivasan, R., Gupta, A., Luthra-Guptasarma, M.  (2011) Expression of Granulocyte colony stimulating factor (GCSF) and its receptor by retinal pigment epithelial cells (RPE) : a role in maintaining differentiation-competent state. Current Eye Research 36:469-480.
7. Negi, R., Bhoria, P.,  Pahuja, A., Saikia, B., Varma, N., Malhotra, P., Varma, S., Luthra-Guptasarma, M. (2011) Investigation of the possible association between the HLA antigens and idiopathic thrombocytopenic purpura (ITP). Immunological Investigations (in press)