The Experts below are selected from a list of 210 Experts worldwide ranked by ideXlab platform
Amira Klip - One of the best experts on this subject based on the ideXlab platform.
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Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line.
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
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expression of vesicle associated membrane protein 2 vamp 2 synaptobrevin ii and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
Chandrasekhar Yallampalli - One of the best experts on this subject based on the ideXlab platform.
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progesterone upregulates calcitonin gene related peptide and adrenomedullin receptor components and cyclic adenosine 3 5 monophosphate generation in eker rat uterine smooth Muscle Cell Line
Biology of Reproduction, 2005Co-Authors: Chandrasekhar Thota, Chandrasekhar YallampalliAbstract:Abstract Calcitonin gene-related peptide (CGRP) and adrenomedullin (AM), two potent smooth-Muscle relaxants, have been shown to cause uterine relaxation. Both CGRP- and AM-binding sites in the uterus increase during pregnancy and decrease at labor and postpartum. These changes in binding sites appear to be related to the changes in calcitonin receptor-like receptor (CRLR), receptor activity-modified protein 1 (RAMP1), RAMP2, and RAMP3 mRNA levels. It is not clear, however, whether the changes in the receptor components occur in the myometrial Cells and whether the steroid hormones can directly alter these receptor components in the Muscle Cells. In addition, the mechanism of CGRP and AM signaling in the rat myometrium is not well understood. Therefore, we examined the mRNA expression of CGRP- and AM-receptor components, G protein Gαs, CGRP, and AM stimulation of cAMP and cGMP, and the effects of progesterone on these parameters in the Eker rat uterine myometrial smooth-Muscle Cell Line (ELT3). ELT3 Cells ...
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Progesterone Upregulates Calcitonin Gene-Related Peptide and Adrenomedullin Receptor Components and Cyclic Adenosine 3′5′-Monophosphate Generation in Eker Rat Uterine Smooth Muscle Cell Line
Biology of reproduction, 2004Co-Authors: Chandrasekhar Thota, Chandrasekhar YallampalliAbstract:Abstract Calcitonin gene-related peptide (CGRP) and adrenomedullin (AM), two potent smooth-Muscle relaxants, have been shown to cause uterine relaxation. Both CGRP- and AM-binding sites in the uterus increase during pregnancy and decrease at labor and postpartum. These changes in binding sites appear to be related to the changes in calcitonin receptor-like receptor (CRLR), receptor activity-modified protein 1 (RAMP1), RAMP2, and RAMP3 mRNA levels. It is not clear, however, whether the changes in the receptor components occur in the myometrial Cells and whether the steroid hormones can directly alter these receptor components in the Muscle Cells. In addition, the mechanism of CGRP and AM signaling in the rat myometrium is not well understood. Therefore, we examined the mRNA expression of CGRP- and AM-receptor components, G protein Gαs, CGRP, and AM stimulation of cAMP and cGMP, and the effects of progesterone on these parameters in the Eker rat uterine myometrial smooth-Muscle Cell Line (ELT3). ELT3 Cells ...
Allen Volchuk - One of the best experts on this subject based on the ideXlab platform.
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Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line.
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
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expression of vesicle associated membrane protein 2 vamp 2 synaptobrevin ii and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
E. Habermann - One of the best experts on this subject based on the ideXlab platform.
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Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line.
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
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expression of vesicle associated membrane protein 2 vamp 2 synaptobrevin ii and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
Zhi Liu - One of the best experts on this subject based on the ideXlab platform.
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Expression of vesicle-associated membrane protein 2 (VAMP-2)/synaptobrevin II and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line.
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
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expression of vesicle associated membrane protein 2 vamp 2 synaptobrevin ii and Cellubrevin in rat skeletal Muscle and in a Muscle Cell Line
Biochemical Journal, 1994Co-Authors: Allen Volchuk, Zhi Liu, William S. Trimble, Y. Mitsumoto, E. Habermann, Amira KlipAbstract:Molecular studies have identified a family of synaptic vesicle-associated membrane proteins (VAMPs, also known as synaptobrevins) which have been implicated in synaptic vesicle docking and/or fusion with plasma membrane proteins. Here we demonstrate the expression of two members of this family, VAMP-2/synaptobrevin II and Cellubrevin, in skeletal Muscle, a tissue with both constitutive and regulated membrane traffic. The 18 kDa VAMP-2 polypeptide was detected in purified membrane fractions from adult skeletal Muscle and from L6 myotubes in culture, demonstrating that the presence of this protein in the isolated Muscle membrane fractions is not the result of contamination by ancillary tissues such as peripheral nerve. Furthermore, skeletal Muscle and the Muscle Cell Line also expressed Cellubrevin, a VAMP-2 homologue of 17 kDa; which is much less abundant in brain Cells. Both VAMP-2 and Cellubrevin were preferentially isolated in membrane fractions rich in plasma membranes, and were less concentrated in light microsomes and other internal membrane fractions of mature Muscle or Muscle Cells in culture. Interestingly, both VAMP-2 and Cellubrevin were much more abundant in the differentiated L6 myotubes than in their precursor myoblasts, suggesting that they are required for functions of differentiated Muscle Cells. The identity of both polypeptides was further confirmed by their susceptibility to proteolysis by Clostridium tetanus toxin. Expression of these products was further established by the presence of mRNA transcripts of VAMP-2 and Cellubrevin, but not of VAMP-1, in both skeletal Muscle and L6 myotubes. In contrast, other synaptic vesicle and docking/fusion components were undetectable, such as VAMP-1, SNAP25 and syntaxin 1A/1B, as were synaptophysin and synapsin Ia/Ib, proteins which are believed to be involved in sensing the signal for neuronal exocytosis. It is concluded that VAMP-2 and Cellubrevin are expressed in skeletal Muscle Cells and may each participate in specific processes of intraCellular membrane traffic.
