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  1. Article ; Online: Therapeutic potential of curcumin in gastrointestinal diseases.

    Rajasekaran, Sigrid A

    World journal of gastrointestinal pathophysiology

    2011  Volume 2, Issue 1, Page(s) 1–14

    Abstract: Curcumin, also known as diferuloylmethane, is derived from the plant Curcuma longa and is the active ingredient of the spice turmeric. The therapeutic activities of curcumin for a wide variety of diseases such as diabetes, allergies, arthritis and other ... ...

    Abstract Curcumin, also known as diferuloylmethane, is derived from the plant Curcuma longa and is the active ingredient of the spice turmeric. The therapeutic activities of curcumin for a wide variety of diseases such as diabetes, allergies, arthritis and other chronic and inflammatory diseases have been known for a long time. More recently, curcumin's therapeutic potential for preventing and treating various cancers is being recognized. As curcumin's therapeutic promise is being explored more systematically in various diseases, it has become clear that, due to its increased bioavailability in the gastrointestinal tract, curcumin may be particularly suited to be developed to treat gastrointestinal diseases. This review summarizes some of the current literature of curcumin's anti-inflammatory, anti-oxidant and anti-cancer potential in inflammatory bowel diseases, hepatic fibrosis and gastrointestinal cancers.
    Language English
    Publishing date 2011-01-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2583474-5
    ISSN 2150-5330 ; 2150-5330
    ISSN (online) 2150-5330
    ISSN 2150-5330
    DOI 10.4291/wjgp.v2.i1.1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Therapeutic potential of curcumin in gastrointestinal diseases

    Sigrid A Rajasekaran

    World Journal of Gastrointestinal Pathophysiology, Vol 2, Iss 1, Pp 1-

    2011  Volume 14

    Abstract: Curcumin, also known as diferuloylmethane, is derived from the plant Curcuma longa and is the active ingredient of the spice turmeric. The therapeutic activities of curcumin for a wide variety of diseases such as diabetes, allergies, arthritis and other ... ...

    Abstract Curcumin, also known as diferuloylmethane, is derived from the plant Curcuma longa and is the active ingredient of the spice turmeric. The therapeutic activities of curcumin for a wide variety of diseases such as diabetes, allergies, arthritis and other chronic and inflammatory diseases have been known for a long time. More recently, curcumin’s therapeutic potential for preventing and treating various cancers is being recognized. As curcumin’s therapeutic promise is being explored more systematically in various diseases, it has become clear that, due to its increased bioavailability in the gastrointestinal tract, curcumin may be particularly suited to be developed to treat gastrointestinal diseases. This review summarizes some of the current literature of curcumin’s anti-inflammatory, anti-oxidant and anti-cancer potential in inflammatory bowel diseases, hepatic fibrosis and gastrointestinal cancers.
    Keywords Curcumin ; Inflammation ; Cancer ; Inflammatory bowel disease ; Liver fibrosis ; Gastrointestinal disease ; Apoptosis ; Diseases of the digestive system. Gastroenterology ; RC799-869 ; Specialties of internal medicine ; RC581-951 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Gastroenterology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
    Subject code 610
    Language English
    Publishing date 2011-02-01T00:00:00Z
    Publisher Baishideng Publishing
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Na,K-ATPase and epithelial tight junctions.

    Rajasekaran, Sigrid A / Rajasekaran, Ayyappan K

    Frontiers in bioscience (Landmark edition)

    2009  Volume 14, Issue 6, Page(s) 2130–2148

    Abstract: Tight junctions are unique organelles in polarized epithelial and endothelial cells that regulate the flow of solutes and ions across the epithelial barrier. The structure and functions of tight junctions are regulated by a wide variety of signaling and ... ...

    Abstract Tight junctions are unique organelles in polarized epithelial and endothelial cells that regulate the flow of solutes and ions across the epithelial barrier. The structure and functions of tight junctions are regulated by a wide variety of signaling and molecular mechanisms. Several recent studies in mammals, drosophila, and zebrafish reported a new role for Na,K-ATPase, a well-studied ion transporter, in the modulation of tight junction development, permeability, and polarity. In this review, we have attempted to compile these new reports and suggest a model for a conserved role of Na,K-ATPase in the regulation of tight junction structure and functions.
    MeSH term(s) Humans ; Sodium-Potassium-Exchanging ATPase/metabolism ; Tight Junctions/enzymology
    Chemical Substances Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
    Language English
    Publishing date 2009-01-01
    Publishing country Singapore
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2704569-9
    ISSN 2768-6698 ; 1093-9946
    ISSN (online) 2768-6698
    ISSN 1093-9946
    DOI 10.2741/3367
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Role of Na-K-ATPase in the assembly of tight junctions.

    Rajasekaran, Ayyappan K / Rajasekaran, Sigrid A

    American journal of physiology. Renal physiology

    2003  Volume 285, Issue 3, Page(s) F388–96

    Abstract: Na-K-ATPase, also known as the sodium pump, is a crucial enzyme that regulates intracellular sodium homeostasis in mammalian cells. In epithelial cells Na-K-ATPase function is also involved in the formation of tight junctions through RhoA GTPase and ... ...

    Abstract Na-K-ATPase, also known as the sodium pump, is a crucial enzyme that regulates intracellular sodium homeostasis in mammalian cells. In epithelial cells Na-K-ATPase function is also involved in the formation of tight junctions through RhoA GTPase and stress fibers. In this review, a new two-step model for the assembly of tight junctions is proposed: step 1, an E-cadherin-dependent formation of partial tight junction strands and of the circumferential actin ring; and step 2, active actin polymerization-dependent tethering of tight junction strands to form functional tight junctions, an event requiring normal function of Na-K-ATPase in epithelial cells. A new role for stress fibers in the assembly of tight junctions is proposed. Also, implications of Na-K-ATPase function on tight junction assembly in diseases such as cancer, ischemia, hypomagnesemia, and polycystic kidney disease are discussed.
    MeSH term(s) Animals ; Cadherins/metabolism ; Disease ; Humans ; Mitogen-Activated Protein Kinases/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism ; Stress Fibers/metabolism ; Tight Junctions/chemistry ; Tight Junctions/enzymology ; Tight Junctions/metabolism
    Chemical Substances Cadherins ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
    Language English
    Publishing date 2003-09
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 603837-2
    ISSN 1522-1466 ; 1931-857X ; 0363-6127
    ISSN (online) 1522-1466
    ISSN 1931-857X ; 0363-6127
    DOI 10.1152/ajprenal.00439.2002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Interactions of tight junctions with membrane channels and transporters.

    Rajasekaran, Sigrid A / Beyenbach, Klaus W / Rajasekaran, Ayyappan K

    Biochimica et biophysica acta

    2007  Volume 1778, Issue 3, Page(s) 757–769

    Abstract: Tight junctions are unique organelles in epithelial cells. They are localized to the apico-lateral region and essential for the epithelial cell transport functions. The paracellular transport process that occurs via tight junctions is extensively studied ...

    Abstract Tight junctions are unique organelles in epithelial cells. They are localized to the apico-lateral region and essential for the epithelial cell transport functions. The paracellular transport process that occurs via tight junctions is extensively studied and is intricately regulated by various extracellular and intracellular signals. Fine regulation of this transport pathway is crucial for normal epithelial cell functions. Among factors that control tight junction permeability are ions and their transporters. However, this area of research is still in its infancy and much more needs to be learned about how these molecules regulate tight junction structure and functions. In this review we have attempted to compile literature on ion transporters and channels involved in the regulation of tight junctions.
    MeSH term(s) Animals ; Epithelial Cells/physiology ; Epithelial Cells/ultrastructure ; Humans ; Ion Channels/physiology ; Membrane Proteins/chemistry ; Membrane Proteins/physiology ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/physiology ; Models, Biological ; Models, Molecular ; Paracrine Communication ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/physiology ; Tight Junctions/physiology ; Tight Junctions/ultrastructure
    Chemical Substances Ion Channels ; Membrane Proteins ; Membrane Transport Proteins ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
    Language English
    Publishing date 2007-11-19
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2007.11.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Multiple functions of Na,K-ATPase in epithelial cells.

    Rajasekaran, Sigrid A / Barwe, Sonali P / Rajasekaran, Ayyappan K

    Seminars in nephrology

    2005  Volume 25, Issue 5, Page(s) 328–334

    Abstract: The Na,K-adenosine triphosphatase (ATPase), or sodium pump, has been well studied for its role in the regulation of ion homeostasis in mammalian cells. Recent studies suggest that Na,K-ATPase might have multiple functions such as a role in the regulation ...

    Abstract The Na,K-adenosine triphosphatase (ATPase), or sodium pump, has been well studied for its role in the regulation of ion homeostasis in mammalian cells. Recent studies suggest that Na,K-ATPase might have multiple functions such as a role in the regulation of tight junction structure and function, induction of polarity, regulation of actin dynamics, control of cell movement, and cell signaling. These functions appear to be modulated by Na,K-ATPase enzyme activity as well as protein-protein interactions of the alpha and beta subunits. In this review we attempt to differentiate functions associated with enzyme activity and subunit interactions. In addition, the consequence of impaired Na,K-ATPase function or reduced subunit expression levels in kidney diseases such as cancer, tubulointerstitial fibrosis, and ischemic nephropathy are discussed.
    MeSH term(s) Animals ; Cell Membrane Permeability/physiology ; Cell Movement/physiology ; Cytoskeleton/physiology ; Epithelial Cells/enzymology ; Humans ; Kidney/cytology ; Kidney Diseases/metabolism ; Kidney Diseases/physiopathology ; Signal Transduction/physiology ; Sodium-Potassium-Exchanging ATPase/metabolism ; Sodium-Potassium-Exchanging ATPase/physiology ; Stress Fibers/enzymology
    Chemical Substances Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
    Language English
    Publishing date 2005-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 604652-6
    ISSN 1558-4488 ; 0270-9295
    ISSN (online) 1558-4488
    ISSN 0270-9295
    DOI 10.1016/j.semnephrol.2005.03.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Expression of Na,K-ATPase beta-subunit in transformed MDCK cells increases the translation of the Na,K-ATPase alpha-subunit.

    Rajasekaran, Sigrid A / Gopal, Jegan / Rajasekaran, Ayyappan K

    Annals of the New York Academy of Sciences

    2003  Volume 986, Page(s) 652–654

    MeSH term(s) Animals ; Binding Sites ; Catalysis ; Cell Line, Transformed ; Dogs ; Isoenzymes/genetics ; Kinetics ; Protein Biosynthesis ; Recombinant Proteins/metabolism ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/genetics ; Sodium-Potassium-Exchanging ATPase/metabolism ; Transfection
    Chemical Substances Isoenzymes ; Recombinant Proteins ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
    Language English
    Publishing date 2003-04
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 211003-9
    ISSN 1749-6632 ; 0077-8923
    ISSN (online) 1749-6632
    ISSN 0077-8923
    DOI 10.1111/j.1749-6632.2003.tb07277.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Na,K-ATPase in the regulation of epithelial cell structure.

    Rajasekaran, Ayyappan K / Gopal, Jegan / Rajasekaran, Sigrid A

    Annals of the New York Academy of Sciences

    2003  Volume 986, Page(s) 649–651

    MeSH term(s) Animals ; Cell Line ; Dogs ; Epithelial Cells/cytology ; Epithelial Cells/enzymology ; Homeostasis ; Mesoderm/cytology ; Mesoderm/enzymology ; Sodium-Potassium-Exchanging ATPase/antagonists & inhibitors ; Sodium-Potassium-Exchanging ATPase/metabolism ; Tight Junctions/enzymology ; Tight Junctions/ultrastructure ; Tumor Cells, Cultured
    Chemical Substances Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
    Language English
    Publishing date 2003-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 211003-9
    ISSN 1749-6632 ; 0077-8923
    ISSN (online) 1749-6632
    ISSN 0077-8923
    DOI 10.1111/j.1749-6632.2003.tb07276.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Encapsulation of curcumin in self-assembling peptide hydrogels as injectable drug delivery vehicles.

    Altunbas, Aysegul / Lee, Seung J / Rajasekaran, Sigrid A / Schneider, Joel P / Pochan, Darrin J

    Biomaterials

    2011  Volume 32, Issue 25, Page(s) 5906–5914

    Abstract: Curcumin, a hydrophobic polyphenol, is an extract of turmeric root with antioxidant, anti-inflammatory and anti-tumorigenic properties. Its lack of water solubility and relatively low bioavailability set major limitations for its therapeutic use. In this ...

    Abstract Curcumin, a hydrophobic polyphenol, is an extract of turmeric root with antioxidant, anti-inflammatory and anti-tumorigenic properties. Its lack of water solubility and relatively low bioavailability set major limitations for its therapeutic use. In this study, a self-assembling peptide hydrogel is demonstrated to be an effective vehicle for the localized delivery of curcumin over sustained periods of time. The curcumin-hydrogel is prepared in-situ where curcumin encapsulation within the hydrogel network is accomplished concurrently with peptide self-assembly. Physical and in vitro biological studies were used to demonstrate the effectiveness of curcumin-loaded β-hairpin hydrogels as injectable agents for localized curcumin delivery. Notably, rheological characterization of the curcumin-loaded hydrogel before and after shear flow have indicated solid-like properties even at high curcumin payloads. In vitro experiments with a medulloblastoma cell line confirm that the encapsulation of the curcumin within the hydrogel does not have an adverse effect on its bioactivity. Most importantly, the rate of curcumin release and its consequent therapeutic efficacy can be conveniently modulated as a function of the concentration of the MAX8 peptide.
    MeSH term(s) Circular Dichroism ; Curcumin/administration & dosage ; Drug Carriers ; Drug Delivery Systems ; Hydrogels ; Microscopy, Electron, Transmission ; Peptides ; Rheology
    Chemical Substances Drug Carriers ; Hydrogels ; Peptides ; Curcumin (IT942ZTH98)
    Language English
    Publishing date 2011-05-23
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 603079-8
    ISSN 1878-5905 ; 0142-9612
    ISSN (online) 1878-5905
    ISSN 0142-9612
    DOI 10.1016/j.biomaterials.2011.04.069
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Curcumin-induced HDAC inhibition and attenuation of medulloblastoma growth in vitro and in vivo.

    Lee, Seung Joon / Krauthauser, Candice / Maduskuie, Victoria / Fawcett, Paul T / Olson, James M / Rajasekaran, Sigrid A

    BMC cancer

    2011  Volume 11, Page(s) 144

    Abstract: Background: Medulloblastoma is the most common brain tumor in children, and its prognosis is worse than for many other common pediatric cancers. Survivors undergoing treatment suffer from serious therapy-related side effects. Thus, it is imperative to ... ...

    Abstract Background: Medulloblastoma is the most common brain tumor in children, and its prognosis is worse than for many other common pediatric cancers. Survivors undergoing treatment suffer from serious therapy-related side effects. Thus, it is imperative to identify safer, effective treatments for medulloblastoma. In this study we evaluated the anti-cancer potential of curcumin in medulloblastoma by testing its ability to induce apoptosis and inhibit tumor growth in vitro and in vivo using established medulloblastoma models.
    Methods: Using cultured medulloblastoma cells, tumor xenografts, and the Smo/Smo transgenic medulloblastoma mouse model, the antitumor effects of curcumin were tested in vitro and in vivo.
    Results: Curcumin induced apoptosis and cell cycle arrest at the G2/M phase in medulloblastoma cells. These effects were accompanied by reduced histone deacetylase (HDAC) 4 expression and activity and increased tubulin acetylation, ultimately leading to mitotic catastrophe. In in vivo medulloblastoma xenografts, curcumin reduced tumor growth and significantly increased survival in the Smo/Smo transgenic medulloblastoma mouse model.
    Conclusions: The in vitro and in vivo data suggest that curcumin has the potential to be developed as a therapeutic agent for medulloblastoma.
    MeSH term(s) Acetylation/drug effects ; Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Apoptosis/drug effects ; Apoptosis/genetics ; Cell Growth Processes/drug effects ; Cell Growth Processes/genetics ; Cell Line, Tumor ; Cerebellar Neoplasms/drug therapy ; Cerebellar Neoplasms/genetics ; Cerebellar Neoplasms/pathology ; Curcumin/pharmacology ; Curcumin/therapeutic use ; Histone Deacetylases/genetics ; Histone Deacetylases/metabolism ; Humans ; Medulloblastoma/drug therapy ; Medulloblastoma/genetics ; Medulloblastoma/pathology ; Mice ; Mice, Transgenic ; Receptors, G-Protein-Coupled/genetics ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Smoothened Receptor ; Tubulin/metabolism ; Xenograft Model Antitumor Assays
    Chemical Substances Antineoplastic Agents ; Receptors, G-Protein-Coupled ; Repressor Proteins ; Smo protein, mouse ; Smoothened Receptor ; Tubulin ; HDAC4 protein, human (EC 3.5.1.98) ; Histone Deacetylases (EC 3.5.1.98) ; Curcumin (IT942ZTH98)
    Language English
    Publishing date 2011-04-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1471-2407
    ISSN (online) 1471-2407
    DOI 10.1186/1471-2407-11-144
    Database MEDical Literature Analysis and Retrieval System OnLINE

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