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  1. Article ; Online: Daboialipase, a phospholipase A

    Kolvekar, Nivedita / Bhattacharya, Navodipa / Mondal, Sukanta / Sarkar, Angshuman / Chakrabarty, Dibakar

    Toxicon : official journal of the International Society on Toxinology

    2024  Volume 239, Page(s) 107632

    Abstract: Snake venoms are known to contain toxins capable of interfering with normal physiological processes of victims. Specificity of toxins from snake venoms give scope to identify new molecules with therapeutic action and/or help to understand different ... ...

    Abstract Snake venoms are known to contain toxins capable of interfering with normal physiological processes of victims. Specificity of toxins from snake venoms give scope to identify new molecules with therapeutic action and/or help to understand different cellular mechanisms. Russell's viper venom (RVV) is a mixture of many bioactive molecules with enzymatic and non-enzymatic proteins. The present article describes Daboialipase (DLP), an enzymatic phospholipase A
    MeSH term(s) Animals ; Humans ; Anticoagulants/chemistry ; Anticoagulants/isolation & purification ; Anticoagulants/pharmacology ; Phospholipases A2/chemistry ; Phospholipases A2/isolation & purification ; Phospholipases A2/pharmacology ; Thrombin/antagonists & inhibitors ; Viper Venoms/chemistry ; Vipera ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/isolation & purification ; Antineoplastic Agents/pharmacology
    Chemical Substances Anticoagulants ; Phospholipases A2 (EC 3.1.1.4) ; Thrombin (EC 3.4.21.5) ; Viper Venoms ; Antineoplastic Agents
    Language English
    Publishing date 2024-02-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2024.107632
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Biological activities of Vipegrin, an anti-adhesive Kunitz-type serine proteinase inhibitor purified from Russell's viper venom.

    Bhattacharya, Navodipa / Kolvekar, Nivedita / Mondal, Sukanta / Sarkar, Angshuman / Chakrabarty, Dibakar

    Toxicon : official journal of the International Society on Toxinology

    2023  Volume 232, Page(s) 107213

    Abstract: Vipegrin is a 6.8 kDa Kunitz-type serine proteinase inhibitor purified from Russell's viper (Vipera russelii russelii) venom. Kunitz-type serine proteinase inhibitors are non-enzymatic proteins and are ubiquitous constituents of viper venoms. Vipegrin ... ...

    Abstract Vipegrin is a 6.8 kDa Kunitz-type serine proteinase inhibitor purified from Russell's viper (Vipera russelii russelii) venom. Kunitz-type serine proteinase inhibitors are non-enzymatic proteins and are ubiquitous constituents of viper venoms. Vipegrin could significantly inhibit the catalytic activity of trypsin. It also posseses disintegrin-like properties and could inhibit collagen and ADP-induced platelet aggregation in a dose-dependent manner. Vipegrin is cytotoxic to MCF7 human breast cancer cells and restricts its invasive property. Confocal microscopic analysis revealed that Vipegrin could induce apoptosis in MCF7 cells. Vipegrin disrupts cell to cell adhesion of MCF7 cells through its disintegrin-like activity. It also causes disruption of attachment of MCF7 cells to synthetic (poly L-lysine) and natural (fibronectin, laminin) matrices. Vipegrin did not cause cytotoxicity on non-cancerous HaCaT, human keratinocytes. The observed properties indicate that Vipegrin may help the development of a potent anti-cancer drug in future.
    MeSH term(s) Animals ; Humans ; Serine Proteinase Inhibitors/pharmacology ; Viper Venoms ; Disintegrins ; Platelet Aggregation ; Daboia/metabolism
    Chemical Substances Serine Proteinase Inhibitors ; Viper Venoms ; Disintegrins
    Language English
    Publishing date 2023-07-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2023.107213
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: How snake venom disintegrins affect platelet aggregation and cancer proliferation.

    Kolvekar, Nivedita / Bhattacharya, Navodipa / Sarkar, Angshuman / Chakrabarty, Dibakar

    Toxicon : official journal of the International Society on Toxinology

    2022  Volume 221, Page(s) 106982

    Abstract: Disintegrins are small peptides possessing a tripeptide motif capable of binding to integrins. These were first isolated from viper venoms and are now also found in many other hematophagous organisms. Many integrins have been studied for their role in ... ...

    Abstract Disintegrins are small peptides possessing a tripeptide motif capable of binding to integrins. These were first isolated from viper venoms and are now also found in many other hematophagous organisms. Many integrins have been studied for their role in the onset of disease and the interaction of disintegrins with these receptors makes them potential therapeutic molecules. Disintegrins are also used as molecular scaffolds to design effective drugs for cardiovascular diseases and cancer. Even the gene and protein sequencing data of disintegrins have provided insights into understanding the molecular complexity of disintegrins. In this review, we try to summarize the structural and functional importance of disintegrins in identifying the biological targets and triggering various signaling pathways involved in platelet aggregation and cancer. Also, we have tried to elucidate a possible molecular mechanism behind the action of disintegrins on platelet aggregation and cancer. This understanding will help us to design and to explore more of these integrin-binding molecules.
    Language English
    Publishing date 2022-11-23
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2022.106982
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Biological activities of Vipegrin, an anti-adhesive Kunitz-type serine proteinase inhibitor purified from Russell's viper venom

    Bhattacharya, Navodipa / Kolvekar, Nivedita / Mondal, Sukanta / Sarkar, Angshuman / Chakrabarty, Dibakar

    Toxicon. 2023 Aug., v. 232 p.107213-

    2023  

    Abstract: Vipegrin is a 6.8 kDa Kunitz-type serine proteinase inhibitor purified from Russell's viper (Vipera russelii russelii) venom. Kunitz-type serine proteinase inhibitors are non-enzymatic proteins and are ubiquitous constituents of viper venoms. Vipegrin ... ...

    Abstract Vipegrin is a 6.8 kDa Kunitz-type serine proteinase inhibitor purified from Russell's viper (Vipera russelii russelii) venom. Kunitz-type serine proteinase inhibitors are non-enzymatic proteins and are ubiquitous constituents of viper venoms. Vipegrin could significantly inhibit the catalytic activity of trypsin. It also posseses disintegrin-like properties and could inhibit collagen and ADP-induced platelet aggregation in a dose-dependent manner. Vipegrin is cytotoxic to MCF7 human breast cancer cells and restricts its invasive property. Confocal microscopic analysis revealed that Vipegrin could induce apoptosis in MCF7 cells. Vipegrin disrupts cell to cell adhesion of MCF7 cells through its disintegrin-like activity. It also causes disruption of attachment of MCF7 cells to synthetic (poly L-lysine) and natural (fibronectin, laminin) matrices. Vipegrin did not cause cytotoxicity on non-cancerous HaCaT, human keratinocytes. The observed properties indicate that Vipegrin may help the development of a potent anti-cancer drug in future.
    Keywords Daboia russelii ; antineoplastic agents ; apoptosis ; breast neoplasms ; catalytic activity ; cell adhesion ; collagen ; cytotoxicity ; dose response ; fibronectins ; humans ; keratinocytes ; laminin ; lysine ; platelet aggregation ; serine proteinase inhibitors ; trypsin ; viper venoms ; Kunitz-type serine proteinase inhibitor ; Disintegrin ; Cytotoxic ; Anti-Cancer ; Russell's viper venom
    Language English
    Dates of publication 2023-08
    Publishing place Elsevier Ltd
    Document type Article ; Online
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2023.107213
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: SPAD-1, a serine proteinase associated disintegrin from Russell's viper venom disrupts adhesion of MCF7 human breast cancer cells.

    Bhattacharya, Navodipa / Kolvekar, Nivedita / Mondal, Sukanta / Sarkar, Angshuman / Chakrabarty, Dibakar

    Toxicon : official journal of the International Society on Toxinology

    2022  Volume 221, Page(s) 106979

    Abstract: Serine Proteinase Associated Disintegrin-1 (SPAD-1) is a low molecular mass (26 kDa) positively charged protein purified from Russell's viper venom (RVV) possessing cytotoxic activity on MCF7, human breast cancer cells. Primary sequence analysis of the ... ...

    Abstract Serine Proteinase Associated Disintegrin-1 (SPAD-1) is a low molecular mass (26 kDa) positively charged protein purified from Russell's viper venom (RVV) possessing cytotoxic activity on MCF7, human breast cancer cells. Primary sequence analysis of the protein confirms that it is a novel Snake Venom Serine Proteinase (SVSP) and a member of the trypsin family. SPAD-1 contains a conserved triad of Histidine (H), Aspartic acid(D) and Serine(S) residues at its active site for proteinase activity and also an adjacent histidine-glycine-aspartic acid (HGD) disintegrin-like motif. The serine proteinase and disintegrin parts are functionally active and independent. SPAD-1 showed proteolytic digestion of fibrinogen and fibronectin, but laminin digestion was below the detectable limit. Proteolytically inactivated SPAD-1 inhibited collagen and ADP-induced platelet aggregation. This study proposes considering Serine Proteinase Associated Disintegrin (SPAD) as a new group of snake venom proteins. Members of this group contain a serine proteinase catalytic triad and a disintegrin-like motif. SPAD-1 caused visible morphological changes in MCF7 cells, including a reduction of the cell-to-cell attachments, rounding of cell shape and death, in vitro. SPAD-1 also showed a dose-dependent significant decrease in the invasive potency of breast cancer cells. Confocal microscopic analysis revealed the breakage of nuclei of the SPAD-1-treated cells. SPAD-1 also increased cell detachment from the poly L-lysine-coated, laminin-coated and fibronectin-coated culture plate matrices, confirming the disintegrin activity. This study concludes that SPAD-1 may be a good candidate for anti-tumour drug design in the future.
    MeSH term(s) Animals ; Humans ; Female ; Viper Venoms/chemistry ; Daboia ; Disintegrins/pharmacology ; Fibronectins ; Serine Proteases/pharmacology ; MCF-7 Cells ; Laminin ; Histidine ; Aspartic Acid ; Breast Neoplasms
    Chemical Substances Viper Venoms ; Disintegrins ; Fibronectins ; Serine Proteases (EC 3.4.-) ; Laminin ; Histidine (4QD397987E) ; Aspartic Acid (30KYC7MIAI)
    Language English
    Publishing date 2022-11-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 204479-1
    ISSN 1879-3150 ; 0041-0101
    ISSN (online) 1879-3150
    ISSN 0041-0101
    DOI 10.1016/j.toxicon.2022.106979
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Sustaining immunity during starvation in bivalve mollusc: A costly affair.

    Mahapatra, Elizabeth / Dasgupta, Dishari / Bhattacharya, Navodipa / Mitra, Suvrotoa / Banerjee, Debakana / Goswami, Soumita / Ghosh, Nabanita / Dey, Avijit / Chakraborty, Sudipta

    Tissue & cell

    2017  Volume 49, Issue 2 Pt B, Page(s) 239–248

    Abstract: Complete or partial depletion of resource in a freshwater habitat is a common phenomenon. As a consequence, aquatic fauna including bivalve molluscs may be exposed to dietary stress on a seasonal basis. Haemocyte based innate immune profile of the ... ...

    Abstract Complete or partial depletion of resource in a freshwater habitat is a common phenomenon. As a consequence, aquatic fauna including bivalve molluscs may be exposed to dietary stress on a seasonal basis. Haemocyte based innate immune profile of the freshwater mollusc Lamellidens marginalis (Bivalvia: Eulamellibranchiata) was evaluated under starvation induced stress for a maximum period of 32 days in a controlled laboratory condition. During starvation, the bivalve haemocytes maintained a homeostasis in phagocytic efficacy and nitric oxide generation ability with respect to the control. The mollusc maintained a significantly high protein content in its haemolymph and tissues under the nutritional stress with respect to the control. The dietary stress had no significant impact on the activity of digestive tissue derived α-amylase till sixteenth day but by 32 days the enzyme activity went down significantly. The histopathological profile revealed that the bivalve was adapted to maintain a steady immune profile by incurring degeneration of its own tissue structure. The total haemocyte count surged significantly till 16 days but differed insignificantly with respect to the control at 32 days implying probable haematopoietic exhaustion. The study reflects the instinctive urge of the bivalve to maintain immune physiology at heavy metabolic cost under nutrient limited condition.
    MeSH term(s) Animals ; Bivalvia/immunology ; Bivalvia/metabolism ; Fresh Water ; Hemocytes/immunology ; Immunity, Innate ; Nitric Oxide/biosynthesis ; Phagocytosis/immunology ; Starvation ; Stress, Physiological/immunology
    Chemical Substances Nitric Oxide (31C4KY9ESH)
    Language English
    Publishing date 2017-04
    Publishing country Scotland
    Document type Journal Article
    ZDB-ID 204424-9
    ISSN 1532-3072 ; 0040-8166
    ISSN (online) 1532-3072
    ISSN 0040-8166
    DOI 10.1016/j.tice.2017.02.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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