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2005 PROGRAM $34.12;, iffl Thirty-Second Annual {2:333 1;?
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8:15 am. Registration and Continental Breakfast, 2:00 pm. Dr. John R. Yates, The Scripps Research lnsti- {,4 1:929:91; gtt Na SympOSlum on tit-"2"? 295;}. 'L"
Atrium (Room 1-65), William T. Young Library tute it? t ght? 35: .2
. "Mass Spectrometry Analysis of Large CeIIu- $123443. "15" {45};
9:00 am. Welcome by Dr. Steven W. Yates, Chairman, Iar Structures" 1,,  f" 124} Chem istr ?T,e"1:;t'
Department of Chemistry, University of Ken- W501 y M'w
tucky - Auditorium (Room 1-62), William T, A component to understanding biological processes in- i if? git:
Young Library volves identifying the proteins expressed in cells as well as knelt; & 31:43:;May." 4.
their modications and the dynamics of processes. Several 95",? " :Miwrff. a???
9:05 am. Introductory Remarks - Dr. Bert C. Lynn, De- major technologies have beneted from large scale genome 3?? 2 ';
partment of Chemistry, University of Kentucky sequencing of organisms. The sequence data produced by 1 31 . 4,1 MOlecu Iar iiiw"
these efforts can be used to interpret mass spectrometry data {$91 33% 3 . :,_3;:1.MM.A$L:1
9:10 am. Dr. Richard M. Caprioli, Vanderbilt University of proteins and thus enables rapid and straightforward analy ;:_.?z_.w:%, ; BIOIO {91,1342 3M4;
"In situ Molecular Imaging and Proling of sis of protein data from experiments. Proteins separated by mi gy git-E1;
Proteins in Tissues Using Mass Spectrometry gel electrophoresis and 2-dimensional gel electrophoresis can 71-, 3.11% ,1 {V Hit:
in Biological and Clinical Research" now be rapidly identified enabling more comprehensive analy- W'f? {15} Er
Profiling and Imaging MALDI MS can be used to assess ses Of bochmical land molecua; biology experiments. Saw it"? 33 in"? 2";
.  g g . g . . . approac es ave aso emerge or pro ein aria ysrs suc as 35- .145; ,M 5,2, 34,1,
the Spatial distributionof peptides and proteins .' blolqgical direct identification of proteins in mixtures without gel separa- 31%,} 7 _, Mid-1;;
M. M  MM
 - g _  g 1 WI mm c roma ograp y irec y into tan em mass spec ."_":i.1,:r::'2-;M_I,,f; r:iitf,-..,,_ *1. 17,
peptides 30d proteins in selected areas 0t tissue to hlgh reso- trometers, sufcient information can be obtained to identify the ; 11 333141;? git 7 :sz if} 5
lution images 0t tissue cross sections. Usmg a raster 0f the peptides and subsequently the proteins present in the mixture. 5 3 gi , .3" W-aii
25541: surfacefby a/laselr beam, images ft Slamp'esE 3r: pro; As peptide mixtures become more complex better separation 621??" 3;; " 5:533:
uce In specr 3 m 7 V3 U851 0 ranges 0 Va ues. ac SPO techniques such as 2-dimensional Ii uid chromato ra h are 1:" 4s; [Wu-3 T.-  ,v'MMJ:
on the sample irradiated bY the laser is approximately 30-50 required to resolve the peptide cgmponents to;g aeiat/ysis. . effig'ytj 35:33.3; .,
microns In diameter and typically COVeTS the m/z range 1000 Technologies and methods of proteomics will be described tiftt . _ $3,: $2.1; ,
100.000- tndtthUet m/z values can then be assembled from and applications illustrated by discussing experiments to iden- 'r @3339." N established in the memory Of it?" ,' 341'?!
the [355 spectra t9 produce selectedlmlz images. Sections tify proteins, modications membrane proteins and membrane 7 :7.):{"4';irs g Anna S Naff :i'i ?".:L~j.:? a:
4 44 M... - 1'
2 ' ast e i o , o ian entrioewill aso edescri ed. n,-. 1? :1. -
sue. We have employed the technology in studies of a variety y g ggffiagfg3____ wag??? L; t
of diseases, including several types of cancers, neurodegen- 3:00 pm. Break (Refreshments Available) 3.3% ,ffgnii Mass Spectrometry of i, Eff-$49M. 21
erative diseases and kidney diseases, comparing proteins - .3194g: j 3' I . IS iftf'f}'~z: 3.
differentially expressed in diseased tissue with those in the 3220 pm. Dr. R. Graham Cooks, Purdue University L0 t;3'1f:.l,143{,': IO oglca YStems it"ia'itcwlitgfi't
corresponding normal tissue. This will be illustrated with stud- "Biological Mass Spectrometry: Metabolom- > L0 3 t 3,3" axis}; __ 3' 75 33%!
ies of breast tumor biopsies and also those for human ics, Tissue Imaging and Protein Separation" 5- >8 $3,, 4 11V; 1"
glioblastomas. In the latter, MS patterns have also been cor- . . . - x ' Rates (-3"? s. :15}; 744: 4,?
related with patient outcomes. This has been applied to a . Samples can be anatyzed 'n the ambient envrronment, g g 8 73353 SPEAKERS i, "
protocol termed histologydirected molecular analysis of tissue wl'thOUt any PeParet'oni I; \I/eryTshort times _usrng desorption _: .._. 8 '4 --;, ..:..
and biopsy specimens. Imaging MS has also been applied to :Ietr%sprayhionization (.D Sf )' his method '5 shown to allow 0 5 q- . 3:., Richard M Ca HO 5" {31 3
drug targeting and metabolic studies with analysis of specic '9 .t roug RU analys's 0 pharmaceutical preparations. It 5 X >_ 2??ng 1;:  p "
tissues after systemic drug administration. Whole animal 6450 '5 959M instudies 0f natural products and in-metabolom- H ~ 55 'frtern- 2,33: JOhn R- Yates vyxi
sagittal sections have been imaged to measure molecular :5 studies to differentiate closely related populations Of sam C O . if, a R Graham COOKS 4%
~ - - - . ~ ~ ples, such as urine samples from healthy and diseased am- (D > C ,Mj'f. - x 
changes in proteins in multiple organs and correlating this With , , E 3: 0 :MM W71. s12, 1... go .
drug concentrations in these same organs. mals. The DESI method can also. be used for direct tissue 4.. 2 4.. L} dig;
analysts, either for proteins or for lipids. In an unrelated ex- ('3 a, g) 3. ;. If," 1 (5.; f
10:10 am. Break (Refreshments Available) penment. mass spectrometwis used as a separation tool to <12 ->< Friday, March 31, 2006 2;
prepare and collect pure protein samples by ion soft landing. CD C a) 559% H" rut" if? (m ",4
10:45 am. Poster Session, Room CP-137, Chemistry- . D D 1 2 ":33. i i? 53 9.
Physics Building 4:20 pm. Closrng Remarks - Dr. Bert C. Lynn, Depart- Egg; 27$? .. w. 1.1 2::
ment of Chemistry, University of Kentucky g 1f: gatirisy Department of Chemistry W" 3
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11:45 am. Buffet L'unch, Alumni House [Please return 4 zit-3:733 "5 University of Kentucky gz;
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vations] (http:/lwww.chem.uky.edu/seminars/naff/welcome.html) @ eXIng OH, - 1:: .
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