Thammanna

@bgsaims.edu.in

Research Scientist, Biochemistry
Adichunchanagiri Institute for Molecular Medicine



              

https://researchid.co/sstgowda.71

EDUCATION

M.Sc, Ph.D

RESEARCH INTERESTS

Biochemistry, Chemical biology, Protein chemistry, Molecular biology, Immuno histochemistry, Cancer biology & so on.

5

Scopus Publications

Scopus Publications

  • Protective Effect of Sundakai (Solanum torvum) Seed Protein (SP) Against Oxidative Membrane Damage in Human Erythrocytes
    M. Sivapriya, S. S. Thammanna Gowda, and Leela Srinivas

    Springer Science and Business Media LLC
    Abstract Lipid peroxidation by ROS at the membrane level disturbs the inherit integrity of components activating subsequent alterations in the function. In this study, the protective effect of purified Sundakai (Solanum torvum) seed protein (SP) was tested against oxidative membrane damage in erythrocyte membrane. SP prevented oxidative RBC lysis induced by pro-oxidants; Fe:As (2:20 μmol), periodate (0.4 mM), and t-BOOH (1 mM) up to 86, 81, and 86 %, respectively. Further, SP prevented the Fe:As-induced K+ leakage up to the tune of 95 %. The inhibition offered by SP on K+ leakage was comparable to inhibition offered by quinine sulfate, a known K+ channel blocker. SP dose dependently restored Na+K+ ATPase and Ca2+Mg2+ ATPase activities in erythrocyte membrane. The restoration of ATPase activity by SP was two times more than standard antioxidants BHA and α-tocopherol. Besides, SP at 1.6 μmol restored the membrane proteins over Fe:As induction when analyzed by SDS-PAGE, which was comparable to protection offered by BHA. In conclusion, SP is an effective antioxidant in preventing oxidative membrane damage and associated functions mediated by ROS. As SP is non-toxic, it can be used as an effective bioprotective antioxidant agent to cellular components.

  • Antibacterial activity of different extracts of Sundakai (Solanum torvum) fruit coat
    M. Sivapriya, R. Dinesha, R. Harsha, S.S.T. Gowda, and L. Srinivas

    Science Alert

  • Lectindb: A plant lectin database
    Nagasuma R. Chandra, Nirmal Kumar, Justin Jeyakani, Desh Deepak Singh, Sharan B. Gowda, and M. N. Prathima

    Oxford University Press (OUP)
    Lectins, a class of carbohydrate-binding proteins, are now widely recognized to play a range of crucial roles in many cell-cell recognition events triggering several important cellular processes. They encompass different members that are diverse in their sequences, structures, binding site architectures, quaternary structures, carbohydrate affinities, and specificities as well as their larger biological roles and potential applications. It is not surprising, therefore, that the vast amount of experimental data on lectins available in the literature is so diverse, that it becomes difficult and time consuming, if not impossible to comprehend the advances in various areas and obtain the maximum benefit. To achieve an effective use of all the data toward understanding the function and their possible applications, an organization of these seemingly independent data into a common framework is essential. An integrated knowledge base ( Lectindb, http://nscdb.bic.physics.iisc.ernet.in ) together with appropriate analytical tools has therefore been developed initially for plant lectins by collating and integrating diverse data. The database has been implemented using MySQL on a Linux platform and web-enabled using PERL-CGI and Java tools. Data for each lectin pertain to taxonomic, biochemical, domain architecture, molecular sequence, and structural details as well as carbohydrate and hence blood group specificities. Extensive links have also been provided for relevant bioinformatics resources and analytical tools. Availability of diverse data integrated into a common framework is expected to be of high value not only for basic studies in lectin biology but also for basic studies in pursuing several applications in biotechnology, immunology, and clinical practice, using these molecules.

  • Smoke treatment triggers the release of a novel DNA damaging factor by lymphocytes
    Raghavendra Pralhada Rao, S. S. Thammanna Gowda, and Srinivas Leela

    Springer Science and Business Media LLC
    AbstactOrganic fuel smoke is a hazardous agent, which pushes the cells towards“prooxidant state'', leading to 4,46,400 strand breaks/cell/day as against 47,000 strand breaks/cell/day produced by constitutive oxygen radicals. This prooxidants scenario switches on a plethora of intercellular events. Here we report a novel DNA damaging factor released by lymphocytes, upon treatment with smoke condensate. Human lymphocytes, when exposed to cow dung cake smoke condensate, were found to release a low molecular weight factor into the media at 20 min of exposure. The conditioned media, displayed a propensity of inducing DNA damage in fresh, normal lymphocytes, which were not exposed to any damaging agent. The above DNA damaging effect of the conditioned media was not due to any residual presence of Polycyclic Aromatic Hydrocarbons, which were present in the smoke. The release of this factor was in correlation with the DNA damaging event, taking place in the cells. This secondary DNA damaging factor had a molecular weight less than 5 kd. The factor had the cell death inducing propensity when allowed to act on lymphocytes

  • A database analysis of jacalin-like lectins: Sequence-structure-function relationships
    S. Raval

    Oxford University Press (OUP)
    Lectins are known to be important for many biological processes, due to their ability to recognize cell surface carbohydrates with high specificity. Plant lectins have been model systems to study protein-carbohydrate recognition, because individually they exhibit high sensitivity and as a group large diversity in recognizing carbohydrate structures. Although extensive studies have been carried out for legume lectins that have led to interesting insights into the sequence determinants of sugar recognition in them, frameworks with such specific correlations are not available for other plant lectin families. This study reports a large-scale data acquisition and extensive analysis of sequences and structures of beta-prism-I or jacalin-related lectins (JRLs) and shows that hypervariability in the binding site loops generates carbohydrate recognition diversity, a strategy analogous to that in legume lectins. Analyses of the size, conformation, and sequence variability in key regions reveal the existence of a common theme, encoded as a set of structural features over a common scaffold, in defining specificity. This study also points to the remarkable range of domain architectures, often arising out of gene duplication events in lectins of this family. The data analyzed here also indicate a spectacular variety of quaternary associations possible in this family of lectins that have implications for glycan recognition. These results thus provide sequence-structure-function correlations, an understanding of the molecular basis of carbohydrate recognition by beta-prism-I lectins, and also a rationale for engineering specific recognition capabilities in relevant molecules.

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