Natural'' Igs, mainly IgM, comprise part of the innate immune system present in healthy individuals, including antigen-free mice. These Igs are thought to delay pathogenicity of infecting agents until antigen-induced high affinity Tgs of all isotypes are produced. Previous studies suggested that the acquired humoral response arises directly from the innate response, i.e., that B cells expressing natural IgM, upon antigen encounter, differentiate to give rise both to cells that secrete high amounts of IgM and to cells that undergo affinity maturation and isotype switching. However, by using a murine model of influenza virus infection, we demonstrate here that the B cells that produce natural antiviral IgM neither increase their IgM production nor undergo isotype switching to IgG2a in response to the infection. These cells are distinct from the B cells that produce the antiviral response after encounter with the pathogen. Our data therefore demonstrate that the innate and the acquired humoral immunities to influenza virus are separate effector arms of the immune system and that antigen exposure per se is not sufficient to increase natural antibody production. Stanford Univ, Sch Med, Beckman Ctr B007, Dept Genet, Stanford, CA 94305 USA; Univ Melbourne, Dept Microbiol, Melbourne, Vic 3056, Australia Stanford University; University of Melbourne Baumgarth, N (corresponding author), Stanford Univ, Sch Med, Beckman Ctr B007, Dept Genet, 300 Pasteur Dr, Stanford, CA 94305 USA. Baumgarth@Stanford.edu Baumgarth, Nicole/AAI-6949-2020 Brown, Lorena/0000-0001-9342-909X AVRAMEAS S, 1991, IMMUNOL TODAY, V12, P154; BACCALA R, 1989, P NATL ACAD SCI USA, V86, P4624, DOI 10.1073/pnas.86.12.4624; BAUMGARTH N, 1994, J VIROL, V68, P7575, DOI 10.1128/JVI.68.11.7575-7581.1994; Baumgarth N, 1996, J VIROL, V70, P4411, DOI 10.1128/JVI.70.7.4411-4418.1996; BHAT NM, 1992, INT IMMUNOL, V4, P243, DOI 10.1093/intimm/4.2.243; BIGOS M, 1999, IN PRESS CYTOMETRY; Boes M, 1998, J IMMUNOL, V160, P4776; Bouvet JP, 1998, INFECT IMMUN, V66, P1; Carroll MC, 1998, ANNU REV IMMUNOL, V16, P545, DOI 10.1146/annurev.immunol.16.1.545; Casali P, 1996, CURR TOP MICROBIOL, V210, P167; CASALI P, 1987, SCIENCE, V236, P77, DOI 10.1126/science.3105056; Coutinho A, 1995, CURR OPIN IMMUNOL, V7, P812, DOI 10.1016/0952-7915(95)80053-0; Fang YF, 1998, J IMMUNOL, V160, P5273; Fischer MB, 1996, J IMMUNOL, V157, P549; FORSTER I, 1987, EUR J IMMUNOL, V17, P521, DOI 10.1002/eji.1830170414; Hardy R.R., 1986, HDB EXPT IMMUNOLOGY, V1, P31; HAYAKAWA K, 1984, P NATL ACAD SCI-BIOL, V81, P2494, DOI 10.1073/pnas.81.8.2494; HAYAKAWA K, 1983, J EXP MED, V157, P202, DOI 10.1084/jem.157.1.202; KANTOR AB, 1993, ANNU REV IMMUNOL, V11, P501, DOI 10.1146/annurev.iy.11.040193.002441; KENNY JJ, 1983, J IMMUNOL, V130, P2574; Kroese FGM, 1989, INT IMMUNOL, V1, P75, DOI 10.1093/intimm/1.1.75; LALOR PA, 1989, EUR J IMMUNOL, V19, P501, DOI 10.1002/eji.1830190314; LALOR PA, 1989, EUR J IMMUNOL, V19, P507, DOI 10.1002/eji.1830190315; MASMOUDI H, 1990, INT IMMUNOL, V2, P515, DOI 10.1093/intimm/2.6.515; OKeefe TL, 1996, SCIENCE, V274, P798, DOI 10.1126/science.274.5288.798; PEREIRA P, 1986, EUR J IMMUNOL, V16, P685, DOI 10.1002/eji.1830160616; Roederer M, 1996, CYTOMETRY, V24, P191, DOI 10.1002/(SICI)1097-0320(19960701)24:3<191::AID-CYTO1>3.0.CO;2-L; ROTHSTEIN TL, 1988, J IMMUNOL, V141, P4089; ROTT O, 1995, J IMMUNOL, V155, P134; Stall A M, 1996, Semin Immunol, V8, P45, DOI 10.1006/smim.1996.0007; Szomolanyi-Tsuda E, 1998, CURR OPIN IMMUNOL, V10, P431, DOI 10.1016/S0952-7915(98)80117-9; TAKI S, 1992, ANN NY ACAD SCI, V651, P328; Tedder TF, 1997, IMMUNITY, V6, P107, DOI 10.1016/S1074-7613(00)80418-5; UEKI Y, 1990, J EXP MED, V171, P19, DOI 10.1084/jem.171.1.19; WEIGLE WO, 1983, SPRINGER SEMIN IMMUN, V6, P173 35 256 329 0 17 NATL ACAD SCIENCES WASHINGTON 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA 0027-8424 P NATL ACAD SCI USA Proc. Natl. Acad. Sci. U. S. A. MAR 2 1999 96 5 2250 2255 10.1073/pnas.96.5.2250 http://dx.doi.org/10.1073/pnas.96.5.2250 6 Multidisciplinary Sciences Science Citation Index Expanded (SCI-EXPANDED) Science & Technology - Other Topics 172ZP 10051627 Green Published 2024-02-29 WOS:000078956600080
J Callahan, LF; Pincus, T Callahan, LF; Pincus, T Access to health care, socioeconomic status, and health - In response ANNALS OF INTERNAL MEDICINE English Letter Univ N Carolina, Chapel Hill, NC 27599 USA; Vanderbilt Univ, Nashville, TN 37232 USA University of North Carolina; University of North Carolina Chapel Hill; Vanderbilt University Callahan, LF (corresponding author), Univ N Carolina, Chapel Hill, NC 27599 USA. Callahan, Leigh/X-3799-2018 Callahan, Leigh/0000-0001-6362-7220 MARMOT MG, 1986, LANCET, V2, P274; McKeown T., 1979, ROLE MED; Pincus T, 1998, ANN INTERN MED, V129, P406, DOI 10.7326/0003-4819-129-5-199809010-00011; PINCUS T, 1987, J CHRON DIS, V40, P865, DOI 10.1016/0021-9681(87)90186-X; Sagan L.A., 1987, The health of nations: True causes of sickness and well-being 5 1 1 0 0 AMER COLL PHYSICIANS PHILADELPHIA INDEPENDENCE MALL WEST 6TH AND RACE ST, PHILADELPHIA, PA 19106-1572 USA 0003-4819 1539-3704 ANN INTERN MED Ann. Intern. Med. MAR 2 1999 130 5 453 453 10.7326/0003-4819-130-5-199903020-00012 http://dx.doi.org/10.7326/0003-4819-130-5-199903020-00012 1 Medicine, General & Internal Science Citation Index Expanded (SCI-EXPANDED) General & Internal Medicine 172AA 2024-02-29 WOS:000078898100020
J Cézanne, L; Lopez, A; Loste, F; Parnaud, G; Saurel, O; Demange, P; Tocanne, JF Cézanne, L; Lopez, A; Loste, F; Parnaud, G; Saurel, O; Demange, P; Tocanne, JF Organization and dynamics of the proteolipid complexes formed by annexin V and lipids in planar supported lipid bilayers BIOCHEMISTRY English Article PLACENTAL ANTICOAGULANT PROTEIN; MEMBRANE-BINDING PROTEIN; PHOSPHOLIPID-BINDING; MOLECULAR-STRUCTURE; CRYSTAL-STRUCTURE; FRAP EXPERIMENTS; CALCIUM-BINDING; FLUORESCENCE; MONOLAYERS; DIFFUSION The consequences of the binding of annexin V on its lateral mobility and that of Lipids were investigated by means of experimental and simulated FRAP experiments. Experiments were carried out on planar supported bilayers (PC/PS 9:2 mol/mol mixtures) in the presence of 1 mM CaCl2 in the subphase. The probes C-12-NBD-PS and fluorescein-labeled annexin V were used and the data compared with that previously obtained for C-12-NBD-PC [Saurel, O., Cezanne, L., Milon, A., Tocanne, J. F., & Demange, P. (1998) Biochemistry 37, 1403-1410]. At complete coverage of the lipid bilayer by the protein (C-annexin = 80 nM), the lateral mobility of C-12-NBD-PC was reduced by 40% while C-12-NBD-PS and bound annexin V molecules were nearly immobilized (D < 10(-11) cm(2)/s). At moderate protein concentration (20 nM < C-annexin < 80 nM), best fitting of the lipid and protein probe recoveries was achieved with one single diffusion coefficient and a mobile fraction close to 100%, indicating homogeneous lipid and protein populations. In contrast, at low protein concentration (C-annexin < 20 nM), C-12-NBD-PS showed a two-component diffusion. The slow PS population at C-annexin < 20 nM and the single PS population at C-annexin > 20 nM moved at the same rate that bound annexin V (mobile fraction close to 100%), indicating strong PS/protein interactions. With the aid of computer simulations of the lateral motion of PC molecules, based on the 2-D crystalline networks formed by annexin V in contact with the lipid bilayer, these FRAP results may be accounted for by considering a rather simple model of a proteolipidic complex consisting of an extended 2-D crystalline protein network facing the lipid bilayer and stabilized by strong interactions between annexin V and PS molecules. In this model, immobilization of annexin V and PS molecules originates from their mutual interactions. The slowing down of PC molecules is due to various obstacles to their lateral diffusion which can be described as: the four PS molecules bound to the protein, the tryptophan 187 which presumably interacts with the lipids at the level of their polar headgroups and probably the three other hydrophobic amino acid residues located on the AB calcium-binding loops of the protein. CNRS, Inst Pharmacol & Biol Struct, F-31062 Toulouse, France Universite de Toulouse; Universite Toulouse III - Paul Sabatier; Centre National de la Recherche Scientifique (CNRS) Cézanne, L (corresponding author), CNRS, Inst Pharmacol & Biol Struct, 118 Route Narbonne, F-31062 Toulouse, France. Wunder, Stephanie L/B-5066-2012; demange, pascal JP/U-3561-2018; Olivier, Saurel/AAQ-7007-2020; Zdilla, Michael J/B-4145-2011 demange, pascal JP/0000-0002-9572-9990; Saurel, Olivier/0000-0003-1439-4103 [Anonymous], [No title captured]; BERENDES R, 1993, SCIENCE, V262, P427, DOI 10.1126/science.7692599; BERENDES R, 1993, FEBS LETT, V317, P131, DOI 10.1016/0014-5793(93)81507-V; BRIAN AA, 1984, P NATL ACAD SCI-BIOL, V81, P6159, DOI 10.1073/pnas.81.19.6159; BRISSON A, 1991, J MOL BIOL, V220, P199, DOI 10.1016/0022-2836(91)90002-N; BUDISA N, 1995, EUR J BIOCHEM, V230, P788; BURGER A, 1993, FEBS LETT, V329, P25, DOI 10.1016/0014-5793(93)80185-W; Campos B, 1998, BIOCHEMISTRY-US, V37, P8004, DOI 10.1021/bi973142n; CONCHA NO, 1993, SCIENCE, V261, P1321, DOI 10.1126/science.8362244; CRUMPTON MJ, 1990, NATURE, V345, P212, DOI 10.1038/345212a0; Dubois T, 1998, BIOCHEM J, V330, P1277, DOI 10.1042/bj3301277; FolleniusWund A, 1997, BIOCHEM BIOPH RES CO, V234, P111, DOI 10.1006/bbrc.1997.6596; FUNAKOSHI T, 1987, BIOCHEMISTRY-US, V26, P8087, DOI 10.1021/bi00399a011; GEISOW MJ, 1986, NATURE, V320, P636, DOI 10.1038/320636a0; GILMANSHIN R, 1994, BIOCHEMISTRY-US, V33, P8225, DOI 10.1021/bi00193a008; HINDERLITER AK, 1994, BIOPHYS J, V67, P1906, DOI 10.1016/S0006-3495(94)80673-3; HUBER R, 1992, J MOL BIOL, V223, P683, DOI 10.1016/0022-2836(92)90984-R; HUBER R, 1990, EMBO J, V9, P3867, DOI 10.1002/j.1460-2075.1990.tb07605.x; HUBER R, 1990, FEBS LETT, V275, P15, DOI 10.1016/0014-5793(90)81428-Q; KALB E, 1992, BIOCHIM BIOPHYS ACTA, V1103, P307, DOI 10.1016/0005-2736(92)90101-Q; LEWITBENTLEY A, 1992, EUR J BIOCHEM, V210, P73, DOI 10.1111/j.1432-1033.1992.tb17392.x; LIEMANN S, 1995, STRUCTURE, V3, P233, DOI 10.1016/S0969-2126(01)00152-6; LOPEZ A, 1988, BIOPHYS J, V53, P963, DOI 10.1016/S0006-3495(88)83177-1; MEERS P, 1993, BIOCHEMISTRY-US, V32, P5411, DOI 10.1021/bi00071a016; MEERS P, 1991, BIOCHEMISTRY-US, V30, P2903, DOI 10.1021/bi00225a025; MEERS P, 1990, BIOCHEMISTRY-US, V29, P3325, DOI 10.1021/bi00465a025; MERKEL R, 1989, J PHYS-PARIS, V50, P1535, DOI 10.1051/jphys:0198900500120153500; NAGLE JF, 1993, BIOPHYS J, V64, P1476, DOI 10.1016/S0006-3495(93)81514-5; NOLLERT P, 1995, BIOPHYS J, V69, P1447, DOI 10.1016/S0006-3495(95)80014-7; OLOFSSON A, 1994, J STRUCT BIOL, V113, P199, DOI 10.1006/jsbi.1994.1054; RAYNAL P, 1994, BBA-REV BIOMEMBRANES, V1197, P63, DOI 10.1016/0304-4157(94)90019-1; Reviakine I, 1998, J STRUCT BIOL, V121, P356, DOI 10.1006/jsbi.1998.4003; ROUSER G, 1970, LIPIDS, V5, P494, DOI 10.1007/BF02531316; Salomé L, 1998, EUR BIOPHYS J BIOPHY, V27, P391, DOI 10.1007/s002490050146; Saurel O, 1998, BIOCHEMISTRY-US, V37, P1403, DOI 10.1021/bi971484n; SCHRAM V, 1994, EUR BIOPHYS J, V23, P337; Seaton BA, 1996, ANNEXINS MOL STRUCTU, P15; SILVIUS JR, 1990, BIOCHEMISTRY-US, V29, P2930, DOI 10.1021/bi00464a007; SWAIRJO MA, 1995, NAT STRUCT BIOL, V2, P968, DOI 10.1038/nsb1195-968; TAIT JF, 1989, J BIOL CHEM, V264, P7944; VOGES D, 1994, J MOL BIOL, V238, P199, DOI 10.1006/jmbi.1994.1281; VONTSCHARNER V, 1981, BIOPHYS J, V36, P421, DOI 10.1016/S0006-3495(81)84741-8 42 39 47 0 15 AMER CHEMICAL SOC WASHINGTON 1155 16TH ST, NW, WASHINGTON, DC 20036 USA 0006-2960 BIOCHEMISTRY-US Biochemistry MAR 2 1999 38 9 2779 2786 10.1021/bi9818568 http://dx.doi.org/10.1021/bi9818568 8 Biochemistry & Molecular Biology Science Citation Index Expanded (SCI-EXPANDED) Biochemistry & Molecular Biology 174BH 10052949 2024-02-29 WOS:000079013900020
J Chu, NF; Wang, DJ; Shieh, SM; Rimm, EB Chu, NF; Wang, DJ; Shieh, SM; Rimm, EB Asssociation of plasma leptin level and obesity on insulin resistance syndrome among school children in Taiwan - The taipei children heart study CIRCULATION English Meeting Abstract Harvard Univ, Sch Publ Hlth, Dept Epidemiol, Boston, MA 02115 USA; Tri Serv Gen Hosp, Taipei, Taiwan Harvard University; Harvard T.H. Chan School of Public Health; Tri-Service General Hospital Chu, Nain-Feng/HNB-4015-2023 0 0 0 0 2 LIPPINCOTT WILLIAMS & WILKINS PHILADELPHIA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA 0009-7322 CIRCULATION Circulation MAR 2 1999 99 8 P30 1113 1113 1 Cardiac & Cardiovascular Systems; Peripheral Vascular Disease Science Citation Index Expanded (SCI-EXPANDED) Cardiovascular System & Cardiology 171BC 2024-02-29 WOS:000078841500080
J Coello, P; Sassen, A; Haywood, V; Davis, KR; Walker, JC Coello, P; Sassen, A; Haywood, V; Davis, KR; Walker, JC Biochemical characterization and expression of RLK4, a receptor-like kinase from Arabidopsis thaliana PLANT SCIENCE English Article Arabidopsis; receptor-like kinases; S-locus glycoproteins; serine/threonine protein kinases GROWTH-FACTOR RECEPTOR; PROTEIN-KINASE; BRASSICA-OLERACEA; GENE; SUPERFAMILY; PATTERNS; SEQUENCE; DOMAINS; FAMILY; MAIZE The Arabidopsis RLK4 gene encodes a Ser/Thr receptor-like protein kinase. A lysine to glutamic acid substitution in an essential subdomain of the RLK4 catalytic domain, results in an inactive protein kinase. Transphosphorylation experiments, using the inactive form of RLK4 as a substrate for an active form? indicated that autophosphorylation could proceed via an intermolecular mechanism. Multiple sites are phosphorylated at the catalytic domain of RLK4, as indicated by two-dimensional (2D) thin-layer electrophoresis and chromatography, To analyze the expression pattern of RLK4, we used the RLK4 promoter to drive the expression of the beta-glucuronidase (GUS) reporter gene in transgenic plants. GUS activity was observed in the shoot apex and roots. In roots, the GUS staining pattern was limited to the lateral roots and at the root-hypocotyl transition zone. Analysis of an RLK4 mutant line did not show any difference in the phenotype with respect to the wild type. The expression of other related RLKs with similar expression patterns suggest there is functional redundancy for RLK4. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved. Univ Missouri, Div Biol Sci, Columbia, MO 65211 USA; Ohio State Univ, Ctr Plant Biotechnol, Columbus, OH 43210 USA University of Missouri System; University of Missouri Columbia; University System of Ohio; Ohio State University Walker, JC (corresponding author), Univ Missouri, Div Biol Sci, 308 Tucker Hall, Columbia, MO 65211 USA. jcw@biosci.mbp.missouri.edu Davis, Keith R/C-5623-2009; Davis, Keith/H-3242-2019; Coello, Patricia/AAH-9448-2021 Davis, Keith R/0000-0002-7432-8610; Davis, Keith/0000-0002-7432-8610; An G., 1988, PLANT MOL BIOL MAN A, VA3, P1; BALLOTTI R, 1989, EMBO J, V8, P3303, DOI 10.1002/j.1460-2075.1989.tb08491.x; BOYLE WJ, 1991, METHOD ENZYMOL, V201, P110; Braun DM, 1997, PLANT J, V12, P83, DOI 10.1046/j.1365-313X.1997.12010083.x; Braun DM, 1996, TRENDS BIOCHEM SCI, V21, P70, DOI 10.1016/S0968-0004(96)80185-X; Craig S., 1992, GUS protocols: using the GUS gene as a reporter of gene expression., P115; DENG WP, 1992, ANAL BIOCHEM, V200, P81, DOI 10.1016/0003-2697(92)90280-K; DWYER KG, 1994, PLANT CELL, V6, P1829, DOI 10.1105/tpc.6.12.1829; FELLER SM, 1994, TIBS, V227, P453; GAMBORG OL, 1968, EXP CELL RES, V50, P151, DOI 10.1016/0014-4827(68)90403-5; HANKS SK, 1988, SCIENCE, V241, P42, DOI 10.1126/science.3291115; HELDIN CH, 1995, CELL, V80, P213, DOI 10.1016/0092-8674(95)90404-2; HORN MA, 1994, BBA-PROTEIN STRUCT M, V1208, P65, DOI 10.1016/0167-4838(94)90160-0; KNIGHTON DR, 1991, SCIENCE, V253, P407, DOI 10.1126/science.1862342; LAEMMLI UK, 1970, NATURE, V227, P680, DOI 10.1038/227680a0; LIU YG, 1995, GENOMICS, V25, P674, DOI 10.1016/0888-7543(95)80010-J; NASRALLAH JB, 1993, PLANT CELL, V5, P1325, DOI 10.2307/3869785; Pastuglia M, 1997, PLANT CELL, V9, P49, DOI 10.1105/tpc.9.1.49; Sambrook J., 1989, MOL CLONING; SMITH DL, 1995, PLANT CELL, V7, P735, DOI 10.1105/tpc.7.6.735; STONE JM, 1994, SCIENCE, V266, P793, DOI 10.1126/science.7973632; SUNDARESAN V, 1995, GENE DEV, V9, P1797, DOI 10.1101/gad.9.14.1797; TOBIAS CM, 1992, PLANT PHYSIOL, V99, P284, DOI 10.1104/pp.99.1.284; VALVEKENS D, 1988, P NATL ACAD SCI USA, V85, P5536, DOI 10.1073/pnas.85.15.5536; WALKER JC, 1993, PLANT J, V3, P451, DOI 10.1046/j.1365-313X.1993.t01-23-00999.x; WALKER JC, 1990, NATURE, V345, P743, DOI 10.1038/345743a0; WEI L, 1994, CURR OPIN STRUC BIOL, V4, P450, DOI 10.1016/S0959-440X(94)90115-5; YARDEN Y, 1987, BIOCHEMISTRY-US, V26, P1443, DOI 10.1021/bi00379a035; YARDEN Y, 1987, BIOCHEMISTRY-US, V26, P1434, DOI 10.1021/bi00379a034; ZHAO Y, 1994, PLANT MOL BIOL, V26, P791, DOI 10.1007/BF00028849 30 9 11 0 5 ELSEVIER IRELAND LTD CLARE ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000, IRELAND 0168-9452 PLANT SCI Plant Sci. MAR 2 1999 142 1 83 91 10.1016/S0168-9452(98)00247-7 http://dx.doi.org/10.1016/S0168-9452(98)00247-7 9 Biochemistry & Molecular Biology; Plant Sciences Science Citation Index Expanded (SCI-EXPANDED) Biochemistry & Molecular Biology; Plant Sciences 191GG 2024-02-29 WOS:000080013700010
J Cushman, M; Arnold, AM; Kuller, LH; Psaty, BM; Manolio, TA; Burke, GL; Polak, JF; Tracy, RP Cushman, M; Arnold, AM; Kuller, LH; Psaty, BM; Manolio, TA; Burke, GL; Polak, JF; Tracy, RP C-reactive protein and risks of myocardial infarction, stroke and death in an elderly cohort CIRCULATION English Meeting Abstract Harvard Univ, Boston, MA 02115 USA; NHLBI, Bethesda, MD 20892 USA; Univ Pittsburgh, Pittsburgh, PA USA; Univ Vermont, Burlington, VT USA; Univ Vermont, Colchester, VT USA; Univ Washington, Seattle, WA 98195 USA; Wake Forest Univ, Winston Salem, NC 27109 USA Harvard University; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI); Pennsylvania Commonwealth System of Higher Education (PCSHE); University of Pittsburgh; University of Vermont; University of Vermont; University of Washington; University of Washington Seattle; Wake Forest University 0 5 5 0 0 LIPPINCOTT WILLIAMS & WILKINS PHILADELPHIA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA 0009-7322 CIRCULATION Circulation MAR 2 1999 99 8 30 1108 1108 1 Cardiac & Cardiovascular Systems; Peripheral Vascular Disease Science Citation Index Expanded (SCI-EXPANDED) Cardiovascular System & Cardiology 171BC 2024-02-29 WOS:000078841500050
J Denton, D; Shade, R; Zamarippa, F; Egan, G; Blair-West, J; McKinley, M; Fox, P Denton, D; Shade, R; Zamarippa, F; Egan, G; Blair-West, J; McKinley, M; Fox, P Correlation of regional cerebral blood flow and change of plasma sodium concentration during genesis and satiation of thirst PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA English Article POSITRON EMISSION TOMOGRAPHY; HUMAN-BRAIN; OSMOTIC THIRST; ACTIVATION; ATTENTION; IMAGES Positron emission tomography studies were conducted during genesis of moderate thirst by rapid i.v. infusion of hypertonic saline (0.51 M) and after satiation of thirst by drinking water. The correlation of regional cerebral blood flow with the change in the plasma Na concentration showed a significant group of cerebral activations in the anterior cingulate region and also a site in the middle temporal gyrus and in the periaqueductal gray. Strongest deactivations occurred in the parahippocampal and frontal gyri. The data are consistent with an important role of the anterior cingulate in the genesis of thirst. Univ Melbourne, Howard Florey Inst Expt Physiol & Med, Parkville, Vic 3052, Australia; Univ Texas, Hlth Sci Ctr, Res Imaging Ctr, San Antonio, TX 78284 USA; SW Fdn Biomed Res, San Antonio, TX 78245 USA Florey Institute of Neuroscience & Mental Health; University of Melbourne; University of Texas System; University of Texas Health Science Center at San Antonio; Texas Biomedical Research Institute Denton, D (corresponding author), Univ Melbourne, Howard Florey Inst Expt Physiol & Med, Parkville, Vic 3052, Australia. dad@hfi.unimelb.edu.au Fox, Peter/B-4725-2010; Egan, Gary F./A-1381-2013 Fox, Peter/0000-0002-0465-2028; Denton, Derek/0000-0002-1931-1365; Egan, Gary/0000-0002-3186-4026 ANDERSSON B, 1952, EXPERIENTIA, V8, P157, DOI 10.1007/BF02170230; ANDERSSON B, 1973, Conditional Reflex, V8, P147; BAYLIS PH, 1980, J ROY SOC MED, V73, P255, DOI 10.1177/014107688007300408; Bentivoglio M., 1993, Neurobiology of Cingulate Cortex and Limbic Thalamus: A Comprehensive Handbook, P71, DOI [10.1007/978-1-4899-6704-6_3, DOI 10.1007/978-1-4899-6704-6_3]; Bernard C., 1856, LECONS PHYSL EXPT AP; BLAIRWEST JR, 1994, BRAIN RES, V637, P335, DOI 10.1016/0006-8993(94)91256-4; Buck R., 1986, MIND BRAIN DIALOGUES, P275; CANNON WB, 1918, P ROY SOC LOND B BIO, V90, P283; COGHILL RC, 1994, J NEUROSCI, V14, P4095; DENENBERG VH, 1981, BEHAV BRAIN SCI, V4, P1, DOI 10.1017/S0140525X00007330; Denton D., 1982, The hunger for salt; Denton DA, 1996, P NATL ACAD SCI USA, V93, P7397, DOI 10.1073/pnas.93.14.7397; Fitzsimons J.T., 1991, THIRST PHYSL PSYCHOL, P3; FITZSIMONS JT, 1979, PHYSL THIRST; FOX PT, 1985, J COMPUT ASSIST TOMO, V9, P141, DOI 10.1097/00004728-198501000-00025; FOX PT, 1989, J NUCL MED, V30, P141; FOX PT, 1988, J CEREBR BLOOD F MET, V8, P642, DOI 10.1038/jcbfm.1988.111; HIRANO T, 1974, J EXP BIOL, V61, P737; HOESON GW, NEUROBIOLOGY CINGULA, P249; Kinomura S, 1996, SCIENCE, V271, P512, DOI 10.1126/science.271.5248.512; KUPPFERMANN I, 1991, PRINICPLES NEURALSCI, P823; Lancaster JL, 1995, HUM BRAIN MAPP, V3, P209, DOI 10.1002/hbm.460030305; Lancaster JL, 1997, HUM BRAIN MAPP, V5, P238, DOI 10.1002/(SICI)1097-0193(1997)5:4<238::AID-HBM6>3.0.CO;2-4; MCKINLEY MJ, 1978, BRAIN RES, V141, P89, DOI 10.1016/0006-8993(78)90619-4; MCKINLEY MJ, 1999, IN PRESS AM J PHYSL; MINTUN MA, 1989, J CEREBR BLOOD F MET, V9, P96, DOI 10.1038/jcbfm.1989.13; MULLERPREUSS P, 1980, BRAIN RES, V202, P307, DOI 10.1016/0006-8993(80)90143-2; Papez JW, 1937, ARCH NEURO PSYCHIATR, V38, P725, DOI 10.1001/archneurpsyc.1937.02260220069003; PARDO JV, 1990, P NATL ACAD SCI USA, V87, P256, DOI 10.1073/pnas.87.1.256; PHILLIPS PA, 1991, AM J PHYSIOL, V261, pR166, DOI 10.1152/ajpregu.1991.261.1.R166; PHILLIPS PA, 1985, AM J PHYSIOL, V248, pR645, DOI 10.1152/ajpregu.1985.248.6.R645; Porrino L. J., 1993, NEUROBIOLOGY CINGULA, P445, DOI https://doi.org/10.1007/978-1-4899-6704-6_16; POSNER MI, 1990, ANNU REV NEUROSCI, V13, P25, DOI 10.1146/annurev.neuro.13.1.25; RAICHLE ME, 1983, J NUCL MED, V24, P790; ROBINSON BW, 1968, EXP BRAIN RES, V4, P330, DOI 10.1007/BF00235700; Roland P. E., 1993, BRAIN ACTIVATION; Talairach G., 1988, Planar Stereotaxic Atlas of the Human Brain; VERNEY EB, 1947, PROC R SOC SER B-BIO, V135, P25, DOI 10.1098/rspb.1947.0037; Vogt B.A., 1993, Neurobiology of Cingulate Cortex and Limbic Thalamus; VOGT BA, 1993, NEUROBIOLOGY CINGULA, pR7; WOLF AV, 1958, THIRST, P32 41 78 81 0 3 NATL ACAD SCIENCES WASHINGTON 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA 0027-8424 P NATL ACAD SCI USA Proc. Natl. Acad. Sci. U. S. A. MAR 2 1999 96 5 2532 2537 10.1073/pnas.96.5.2532 http://dx.doi.org/10.1073/pnas.96.5.2532 6 Multidisciplinary Sciences Science Citation Index Expanded (SCI-EXPANDED) Science & Technology - Other Topics 172ZP 10051677 Green Published 2024-02-29 WOS:000078956600130
J Din-Dzietham, R; Liao, DP; Diez-Roux, A; Paton, K; Brown, A; Carnethon, M; Howard, G; Nieto, FJ; Tyroler, HA Din-Dzietham, R; Liao, DP; Diez-Roux, A; Paton, K; Brown, A; Carnethon, M; Howard, G; Nieto, FJ; Tyroler, HA Carotid artery elasticity varies directly with educational achievement level: The ARIC Study, 1987-1992. CIRCULATION English Meeting Abstract Wake Forest Univ, Bowman Gray Sch Med, Dept Publ Hlth, Winston Salem, NC USA; Columbia Presbyterian Med Ctr, New York, NY 10032 USA; Johns Hopkins Univ, Sch Hyg & Publ Hlth, Baltimore, MD USA; Penn State Univ, Hershey, PA USA; Univ Mississippi, Ctr Med, Jackson, MS 39216 USA; Univ N Carolina, Chapel Hill, NC USA; Univ N Carolina, Sch Publ Hlth, Chapel Hill, NC USA Wake Forest University; Wake Forest Baptist Medical Center; Columbia University; NewYork-Presbyterian Hospital; Johns Hopkins University; Pennsylvania Commonwealth System of Higher Education (PCSHE); Pennsylvania State University; Penn State Health; University of Mississippi; University of North Carolina; University of North Carolina Chapel Hill; University of North Carolina; University of North Carolina Chapel Hill 0 0 0 0 0 LIPPINCOTT WILLIAMS & WILKINS PHILADELPHIA 530 WALNUT ST, PHILADELPHIA, PA 19106-3621 USA 0009-7322 CIRCULATION Circulation MAR 2 1999 99 8 P20 1112 1112 1 Cardiac & Cardiovascular Systems; Peripheral Vascular Disease Science Citation Index Expanded (SCI-EXPANDED) Cardiovascular System & Cardiology 171BC 2024-02-29 WOS:000078841500070
J Doyle, LA; Yang, WD; Abruzzo, LV; Krogmann, T; Gao, YM; Rishi, AK; Ross, DD Doyle, LA; Yang, WD; Abruzzo, LV; Krogmann, T; Gao, YM; Rishi, AK; Ross, DD A multidrug resistance transporter from human MCF-7 breast cancer cells (vol 95, pg 15665, 1998) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA English Correction Doyle LA, 1998, P NATL ACAD SCI USA, V95, P15665, DOI 10.1073/pnas.95.26.15665 1 24 25 0 6 NATL ACAD SCIENCES WASHINGTON 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA 0027-8424 P NATL ACAD SCI USA Proc. Natl. Acad. Sci. U. S. A. MAR 2 1999 96 5 2569 2569 1 Multidisciplinary Sciences Science Citation Index Expanded (SCI-EXPANDED) Science & Technology - Other Topics 172ZP 2024-02-29 WOS:000078956600140
J Eres, MH; Weidner, DE; Schwartz, LW Eres, MH; Weidner, DE; Schwartz, LW Three-dimensional direct numerical simulation of surface-tension-gradient effects on the leveling of an evaporating multicomponent fluid LANGMUIR English Article THERMOSETTING WATERBORNE COATINGS; BEHAVIOR; LAYER Mathematical and numerical modeling of drying coating layers is of interest to both industrial and academic communities. Compositional changes that occur during the drying process make the implementation of practical and efficient numerical models rather difficult. In this paper we present a three-dimensional mathematical and numerical model based on the lubrication approximation for the flow of drying paint films on horizontal substrates. The paint is modeled as a multicomponent liquid with one nonvolatile and one volatile component, termed the resin" and the "solvent" respectively. Our model includes the effects of surface tension and gravitational forces as well as surface tension gradient effects which arise due to solvent evaporation. The dependence of viscosity, diffusivity, and evaporation rate on resin concentration is also incorporated in the model. A closed-form Linearized solution has been found for coating layers that are of almost uniform thickness. The numerical solution agrees closely with the linear solution in the appropriate Limit. A model simulation demonstrates the effect of surface tension gradients due to compositional changes in a three-dimensional flow field, and we suggest methods by which these gradients may be used to obtain a more uniform final coating layer.