xt70cf9j6d9t https://exploreuk.uky.edu/dips/xt70cf9j6d9t/data/mets.xml University of Kentucky University of Kentucky Chemistry Department 20030418 A brochure for the Naff Symposium, an event hosted by the University of Kentucky Chemistry Department supported by the Anna S. Naff Endowment Fund. This brochure belongs to the University of Kentucky Chemistry Department Records collection, accession number 2014ua075. archival material  English University of Kentucky Chemistry Department Contact the Special Collections Research Center for information regarding rights and use of this collection. University of Kentucky Chemistry Department Naff Symposium brochures Twenty-Ninth Annual Symposium on Chemistry and Molecular Biology: "Neuroscience" text Twenty-Ninth Annual Symposium on Chemistry and Molecular Biology: "Neuroscience" 2003 2017 true xt70cf9j6d9t section xt70cf9j6d9t 9:» .8 .1' “3.2””; also :7r7..“!1', ’2 t. my: - "Fete..i;~-;.:e:~t;r,~.i ;=.«'%;'»:~.‘é.~.,~.ig;w,¢t«.v»;;..t;.:mares:-wet-’0; with": 'g’fsx‘ﬁemév‘rﬁw“is: -.-‘!..»-»‘—.~if-‘ {Ft “-ogtvv'w ”’l‘V’i» "'7‘” 3’3" ""1537": ii": a? ‘ ' mi n
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8:30 am. Registration and Continental Breakfast fibronectin region and a putative kinase domain. The gene encod- ‘2 3 ‘12,, Symposmm on .2511» {ké “
Atrium (Room 1-65), William T. Young Library ing Kalirin uses multiple promoters and alternative splicing to gen- g g .3 “'3 l? ’ 3':i'.‘":#§:.;.::t-=i:£ ‘;T.:%ii::,2fﬁ6‘="3 ,‘

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9:00 am. Welcome by Dr. Lee T. Todd, J_r., president, The spectrin-like region of Kalirin and Trio is the site of interaction 3 8 e x 2 tn” : C he IStry J 1‘”,
University of Kentucky. - Auditorium (Room 1- with peptidylglycine alpha-amidating monooxygenase (a secretory : 0'. < S E ifﬁgﬂ" 13" #:- ’ﬁtfﬂm

62), William T. Young Library granule enzyme), the inducible form of nitric acid synthase. and E (D. o. 3 a; WF‘IQ‘ V & Ei‘gfii'éﬁmf

. . huntingtin associated protein. The first GEF domain of Kalirin and q. 3 E 0- :?ﬁ"? ’ ﬁbz' {29.33.59
9.05 am. lrftroductory Remarks - Dr. Tae H. Ji, Univer- Trio activates Raci and RhoG while the second GEF domain acti- ‘5 3 iﬁgﬂbkh‘ I if.“ Pﬁyi 0‘
Sity of Kentucky vates RhoA. Expression of dual GEF isoforms of Kalirin causes 2 i,“~%‘.i:, §"‘ b Mo Iecu Iar s;ﬁ‘£:

. exuberant outgrowth of axons from sympathetic neurons while I'il‘r'ifﬁw: (“5 ‘3»
9.10 am. Dr. Susumu Tonegawa, Massachusetts Institute expression of a mono GEF isoform of Kalirin greatly increases the if: ﬁ.‘5‘.{_ "A I ' .. [if it
ﬁt Technology ,, number of dendritic spines in hippocampal and cortical neurons. iiﬁikg’gﬁf BIOlogy ‘,?:f;i;{i';‘~; L

Memory Ftecall lmportantly, antisense-mediated reductions in Kalirin expression ﬁvm‘ﬁ {W’S‘yi} J;

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it might prowde this function. We have tested this hypothesis by E; :3? it, “I“. $4.4"
generating and analyzing a genetically engineered mouse strain 2-00 p m Dr Ashley I Bush Massach MSW: A ti;giw?ﬁ

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In which the N—methyl-D-asparate (NMDA) receptor gene is ab- Hospital and Harvard Medical School "IE“? / \ $91?
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memory I’} the Morris water maze. but they were impaired in re- , AB is the principal component of the plaque pathology which 3313:3354 2“"?! ﬁg???" 5
trievmg ihl? memQVY When presented with a fraction of the original Is the hallmark of Alzheimer‘s disease (AD). We have characterized my“ a. ' ‘ fix it? W3 l
0995. Similarly, hippocampal CA1 pyramidal cells in mutant mice AB asauQ'qutOUS metalloprotein, With selective high-affinity binding $3“? if eStabllShed m the memory Of prﬁ,
displayed normal plaCe-related activity in a full-cue environment Sites. for Z'nC (K5!z 100 nM) and copper (K31z 10 attoM). Several angst; T3; Anna 8 Na“ 5’97”? Eigdi i
but showed a reduction in activity upon partial cue removal. These studies have reported that there is an elevation 0f zinc and copper I ‘353§;;‘33e5i3" i I high £34 1
result? Provide direct evidence for CA3 NMDA receptor involve- in the plaques in Alzheimer‘s disease. Furthermore, genetic ablation i I I {£1332 —-———————-——-——-—-— {'in «33‘
merit m assomative memory recall. of the ZnT3 transporter, which loads zinc into the glutamatergic lt‘?:{s- Skiff“; ﬁt}

. SYnapse, abolishes amyloid de osition in the T 2576 mouse mod I a. ~ ”’1' ' ‘1)

10:00 am. Poster Sessmn, Room 137, Chemistry-Physics for AD. p g e .o x ’ NeurOSCIence “Wag”
Building :43 binds Cu and Zn through a site that involves oligomeric Lo Hf: 5:}

Pepti e assembly. and resembles the structure of SOD1. When Lo r“ “ “N

11 :45 a.m. Buffet Lunch, Faculty Club [Please return regis- synthetic AB binds copper in the absence of zinc, it is highly redox v? 8 3%15 '65 ﬁ '2“; «Fl-f .1".
tration card by April 11, 2003 for reservations] active. Biolo ical reducin a ents such as do a ' ,9 >‘ ' 1'5: $53.9} {if L, ">::’;ji§$m

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1.00 pm. 3r. littllfleardtMains, University of Connecticut the AB/Cu complex acts as a catalyst generating H202 (Km: 5 pM g 3 8 1H t.:z?ﬁg~,
ea en er Vmax: 3O nM/min) The toxicity of AB species is pro ' , C ttux I ‘étiﬁsif'iiret-L”:

n . . , ,. . , - portional to O V “ "m" ' at: H

Kalirin and Trio. A Medley of lnteractors the peptides ability to reduce Cu or Fe and generate H20 (AB42> M— E >_ ‘17:».- ,3 Susumu Toneggwa *3 rﬁft”‘

. . . .. AB4O >rat AB). / 2 0 ._ x «4 31314 Richard E. Mains “’31"

PreCise control of the actin cytoskeleton is critical to many Chelators of copper and zinc both disa K t A ‘ E o Iﬁwﬂ )&“M
cellular functions; members of the Rho subfamily of small GTP from post-modem human brain and al i ﬁbiaﬁa: p13 dipt3t8* CD 3‘ If git/3353:)” AShIey l' BUSh Q’aki";
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family of Rho proteins. While most Rho GEFs have a single Dbl com .leted a Phapseu; clilns' alrtetir|ed Elngbioticlegd h recently a) C is hit? 5'?an I'I av, p" 5 003 43"}:
homology (DH) domain, Kalirin and Trio define a small family of P ica net in z ei e. D D _l iiakﬁ" Jami
structurally related dual GEF proteins facilitating the coordinate 3-00 ' ' \ ' 3’5“? Si; Riff- 5 W.

. . . 1 . pm. Reception and Meet With 8 akers Atrium " ‘9‘ M” - ‘ *5 4:31.43:
regulation of multiple Rho family members. In addition to their (Room 1-65), William T. Youpn Library :I’ggﬁjiﬁﬁ Department Of ChemlStry ‘i’yé‘f:
two DH domainsaboth have a Sec14p domain. 9 spectrin-Iike re- ° Vii??? University Of KentUCk :fm;
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epa men 0 emls ry, nlverSIty o entucky :3
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1 Friday, April 18, 2003 9:00 am. 3’3
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Susumu Tonegawa, Whitehead Professor of Biology and Neuro- ‘gqéfgc‘r’
.yj science, Departments of Biology and Brain and Cognitive Sciences; 3333?;
1 Director, Center for Learning and Memory; Investigator, Howard 335?},35 ””3;
‘ Hughes Medical Institute Investigator; Director of the RIKEN-MIT Neu- ;, 3353* L»,
roscience Research Center. Susumu Tonegawa received his Ph.D. in {i} ’mag‘“
-; Molecular Biology from the University of California, San Diego. After 33%};3373
j - postdoctoral training at the Salk Institute, he joined the Basel Institute for £04».
I . Immunology. In 1981, he was appointed as Professor of Biology at MIT :jffvz’vﬁt,
‘ " and a member of the Center for Cancer Research. In 1994, he founded ;:‘¢?§%s; 523';
,, ° the Picower Center for Learning and Memory at MIT. He is a recipient of 3:335;th
. the Louisa Gross Horwitz Prize, the Gairdner Foundation International $‘13’v:
2 Award, Order ofCuIture ”Bunkakunsho" from the Emperor ofJapan, Bristol igﬁé‘g‘ A”
i. Myers Squibb Prize in Cancer Research, the Albert and Mary Lasker *f‘gﬁ’
. Award, and the 1987 Nobel Prize in Physiology or Medicine. 5%:1‘
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Richard E. Mains, Professor and Chair, Department of Ashleyl. Bush, Director and Associate Professor of Psy- “gift/“:3 -.
5,- Neuroscience, University of Connecticut Health Center. chiatry, Massachusetts General Hospital and Harvard ﬁxes: ,
E, Ph.D., Harvard University, 1973; Helen Hay Whitney Post- Medical School. MD, University of Melbourne, 1982; ,.i‘s§:.g’3§'~i
é . . . xx”- 73* '4“; .
g doctoral Fellow, University of Oregon, 1973-75; Assrstant D.P.M., University of Melbourne, 1988; Ph.D., Unrversrty of fgfggsgggqug
f Professor/Associate Professor, Physiology, University of Melbourne, 1992; Victorian Medical Postgraduate Founda- g‘wﬁﬁ
fColorado Health Science Center, 1975-83; Professor, De- tion Research Award, 1986; National Health and Medical 635;:th
3 partment of Neuroscience and Physiology, 1983-00; Vincent Research Council Postgraduate Medical Scholarship, 1989- ’r’i .3 {it
Du Vigneaud Award for Peptide Research by Young lnves- 92; Harkness Fellowship, Commonwealth Fund of NY, 1992- 3335;333:3333?
tflgators, American Peptide Society, 1984; Ernst 93; Organon Psychiatric Research Award, 1994; Ellison @3333“?
{éOppenheimerAward Endocrine Society,1986; Merit Award Scholarship, 1994-95; Paul Beeson Physicians Faculty 3’19“
5 DK-32948, National Institutes of Health, 1990; William Scholar Award, 1995-98; Alzheimer Association Hatfield “E“, ,3
Beecher Scoville Chair of Neuroscience, University of Con- Award, 2000; American Board of Psychiatry & Neurology: 33:13
5; necticut Health Center, 2000; Member: American Society Certification in Psychiatry, 1997; Member, Pfizer Specialist 335$
for Cell Biology, Endocrine Society, American Society for Advisory Council, AHAFNatlonal Council. Associate Editor, ,éggr“
Cell Biology. Journal of Alzheimer's Disease (2000-01). (fig... 3?";
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Free parking available at the William T. Young Library in the Visitor Parking Lot on Hilltop Avenue. Additional parking (for a fee) gaggf‘vjv‘u,
available in UK Medical Plaza Parking Garage, located approximately one block south of the Chemistry-Physics Building; this #33341. ,
garage can be accessed from both Rose and Limestone Streets - look for Medical Plaza Parking signs. For additional informa- x33 g
f tion, call Professor Tae H. Ji, Department of Chemistry, (859) 257-3163 or by e-mail (tji@uky.edu). :3; my;
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f 2003 Committee: Tae H. Ji, Chair (Chemistry), Robert B. Grossman (Chemistry), Greg A. Gerhardt (Anatomy and Neurobiology) fﬁgfgfg,
Symposium supported by the Anna S. Naff Endowment Fund 331%:
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