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  • Spectrum Analysis, Raman  (4)
  • Eating  (2)
  • 1
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    Rapid rewiring of arcuate nucleus feeding circuits by leptin (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-06
    Description: The fat-derived hormone leptin regulates energy balance in part by modulating the activity of neuropeptide Y and proopiomelanocortin neurons in the hypothalamic arcuate nucleus. To study the intrinsic activity of these neurons and their responses to leptin, we generated mice that express distinct green fluorescent proteins in these two neuronal types. Leptin-deficient (ob/ob) mice differed from wild-type mice in the numbers of excitatory and inhibitory synapses and postsynaptic currents onto neuropeptide Y and proopiomelanocortin neurons. When leptin was delivered systemically to ob/ob mice, the synaptic density rapidly normalized, an effect detectable within 6 hours, several hours before leptin's effect on food intake. These data suggest that leptin-mediated plasticity in the ob/ob hypothalamus may underlie some of the hormone's behavioral effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinto, Shirly -- Roseberry, Aaron G -- Liu, Hongyan -- Diano, Sabrina -- Shanabrough, Marya -- Cai, Xiaoli -- Friedman, Jeffrey M -- Horvath, Tamas L -- DK060711/DK/NIDDK NIH HHS/ -- F32DK61176/DK/NIDDK NIH HHS/ -- F32NS046921/NS/NINDS NIH HHS/ -- R01 DK041096/DK/NIDDK NIH HHS/ -- R01 DK061619/DK/NIDDK NIH HHS/ -- RR014451/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 2;304(5667):110-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15064421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arcuate Nucleus of Hypothalamus/cytology/*physiology ; Body Weight/drug effects ; Eating ; Evoked Potentials ; Excitatory Postsynaptic Potentials ; *Feeding Behavior/drug effects ; Ghrelin ; Glutamic Acid/analysis ; Green Fluorescent Proteins ; In Vitro Techniques ; Leptin/genetics/pharmacology/*physiology ; Luminescent Proteins/analysis ; Mice ; Mice, Obese ; Mice, Transgenic ; Neuronal Plasticity/*physiology ; Neurons/drug effects/*physiology ; Neuropeptide Y/genetics/physiology ; Patch-Clamp Techniques ; Peptide Hormones/pharmacology ; Pro-Opiomelanocortin/genetics/physiology ; Recombinant Fusion Proteins/analysis ; Synapses/chemistry/ultrastructure ; Tetrodotoxin/pharmacology ; Transgenes ; gamma-Aminobutyric Acid/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Role for stearoyl-CoA desaturase-1 in leptin-mediated weight loss (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-13
    Description: Leptin elicits a metabolic response that cannot be explained by its anorectic effects alone. To examine the mechanism underlying leptin's metabolic actions, we used transcription profiling to identify leptin-regulated genes in ob/ob liver. Leptin was found to specifically repress RNA levels and enzymatic activity of hepatic stearoyl-CoA desaturase-1 (SCD-1), which catalyzes the biosynthesis of monounsaturated fatty acids. Mice lacking SCD-1 were lean and hypermetabolic. ob/ob mice with mutations in SCD-1 were significantly less obese than ob/ob controls and had markedly increased energy expenditure. ob/ob mice with mutations in SCD-1 had histologically normal livers with significantly reduced triglyceride storage and VLDL (very low density lipoprotein) production. These findings suggest that down-regulation of SCD-1 is an important component of leptin's metabolic actions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Paul -- Miyazaki, Makoto -- Socci, Nicholas D -- Hagge-Greenberg, Aaron -- Liedtke, Wolfgang -- Soukas, Alexander A -- Sharma, Ratnendra -- Hudgins, Lisa C -- Ntambi, James M -- Friedman, Jeffrey M -- GM07739/GM/NIGMS NIH HHS/ -- R01-DK41096/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):240-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Center for Studies in Physics and Biology, Rogosin Institute, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114623" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Weight ; Crosses, Genetic ; Down-Regulation ; Eating ; Energy Metabolism ; Female ; Gene Expression ; Gene Expression Profiling ; Leptin/genetics/*physiology ; Lipid Metabolism ; Lipids/analysis ; Lipoproteins, VLDL/metabolism ; Liver/*enzymology/metabolism/ultrastructure ; Male ; Mice ; Mice, Obese ; Microsomes, Liver/enzymology ; Mutation ; Oligonucleotide Array Sequence Analysis ; Oxygen Consumption ; RNA, Messenger/genetics/metabolism ; Stearoyl-CoA Desaturase/genetics/*metabolism ; Vacuoles/chemistry/ultrastructure ; *Weight Loss
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-17
    Description: Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T- state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friedman, J M -- Rousseau, D L -- Ondrias, M R -- Stepnoski, R A -- New York, N.Y. -- Science. 1982 Dec 17;218(4578):1244-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7146910" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxyhemoglobin ; Heme ; *Hemoglobins ; Histidine ; Humans ; Iron ; Motion ; Myoglobin ; Photolysis ; Spectrum Analysis, Raman
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Metastable species of hemoglobin: room temperature transients and cryogenically trapped intermediates (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-06
    Description: Resonance Raman spectra of photolyzed carbonmonoxyhemoglobin obtained with 10-nanosecond pulses are compared with the spectra of photolyzed carbonmonoxyhemoglobin stabilized at 80 K. In comparing the deoxy with the photodissociated species, the changes in the Raman spectra are the same for these two experimental regimes. These results show that at ambient and cryogenic temperatures the heme pocket in liganded hemoglobin is significantly different from that of deoxyhemoglobin. It is concluded that measurements of the properties of intermediate species from photodissociated hemoglobin stabilized at low temperatures can be used to probe the short-lived metastable forms of hemoglobin present after photodissociation under biologically relevant solution conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Friedman, J M -- Rousseau, D L -- New York, N.Y. -- Science. 1983 May 6;220(4597):615-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836305" target="_blank"〉PubMed〈/a〉
    Keywords: Carboxyhemoglobin ; Chemical Phenomena ; Chemistry ; Freezing ; *Hemoglobins ; Humans ; Ligands ; Spectrum Analysis, Raman ; Temperature
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Picosecond time-resolved resonance Raman studies of hemoglobin: implications for reactivity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-16
    Description: Picosecond time-resolved Raman spectra of hemoglobin generated with blue pulses (20 to 30 picoseconds) that were resonant with the Soret band and of sufficient intensity to completely photodissociate the starting liganded sample are reported. For both R- and T-state liganded hemoglobins, the peak frequencies in the spectrum of the deoxy transient were the same at approximately 25 picoseconds as those observed at 10 nanoseconds subsequent to photodissociation. In particular, the large R-T differences in the frequency of the stretching mode for the iron-proximal histidine bond (VFe-His) detected in previously reported nanosecond-resolved spectra were also evident in the picosecond-resolved spectra. The implications of this finding with respect to the distribution of strain energy in the liganded protein and the origin of the time course for geminate recombination are discussed. On the basis of these results, a microscopic model is proposed in which delocalization of strain energy is strongly coupled to the coordinate of the iron. The model is used to explain the origin of the R-T differences in the rates of ligand dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Findsen, E W -- Friedman, J M -- Ondrias, M R -- Simon, S R -- 2-506 RR-8139/RR/NCRR NIH HHS/ -- R01 GM3333O-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):661-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023704" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Hemoglobin A ; Humans ; Motion ; Protein Conformation ; Spectrum Analysis, Raman ; Structure-Activity Relationship ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Structure, dynamics, and reactivity in hemoglobin (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-14
    Description: The static structure of hemoglobin and its functional properties are very well characterized. It is still not known how energy is stored and used within the structure of the protein to promote function and functional diversity. An essential part of this question is understanding the mechanism through which the overall protein structure (quaternary structure) couples to the local environment about the oxygen binding sites. Time-resolved resonance Raman spectroscopy has been used to probe the vibrational degrees of the freedom of the binding site as a function of protein structure. Comparison of the spectra from both equilibrium and transient forms of deoxy hemoglobin from a variety of mammalian, reptilian, and fish hemoglobins reveals that for each quaternary structure there exist two tertiary states stabilized by the presence or absence of an iron-bound ligand. Pulse-probe Raman experiments show that for photodissociated, ligated hemoglobins the local tertiary structure relaxes at a solution-dependent rate extending from tens of nanoseconds to microseconds. In this local environment, the linkage between the iron and the proximal histidine proves to be the single observed structural feature that responds in a systematic and substantial manner to structural changes in the protein. The additional finding of a correlation between the frequency of the iron-proximal histidine stretching motion (nu Fe-His) and various parameters of ligand reactivity, including geminate recombination, implicates the associated localized structural element in the mechanism of protein control of ligand binding. On the basis of these and related finds, a model is presented to account for both coarse and fine control of ligand binding by the protein structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Friedman, J M -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1273-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001941" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Carboxyhemoglobin ; Cold Temperature ; *Hemoglobins ; Histidine ; Humans ; Hydrogen-Ion Concentration ; Iron ; *Oxyhemoglobins ; Protein Conformation ; Spectrum Analysis, Raman ; Structure-Activity Relationship ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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