The Experts below are selected from a list of 273 Experts worldwide ranked by ideXlab platform
J H Mcneill - One of the best experts on this subject based on the ideXlab platform.
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Insulin-induced Glut4 recruitment in the fatty Zucker rat heart is not associated with changes in Glut4 content in the Intracellular Membrane.
Molecular and cellular biochemistry, 1998Co-Authors: W. M. Li, Patrick Poucheret, J H McneillAbstract:Impaired cardiac glucose metabolism and glucose transport have been shown in the insulin resistant fatty Zucker rat. The aim of the present study was to examine the translocation of the insulin-sensitive glucose transporter (Glut4) in the heart of the fatty Zucker rat under in vivo conditions. Insulin was injected into both lean (FA/?) and fatty (fa/fa) Zucker rats via the tail vein. The time course of cardiac Glut4 translocation was studied by determining the subcellular distribution of Glut4 using a newly developed ELISA quantitation method. Insulin (10 U/kg) caused a 30% and 37% increase in plasma Membrane Glut4 content at 20 min after injection in lean and fatty rats respectively. The plasma Membrane Glut4 contents in the basal and insulin-stimulated states were significantly lower in the fatty rat when compared to the lean control. The dose effect of insulin (2.5-10 U/kg) on Glut4 mobilization to the plasma Membrane was similar in both phenotypes. The time course of Glut4 mobilization to the plasma Membrane (5-30 min), which was similar in both lean and fatty Zucker rats, showed that maximal translocation was reached at 5 min post insulin injection and persisted throughout the remaining 25 min. However, in fatty Zucker rats, Glut4 content in the Intracellular Membrane remained unchanged at all insulin doses and all time points studied. Collectively, these results show that Glut4 recruitment to the plasma Membrane is responsive to insulin in the fatty Zucker rat heart and that the maximal response was similar to that in lean Zucker rats. However, the recruitment of Glut4 to the plasma Membrane was not associated with changes in the Intracellular Membrane Glut4 content.
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Insulin-induced Glut4 recruitment in the fatty Zucker rat heart is not associated with changes in Glut4 content in the Intracellular Membrane
Molecular and Cellular Biochemistry, 1998Co-Authors: W. M. Li, Patrick Poucheret, J H McneillAbstract:Impaired cardiac glucose metabolism and glucose transport have been shown in the insulin resistant fatty Zucker rat. The aim of the present study was to examine the translocation of the insulin-sensitive glucose transporter (Glut4) in the heart of the fatty Zucker rat under in vivo conditions. Insulin was injected into both lean (FA/?) and fatty (fa/fa) Zucker rats via the tail vein. The time course of cardiac Glut4 translocation was studied by determining the subcellular distribution of Glut4 using a newly developed ELISA quantitation method. Insulin (10 U/kg) caused a 30% and 37% increase in plasma Membrane Glut4 content at 20 min after injection in lean and fatty rats respectively. The plasma Membrane Glut4 contents in the basal and insulin-stimulated states were significantly lower in the fatty rat when compared to the lean control. The dose effect of insulin (2.5‐10 U/kg) on Glut4 mobilization to the plasma Membrane was similar in both phenotypes. The time course of Glut4 mobilization to the plasma Membrane (5‐30 min), which was similar in both lean and fatty Zucker rats, showed that maximal translocation was reached at 5 min post insulin injection and persisted throughout the remaining 25 min. However, in fatty Zucker rats, Glut4 content in the Intracellular Membrane remained unchanged at all insulin doses and all time points studied. Collectively, these results show that Glut4 recruitment to the plasma Membrane is responsive to insulin in the fatty Zucker rat heart and that the maximal response was similar to that in lean Zucker rats. However, the recruitment of Glut4 to the plasma Membrane was not associated with changes in the Intracellular Membrane Glut4 content. (Mol Cell Biochem 183: 193‐200, 1998)
Sven Miller - One of the best experts on this subject based on the ideXlab platform.
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Modification of Intracellular Membrane structures for virus replication
Nature Reviews Microbiology, 2008Co-Authors: Sven Miller, Jacomine Krijnse-lockerAbstract:Many viruses induce the formation of altered Membrane structures upon replication in host cells. This Review examines how viruses modify Intracellular Membranes, highlights similarities between the structures that are induced by viruses from different families and discusses how these structures could be formed. Viruses are Intracellular parasites that use the host cell they infect to produce new infectious progeny. Distinct steps of the virus life cycle occur in association with the cytoskeleton or cytoplasmic Membranes, which are often modified during infection. Plus-stranded RNA viruses induce Membrane proliferations that support the replication of their genomes. Similarly, cytoplasmic replication of some DNA viruses occurs in association with modified cellular Membranes. We describe how viruses modify Intracellular Membranes, highlight similarities between the structures that are induced by viruses of different families and discuss how these structures could be formed. Plus-stranded RNA viruses induce large Membrane structures that might support the replication of their genomes. Similarly, cytoplasmic replication of poxviruses (large DNA viruses) occurs in associated Membranes. These Membranes originate from the endoplasmic reticulum (ER) or endosomes. Membrane vesicles that support viral replication are induced by a number of RNA viruses. Similarly, the poxvirus replication site is surrounded by a double-Membraned cisterna that is derived from the ER. Analogies to autophagy have been proposed since the finding that autophagy cellular processes involve the formation of double-Membrane vesicles. However, molecular evidence to support this hypothesis is lacking. Membrane association of the viral replication complex is mediated by the presence of one or more viral proteins that contain sequences which associate with, or integrate into, Membranes. Replication-competent Membranes might contain viral or cellular proteins that contain amphipathic helices, which could mediate the Membrane bending that is required to form spherical vesicles. Whereas poxvirus DNA replication occurs inside the ER-enclosed site, for most RNA viruses the topology of replication is not clear. Preliminary results for some RNA viruses suggest that their replication could also occur inside double-Membrane vesicles. We speculate that cytoplasmic replication might occur inside sites that are 'enwrapped' by an ER-derived cisterna, and that these cisternae are open to the cytoplasm. Thus, RNA and DNA viruses could use a common mechanism for replication that involves Membrane wrapping by cellular cisternal Membranes. We propose that three-dimensional analyses using high-resolution electron-microscopy techniques could be useful for addressing this issue. High-throughput small-interfering-RNA screens should also shed light on molecular requirements for virus-induced Membrane modifications.
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modification of Intracellular Membrane structures for virus replication
Nature Reviews Microbiology, 2008Co-Authors: Sven Miller, Jacomine KrijnselockerAbstract:Viruses are Intracellular parasites that use the host cell they infect to produce new infectious progeny. Distinct steps of the virus life cycle occur in association with the cytoskeleton or cytoplasmic Membranes, which are often modified during infection. Plus-stranded RNA viruses induce Membrane proliferations that support the replication of their genomes. Similarly, cytoplasmic replication of some DNA viruses occurs in association with modified cellular Membranes. We describe how viruses modify Intracellular Membranes, highlight similarities between the structures that are induced by viruses of different families and discuss how these structures could be formed.
W. M. Li - One of the best experts on this subject based on the ideXlab platform.
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Insulin-induced Glut4 recruitment in the fatty Zucker rat heart is not associated with changes in Glut4 content in the Intracellular Membrane.
Molecular and cellular biochemistry, 1998Co-Authors: W. M. Li, Patrick Poucheret, J H McneillAbstract:Impaired cardiac glucose metabolism and glucose transport have been shown in the insulin resistant fatty Zucker rat. The aim of the present study was to examine the translocation of the insulin-sensitive glucose transporter (Glut4) in the heart of the fatty Zucker rat under in vivo conditions. Insulin was injected into both lean (FA/?) and fatty (fa/fa) Zucker rats via the tail vein. The time course of cardiac Glut4 translocation was studied by determining the subcellular distribution of Glut4 using a newly developed ELISA quantitation method. Insulin (10 U/kg) caused a 30% and 37% increase in plasma Membrane Glut4 content at 20 min after injection in lean and fatty rats respectively. The plasma Membrane Glut4 contents in the basal and insulin-stimulated states were significantly lower in the fatty rat when compared to the lean control. The dose effect of insulin (2.5-10 U/kg) on Glut4 mobilization to the plasma Membrane was similar in both phenotypes. The time course of Glut4 mobilization to the plasma Membrane (5-30 min), which was similar in both lean and fatty Zucker rats, showed that maximal translocation was reached at 5 min post insulin injection and persisted throughout the remaining 25 min. However, in fatty Zucker rats, Glut4 content in the Intracellular Membrane remained unchanged at all insulin doses and all time points studied. Collectively, these results show that Glut4 recruitment to the plasma Membrane is responsive to insulin in the fatty Zucker rat heart and that the maximal response was similar to that in lean Zucker rats. However, the recruitment of Glut4 to the plasma Membrane was not associated with changes in the Intracellular Membrane Glut4 content.
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Insulin-induced Glut4 recruitment in the fatty Zucker rat heart is not associated with changes in Glut4 content in the Intracellular Membrane
Molecular and Cellular Biochemistry, 1998Co-Authors: W. M. Li, Patrick Poucheret, J H McneillAbstract:Impaired cardiac glucose metabolism and glucose transport have been shown in the insulin resistant fatty Zucker rat. The aim of the present study was to examine the translocation of the insulin-sensitive glucose transporter (Glut4) in the heart of the fatty Zucker rat under in vivo conditions. Insulin was injected into both lean (FA/?) and fatty (fa/fa) Zucker rats via the tail vein. The time course of cardiac Glut4 translocation was studied by determining the subcellular distribution of Glut4 using a newly developed ELISA quantitation method. Insulin (10 U/kg) caused a 30% and 37% increase in plasma Membrane Glut4 content at 20 min after injection in lean and fatty rats respectively. The plasma Membrane Glut4 contents in the basal and insulin-stimulated states were significantly lower in the fatty rat when compared to the lean control. The dose effect of insulin (2.5‐10 U/kg) on Glut4 mobilization to the plasma Membrane was similar in both phenotypes. The time course of Glut4 mobilization to the plasma Membrane (5‐30 min), which was similar in both lean and fatty Zucker rats, showed that maximal translocation was reached at 5 min post insulin injection and persisted throughout the remaining 25 min. However, in fatty Zucker rats, Glut4 content in the Intracellular Membrane remained unchanged at all insulin doses and all time points studied. Collectively, these results show that Glut4 recruitment to the plasma Membrane is responsive to insulin in the fatty Zucker rat heart and that the maximal response was similar to that in lean Zucker rats. However, the recruitment of Glut4 to the plasma Membrane was not associated with changes in the Intracellular Membrane Glut4 content. (Mol Cell Biochem 183: 193‐200, 1998)
Richard H. Scheller - One of the best experts on this subject based on the ideXlab platform.
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In search of the molecular mechanism of Intracellular Membrane fusion and neurotransmitter release
Nature medicine, 2013Co-Authors: Richard H. SchellerAbstract:In search of the molecular mechanism of Intracellular Membrane fusion and neurotransmitter release
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snares engines for Membrane fusion
Nature Reviews Molecular Cell Biology, 2006Co-Authors: Reinhard Jahn, Richard H. SchellerAbstract:Since their discovery in the late 1980s, SNARE proteins have been recognized as key components of protein complexes that drive Intracellular Membrane fusion. Despite considerable sequence divergence, their mechanism seems to be conserved and is adaptable for diverse fusion reactions.
Reinhard Jahn - One of the best experts on this subject based on the ideXlab platform.
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probing and manipulating Intracellular Membrane traffic by microinjection of artificial vesicles
Proceedings of the National Academy of Sciences of the United States of America, 2017Co-Authors: Seiichi Koike, Reinhard JahnAbstract:There is still a large gap in our understanding between the functional complexity of cells and the reconstruction of partial cellular functions in vitro from purified or engineered parts. Here we have introduced artificial vesicles of defined composition into living cells to probe the capacity of the cellular cytoplasm in dealing with foreign material and to develop tools for the directed manipulation of cellular functions. Our data show that protein-free liposomes, after variable delay times, are captured by the Golgi apparatus that is reached either by random diffusion or, in the case of large unilamellar vesicles, by microtubule-dependent transport via a dynactin/dynein motor complex. However, insertion of early endosomal SNARE proteins suffices to convert liposomes into trafficking vesicles that dock and fuse with early endosomes, thus overriding the default pathway to the Golgi. Moreover, such liposomes can be directed to mitochondria expressing simple artificial affinity tags, which can also be employed to divert endogenous trafficking vesicles. In addition, fusion or subsequent acidification of liposomes can be monitored by incorporation of appropriate chemical sensors. This approach provides an opportunity for probing and manipulating cellular functions that cannot be addressed by conventional genetic approaches. We conclude that the cellular cytoplasm has a remarkable capacity for self-organization and that introduction of such macromolecular complexes may advance nanoengineering of eukaryotic cells.
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snares engines for Membrane fusion
Nature Reviews Molecular Cell Biology, 2006Co-Authors: Reinhard Jahn, Richard H. SchellerAbstract:Since their discovery in the late 1980s, SNARE proteins have been recognized as key components of protein complexes that drive Intracellular Membrane fusion. Despite considerable sequence divergence, their mechanism seems to be conserved and is adaptable for diverse fusion reactions.
