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Robert Vadnal - One of the best experts on this subject based on the ideXlab platform.

  • The effects of lithium isotopes on the myo-Inositol 1-phosphatase reaction in rat brain, liver, and testes
    Life Sciences, 1992
    Co-Authors: Ranganathan Parthasarathy, Lathakumari Parthasarathy, C. S. Shyamala Devi, T. G. Ramesh, Robert Vadnal
    Abstract:

    Abstract Enzyme inhibition studies were performed with several lithium isotopes in order to more precisely define how lithium inhibits the enzyme myo-Inositol 1-phosphatase. This lithium-induced inhibition is thought to be central to the therapeutic effects of lithium in the treatment of manic-depressive disorder. Naturally occurring lithium (NLi) exists as a combination of isotopes: 6Li and 7Li. Lethality studies were performed comparing 6LiCl, 7LiCl, and NLiCl, did not demonstrate a differential effect as previous studies had suggested. Enzyme inhibition studies were performed with these individual lithium isotopes, and compared to the effects of the naturally occurring combination (NLi) on the inhibition of myo-Inositol 1-phosphatase using a partially purified enzyme preparation from rat brain, liver and testes. Identical inhibition was observed with all lithium isotopes and their combinations. In addition, both D- and L- myo-Inositol 1-phosphates were used as enzyme substrates and found to be equivalent. These experiments, along with previous work demonstrating lithium acting as an uncompetitive inhibitor in the reaction, and the lack of lithium binding sites on the enzyme, suggests the hypothesis that lithium is possibly inhibiting this reaction by interfering with the formation of a transition cyclic intermediate, myo-Inositol 1,3-cyclic phosphate, which may be formed from either the D- or L- substrates. This proposal is in contrast to previous suggestions regarding the inhibitory mechanism of action of lithium on the myo-Inositol 1-phosphatase reaction.

  • The identification of a membrane-bound myo-Inositol 1-phosphatase in rat brain, liver, and testes.
    Biochemistry international, 1992
    Co-Authors: Robert Vadnal, Lathakumari Parthasarathy, Ranganathan Parthasarathy, T. G. Ramesh, C.s. Shyamaladevi
    Abstract:

    A membrane-bound myo-Inositol 1-phosphatase has been solubilized and partially purified from rat tissues. This particulate enzyme was detected in brain, liver and testis and certain physicochemical and enzymological properties were examined. Previously this major enzyme of the Inositol signaling system was considered strictly cytosolic. The ratio of activity in the membrane form was approximately one-eighth of the activity found with the cytosolic fraction. The molecular weight of this phosphatase was found to be 59,000 by gel filtration chromatography and a subunit molecular weight of 29,000 by Western blot analysis, values comparable to the cytosolic form. This phosphatase cleaves both D- and L- myo-Inositol 1-phosphates which originate from two different cellular pathways and is inhibited by lithium ions. Polyclonal antibodies were raised against homogeneous testicular cytosolic myo-Inositol 1-phosphatase and cross-reacted with this membrane form as determined by western blot analysis showing immunological identity.

Ranganathan Parthasarathy - One of the best experts on this subject based on the ideXlab platform.

  • The effects of lithium isotopes on the myo-Inositol 1-phosphatase reaction in rat brain, liver, and testes
    Life Sciences, 1992
    Co-Authors: Ranganathan Parthasarathy, Lathakumari Parthasarathy, C. S. Shyamala Devi, T. G. Ramesh, Robert Vadnal
    Abstract:

    Abstract Enzyme inhibition studies were performed with several lithium isotopes in order to more precisely define how lithium inhibits the enzyme myo-Inositol 1-phosphatase. This lithium-induced inhibition is thought to be central to the therapeutic effects of lithium in the treatment of manic-depressive disorder. Naturally occurring lithium (NLi) exists as a combination of isotopes: 6Li and 7Li. Lethality studies were performed comparing 6LiCl, 7LiCl, and NLiCl, did not demonstrate a differential effect as previous studies had suggested. Enzyme inhibition studies were performed with these individual lithium isotopes, and compared to the effects of the naturally occurring combination (NLi) on the inhibition of myo-Inositol 1-phosphatase using a partially purified enzyme preparation from rat brain, liver and testes. Identical inhibition was observed with all lithium isotopes and their combinations. In addition, both D- and L- myo-Inositol 1-phosphates were used as enzyme substrates and found to be equivalent. These experiments, along with previous work demonstrating lithium acting as an uncompetitive inhibitor in the reaction, and the lack of lithium binding sites on the enzyme, suggests the hypothesis that lithium is possibly inhibiting this reaction by interfering with the formation of a transition cyclic intermediate, myo-Inositol 1,3-cyclic phosphate, which may be formed from either the D- or L- substrates. This proposal is in contrast to previous suggestions regarding the inhibitory mechanism of action of lithium on the myo-Inositol 1-phosphatase reaction.

  • The identification of a membrane-bound myo-Inositol 1-phosphatase in rat brain, liver, and testes.
    Biochemistry international, 1992
    Co-Authors: Robert Vadnal, Lathakumari Parthasarathy, Ranganathan Parthasarathy, T. G. Ramesh, C.s. Shyamaladevi
    Abstract:

    A membrane-bound myo-Inositol 1-phosphatase has been solubilized and partially purified from rat tissues. This particulate enzyme was detected in brain, liver and testis and certain physicochemical and enzymological properties were examined. Previously this major enzyme of the Inositol signaling system was considered strictly cytosolic. The ratio of activity in the membrane form was approximately one-eighth of the activity found with the cytosolic fraction. The molecular weight of this phosphatase was found to be 59,000 by gel filtration chromatography and a subunit molecular weight of 29,000 by Western blot analysis, values comparable to the cytosolic form. This phosphatase cleaves both D- and L- myo-Inositol 1-phosphates which originate from two different cellular pathways and is inhibited by lithium ions. Polyclonal antibodies were raised against homogeneous testicular cytosolic myo-Inositol 1-phosphatase and cross-reacted with this membrane form as determined by western blot analysis showing immunological identity.

Lathakumari Parthasarathy - One of the best experts on this subject based on the ideXlab platform.

  • The effects of lithium isotopes on the myo-Inositol 1-phosphatase reaction in rat brain, liver, and testes
    Life Sciences, 1992
    Co-Authors: Ranganathan Parthasarathy, Lathakumari Parthasarathy, C. S. Shyamala Devi, T. G. Ramesh, Robert Vadnal
    Abstract:

    Abstract Enzyme inhibition studies were performed with several lithium isotopes in order to more precisely define how lithium inhibits the enzyme myo-Inositol 1-phosphatase. This lithium-induced inhibition is thought to be central to the therapeutic effects of lithium in the treatment of manic-depressive disorder. Naturally occurring lithium (NLi) exists as a combination of isotopes: 6Li and 7Li. Lethality studies were performed comparing 6LiCl, 7LiCl, and NLiCl, did not demonstrate a differential effect as previous studies had suggested. Enzyme inhibition studies were performed with these individual lithium isotopes, and compared to the effects of the naturally occurring combination (NLi) on the inhibition of myo-Inositol 1-phosphatase using a partially purified enzyme preparation from rat brain, liver and testes. Identical inhibition was observed with all lithium isotopes and their combinations. In addition, both D- and L- myo-Inositol 1-phosphates were used as enzyme substrates and found to be equivalent. These experiments, along with previous work demonstrating lithium acting as an uncompetitive inhibitor in the reaction, and the lack of lithium binding sites on the enzyme, suggests the hypothesis that lithium is possibly inhibiting this reaction by interfering with the formation of a transition cyclic intermediate, myo-Inositol 1,3-cyclic phosphate, which may be formed from either the D- or L- substrates. This proposal is in contrast to previous suggestions regarding the inhibitory mechanism of action of lithium on the myo-Inositol 1-phosphatase reaction.

  • The identification of a membrane-bound myo-Inositol 1-phosphatase in rat brain, liver, and testes.
    Biochemistry international, 1992
    Co-Authors: Robert Vadnal, Lathakumari Parthasarathy, Ranganathan Parthasarathy, T. G. Ramesh, C.s. Shyamaladevi
    Abstract:

    A membrane-bound myo-Inositol 1-phosphatase has been solubilized and partially purified from rat tissues. This particulate enzyme was detected in brain, liver and testis and certain physicochemical and enzymological properties were examined. Previously this major enzyme of the Inositol signaling system was considered strictly cytosolic. The ratio of activity in the membrane form was approximately one-eighth of the activity found with the cytosolic fraction. The molecular weight of this phosphatase was found to be 59,000 by gel filtration chromatography and a subunit molecular weight of 29,000 by Western blot analysis, values comparable to the cytosolic form. This phosphatase cleaves both D- and L- myo-Inositol 1-phosphates which originate from two different cellular pathways and is inhibited by lithium ions. Polyclonal antibodies were raised against homogeneous testicular cytosolic myo-Inositol 1-phosphatase and cross-reacted with this membrane form as determined by western blot analysis showing immunological identity.

T. G. Ramesh - One of the best experts on this subject based on the ideXlab platform.

  • The effects of lithium isotopes on the myo-Inositol 1-phosphatase reaction in rat brain, liver, and testes
    Life Sciences, 1992
    Co-Authors: Ranganathan Parthasarathy, Lathakumari Parthasarathy, C. S. Shyamala Devi, T. G. Ramesh, Robert Vadnal
    Abstract:

    Abstract Enzyme inhibition studies were performed with several lithium isotopes in order to more precisely define how lithium inhibits the enzyme myo-Inositol 1-phosphatase. This lithium-induced inhibition is thought to be central to the therapeutic effects of lithium in the treatment of manic-depressive disorder. Naturally occurring lithium (NLi) exists as a combination of isotopes: 6Li and 7Li. Lethality studies were performed comparing 6LiCl, 7LiCl, and NLiCl, did not demonstrate a differential effect as previous studies had suggested. Enzyme inhibition studies were performed with these individual lithium isotopes, and compared to the effects of the naturally occurring combination (NLi) on the inhibition of myo-Inositol 1-phosphatase using a partially purified enzyme preparation from rat brain, liver and testes. Identical inhibition was observed with all lithium isotopes and their combinations. In addition, both D- and L- myo-Inositol 1-phosphates were used as enzyme substrates and found to be equivalent. These experiments, along with previous work demonstrating lithium acting as an uncompetitive inhibitor in the reaction, and the lack of lithium binding sites on the enzyme, suggests the hypothesis that lithium is possibly inhibiting this reaction by interfering with the formation of a transition cyclic intermediate, myo-Inositol 1,3-cyclic phosphate, which may be formed from either the D- or L- substrates. This proposal is in contrast to previous suggestions regarding the inhibitory mechanism of action of lithium on the myo-Inositol 1-phosphatase reaction.

  • The identification of a membrane-bound myo-Inositol 1-phosphatase in rat brain, liver, and testes.
    Biochemistry international, 1992
    Co-Authors: Robert Vadnal, Lathakumari Parthasarathy, Ranganathan Parthasarathy, T. G. Ramesh, C.s. Shyamaladevi
    Abstract:

    A membrane-bound myo-Inositol 1-phosphatase has been solubilized and partially purified from rat tissues. This particulate enzyme was detected in brain, liver and testis and certain physicochemical and enzymological properties were examined. Previously this major enzyme of the Inositol signaling system was considered strictly cytosolic. The ratio of activity in the membrane form was approximately one-eighth of the activity found with the cytosolic fraction. The molecular weight of this phosphatase was found to be 59,000 by gel filtration chromatography and a subunit molecular weight of 29,000 by Western blot analysis, values comparable to the cytosolic form. This phosphatase cleaves both D- and L- myo-Inositol 1-phosphates which originate from two different cellular pathways and is inhibited by lithium ions. Polyclonal antibodies were raised against homogeneous testicular cytosolic myo-Inositol 1-phosphatase and cross-reacted with this membrane form as determined by western blot analysis showing immunological identity.

C.s. Shyamaladevi - One of the best experts on this subject based on the ideXlab platform.

  • The identification of a membrane-bound myo-Inositol 1-phosphatase in rat brain, liver, and testes.
    Biochemistry international, 1992
    Co-Authors: Robert Vadnal, Lathakumari Parthasarathy, Ranganathan Parthasarathy, T. G. Ramesh, C.s. Shyamaladevi
    Abstract:

    A membrane-bound myo-Inositol 1-phosphatase has been solubilized and partially purified from rat tissues. This particulate enzyme was detected in brain, liver and testis and certain physicochemical and enzymological properties were examined. Previously this major enzyme of the Inositol signaling system was considered strictly cytosolic. The ratio of activity in the membrane form was approximately one-eighth of the activity found with the cytosolic fraction. The molecular weight of this phosphatase was found to be 59,000 by gel filtration chromatography and a subunit molecular weight of 29,000 by Western blot analysis, values comparable to the cytosolic form. This phosphatase cleaves both D- and L- myo-Inositol 1-phosphates which originate from two different cellular pathways and is inhibited by lithium ions. Polyclonal antibodies were raised against homogeneous testicular cytosolic myo-Inositol 1-phosphatase and cross-reacted with this membrane form as determined by western blot analysis showing immunological identity.