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  • Rabbits  (25)
  • American Association for the Advancement of Science (AAAS)  (25)
  • 1980-1984  (25)
  • 1940-1944
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  • American Association for the Advancement of Science (AAAS)  (25)
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Year
  • 1
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    Hyperkeratosis induced by sunlight degradation products of the major polybrominated biphenyl in Firemaster (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-21
    Description: Sunlight photodegradation of 2,2', 4,4', 5,5' -hexabromobiphenyl, the major component of Firemaster, gave a mixture that produces severe hyperkeratosis of the rabbit ear. This component in its pure state does not cause hyperkeratosis. One or more of the four major photolysis products must be responsible for this activity. A similar photodegradation pattern was observed for 2,2', 3,4,4', 5,5' -heptabromobiphenyl, the second largest component of Firemaster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patterson, D G -- Hill, R H -- Needham, L L -- Orti, D L -- Kimbrough, R D -- Liddle, J A -- New York, N.Y. -- Science. 1981 Aug 21;213(4510):901-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6266016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biphenyl Compounds/radiation effects ; Chemical Industry ; Disease Models, Animal ; Environmental Exposure ; Keratosis/*chemically induced ; Michigan ; Photochemistry ; *Polybrominated Biphenyls/radiation effects ; Rabbits ; Sunlight
    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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  • 2
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    Significance of tissue myo-inositol concentrations in metabolic regulation in nerve (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-27
    Description: Approximately 25 percent of resting energy utilization in isolated nerve endoneurium is inhibited by medium containing defatted albumin and selectively restored by arachidonic acid but is unaffected by indomethacin or nordihydroguaiaretic acid. The same component of energy utilization is inhibited by small decreases in endoneurial myo-inositol, which decrease incorporation of carbon-14-labeled arachidonic acid into phosphatidylinositol. The fraction of the resting oxygen uptake inhibited by ouabain is decreased 40 to 50 percent by a reduced tissue myo-inositol concentration or by defatted albumin. Metabolic regulation by rapid, basal phosphatidylinositol turnover is dependent on the maintenance of normal tissue myoinositol concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, D A -- Winegrad, A I -- Martin, D B -- T32 AMO7314/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):848-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6285474" target="_blank"〉PubMed〈/a〉
    Keywords: Albumins/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/pharmacology ; Catechols/pharmacology ; Indomethacin/pharmacology ; Inositol/*metabolism ; Linolenic Acids/pharmacology ; Masoprocol ; Ouabain/pharmacology ; Oxygen Consumption ; Palmitic Acids/pharmacology ; Peripheral Nerves/*metabolism ; Phosphatidylinositols/metabolism ; Rabbits ; gamma-Linolenic Acid
    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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    Antibody to spermine: a natural biological constituent (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-06
    Description: A protein that binds spermine specifically was separated from normal rabbit serum by affinity chromatography. Immunoelectrophoresis, the Ouchterlony immunodiffusion test, and gradient gel electrophoresis indicated that this protein has immunoglobulin characteristics and consists of several populations of antibodies to spermine. These were sequentially released from Sepharose-spermine gel by step-wise elution with solutions ranging in pH from 4 to 1. The binding constants varied from 5.0 x 10(8) to 11.1 x 10(8) liters per mole. These globulins did not react with monoacetylputrescine, L-ornithine, L-lysine, and histamine. Negligible cross-reactivity was detected with spermidine, putrescine, N8-monoacetylspermidine, cadaverine, and diaminopropane. Since perturbations in polyamine metabolism have been identified in several diseases, the study of extracellular polyamine homeostasis may reveal an important regulatory function for this protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartos, D -- Bartos, F -- Campbell, R A -- Grettie, D P -- Smejtek, P -- New York, N.Y. -- Science. 1980 Jun 6;208(4448):1178-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*isolation & purification ; Binding Sites, Antibody ; Chromatography, Affinity ; Homeostasis ; Immunoglobulin G/isolation & purification ; Kinetics ; Rabbits ; Spermine/*immunology/metabolism
    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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    Running and breathing in mammals (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-01-21
    Description: Mechanical constraints appear to require that locomotion and breathing be synchronized in running mammals. Phase locking of limb and respiratory frequency has now been recorded during treadmill running in jackrabbits and during locomotion on solid ground in dogs, horses, and humans. Quadrupedal species normally synchronize the locomotor and respiratory cycles at a constant ratio of 1:1 (strides per breath) in both the trot and gallop. Human runners differ from quadrupeds in that while running they employ several phase-locked patterns (4:1, 3:1, 2:1, 1:1, 5:2, and 3:2), although a 2:1 coupling ratio appears to be favored. Even though the evolution of bipedal gait has reduced the mechanical constraints on respiration in man, thereby permitting greater flexibility in breathing pattern, it has seemingly not eliminated the need for the synchronization of respiration and body motion during sustained running. Flying birds have independently achieved phase-locked locomotor and respiratory cycles. This hints that strict locomotor-respiratory coupling may be a vital factor in the sustained aerobic exercise of endothermic vertebrates, especially those in which the stresses of locomotion tend to deform the thoracic complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bramble, D M -- Carrier, D R -- New York, N.Y. -- Science. 1983 Jan 21;219(4582):251-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6849136" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Gait ; Horses ; Humans ; *Locomotion ; Mammals ; *Physical Exertion ; Rabbits ; *Respiration
    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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    Turnover, membrane insertion, and degradation of sodium channels in rabbit urinary bladder (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-09-23
    Description: Noise analysis of rabbit bladder revealed two components: Lorentzian noise, arising from interaction of amiloride with the Na+ channel, and flicker noise (l/f, where f is frequency), as in other biological membranes. Hydrostatic pressure, which causes exchange between intracellular vesicular membrane and apical membrane, increases the number but not the single-channel current of the amiloride-sensitive channels. Flicker noise arises from degraded channels that have lost amiloride sensitivity and Na+ to K+ selectivity. The degraded channels were selectively removed by washing the mucosal surface. These results imply channel turnover by intracellular synthesis, transfer from vesicular to apical membrane, degradation, and elimination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loo, D D -- Lewis, S A -- Ifshin, M S -- Diamond, J M -- AM17327/AM/NIADDK NIH HHS/ -- AM20851/AM/NIADDK NIH HHS/ -- GM14772/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1288-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6612343" target="_blank"〉PubMed〈/a〉
    Keywords: Amiloride/pharmacology ; Animals ; Cell Membrane/metabolism ; Cytoplasmic Granules/metabolism ; Epithelium/physiology ; Rabbits ; Sodium/*metabolism ; Urinary Bladder/*metabolism
    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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    Bladder-surface glycosaminoglycans: an efficient mechanism of environmental adaptation (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-09
    Description: The transitional epithelium of the urinary bladder secretes and binds to its surface a glycosaminoglycan than inhibits the adherence of bacteria. Synthetic sulfonated glycosaminoglycans instilled intraluminally into bladders whose natural mucin layer has been removed are as effective as the natural mucin in preventing bacterial adherence. It also appears that adherence of calcium and protein is reduced in the presence of both the natural mucin layer and the synthetic sulfonated glycosaminoglycan sodium pentosanpolysulfate, suggesting that the antiadherence activity of both natural and synthetic surface glycosaminoglycans in the bladder extends to the molecular and ionic levels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parsons, C L -- Stauffer, C -- Schmidt, J D -- New York, N.Y. -- Science. 1980 May 9;208(4444):605-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154316" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Animals ; Calcium/metabolism ; Cell Adhesion ; Environmental Exposure ; Epithelium/physiology ; Glycosaminoglycans/*physiology ; Male ; Mucins/pharmacology ; Pentosan Sulfuric Polyester/pharmacology ; Protein Binding/drug effects ; Proteins/metabolism ; Rabbits ; Urinary Bladder/microbiology/*physiology
    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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  • 7
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    The hormonal control of sexual development (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, J D -- George, F W -- Griffin, J E -- AM03892/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Mar 20;211(4488):1278-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010602" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Mullerian Hormone ; Estradiol/metabolism/*physiology ; Female ; *Glycoproteins ; Gonadotropins/physiology ; *Growth Inhibitors ; Humans ; Male ; Morphogenesis ; Mullerian Ducts ; Ovary/embryology ; Rabbits ; Receptors, Androgen/metabolism ; *Sex Differentiation ; Testicular Hormones/*physiology ; Testis/embryology/secretion ; Testosterone/metabolism/*physiology ; Time Factors ; Urogenital System/embryology ; Wolffian Ducts
    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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  • 8
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    Bioactive cardiac substances: potent vasorelaxant activity in mammalian atria (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-07-01
    Description: Mammalian atrial extracts possess natriuretic and diuretic activity. In experiments reported here it was found that atrial, but not ventricular, extract also causes relaxation of isolated vascular and nonvascular smooth muscle preparations. The smooth muscle relaxant activity of atrial extract was heat-stable and concentration-dependent and could be destroyed with protease. Rabbit aortic and chick rectum strips were used for the detection of atrial biological activity. The atrial activity was separated by column chromatography into two peaks having apparent molecular weights of 20,000 to 30,000 and less than 10,000. The atrial substance that copurified with the smooth muscle relaxant activity in both peaks caused natriuresis when injected into conscious rats. It appears that atria possess at least two peptides that elicit smooth muscle relaxation and natriuresis, suggesting an endogenous system of fluid volume regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Currie, M G -- Geller, D M -- Cole, B R -- Boylan, J G -- YuSheng, W -- Holmberg, S W -- Needleman, P -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857267" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atrial Function ; Chickens ; Chromatography, Gel ; Dogs ; Dose-Response Relationship, Drug ; Humans ; Molecular Weight ; Muscle, Smooth/drug effects ; Muscle, Smooth, Vascular/*drug effects ; Natriuresis/drug effects ; Rabbits ; Rats ; Swine ; Vasodilation/drug effects
    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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  • 9
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    Oxygen tension regulates the expression of angiogenesis factor by macrophages (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-09-23
    Description: When cultured in a hypoxic environment similar to that found in the center of a wound, macrophages secreted active angiogenesis factor into the medium. Under conditions similar to those of well-oxygenated tissue, macrophages did not secrete active angiogenesis factor. Macrophages that secreted the factor at hypoxic conditions stopped secreting it when returned to room air. Thus the control of angiogenesis in wound healing may be the result of macrophages responding to tissue oxygen tension without the necessity of interacting with other cell types or biochemical signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Hunt, T K -- Scheuenstuhl, H -- Halliday, B J -- Werb, Z -- Banda, M J -- GM27345/GM/NIGMS NIH HHS/ -- HL26323/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1283-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6612342" target="_blank"〉PubMed〈/a〉
    Keywords: Angiogenesis Inducing Agents/*biosynthesis ; Animals ; Anoxia/physiopathology ; Cells, Cultured ; Cornea ; Growth Substances/*biosynthesis ; Macrophages/*physiology ; Models, Biological ; Oxygen/*physiology ; Rabbits ; *Wound Healing
    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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  • 10
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    Identification and location of brain protein 4.1 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-29
    Description: Protein 4.1 is a membrane skeletal protein that converts the low-affinity interaction between spectrin and actin into a high-affinity ternary complex of spectrin, protein 4.1, and actin that is essential to the structural stability of the erythrocyte. Pig brain was shown to contain an 87-kilodalton immunoreactive analog of protein 4.1 that has partial sequence homology with pig erythrocyte protein 4.1 and the same location as spectrin in the cortical cytoplasm of neuronal and glial cell types of the cerebellum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodman, S R -- Casoria, L A -- Coleman, D B -- Zagon, I S -- HL 26059/HL/NHLBI NIH HHS/ -- NS19357/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1433-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6374897" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Blood Proteins/*metabolism ; Brain/*metabolism ; *Cytoskeletal Proteins ; Erythrocytes/metabolism ; Fluorescent Antibody Technique ; Immunoglobulin G/immunology ; Male ; *Membrane Proteins ; *Neuropeptides ; Rabbits ; Spectrin/metabolism ; Swine
    Print ISSN: 0036-8075
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