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<TITLE>UMKC SBS MBB Doctoral Faculty</TITLE>
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<P><!--Created by Dorin-Bogdan Borza in Nov. 1995--><A HREF="sbshome.html"><IMG SRC="gif/sbslogo.gif" ALT="[SBS Home]" HSPACE=10 HEIGHT=97 WIDTH=103 ALIGN=LEFT></A></P>
<ADDRESS>School of Biological Sciences<BR>
University of Missouri-Kansas City<BR>
103 Biological Sciences Building<BR>
5007 Rockhill Road<BR>
Kansas City, Missouri 64110</ADDRESS>
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<H1 ALIGN=CENTER>Doctoral Faculty<BR>
Molecular Biology and Biochemistry</H1>
<TABLE BORDER="0" CELLSPACING=0 CELLPADDING=0>
<TR><TD><BR></TD><TD>&nbsp;<A HREF="sRec04.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Carlson">Gerald M. Carlson</A>, Head</TD></TR>
<TR><TD><BR></TD><TD>&nbsp;<A HREF="sRec26.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A></TD><TD>&nbsp;<A HREF="#Bame">Karen Bame</A></TD></TR>
<TR><TD><A HREF="http://sgi.bls.umkc.edu/funnylab/"><IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=11 HEIGHT=12 BORDER=0></A></TD><TD>&nbsp;<A HREF="sRec18.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Crawford">Douglas Crawford</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec27.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Gorski">Jeffrey P. Gorski</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec23.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Hirschberg">Rona Hirschberg</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec38.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Huang">Chi-ming Huang</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec11.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#LHF">Lindsey Hutt-Fletcher</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec35.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Iriarte">Ana J. Iriarte</A></TD></TR>
<TR><TD><A HREF="http://www.umkc.edu/gfr/rm"><IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=11 HEIGHT=12 BORDER=0></A></TD><TD><BR></TD><TD>&nbsp;<A HREF="#MacQuarrie">Ronald A. MacQuarrie</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec36.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Mattingly">Joseph Mattingly</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec17.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Morgan">William T. Morgan</A></TD></TR>
<TR><TD><A HREF="http://sgi.bls.umkc.edu/sjmorris/"><IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=11 HEIGHT=12 BORDER=0></A></TD><TD>&nbsp;<A HREF="sRec14.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Morris">Stephen J. Morris</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec39.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Popov">Kirill M. Popov</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec08.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Rider">Virginia Rider</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec10.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Schaefer">Michael R. Schaefer</A></TD></TR>
<TR><TD></TD><TD>&nbsp;<A HREF="sRec32.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#Smith">Ann Smith</A></TD></TR>
<TR><TD><A HREF="http://cctr.umkc.edu/user/kthomas/index.html"><IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=11 HEIGHT=12 BORDER=0></A></TD><TD>&nbsp;<A HREF="sRec15.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0></A>&nbsp;</TD><TD>&nbsp;<A HREF="#KThomas">W. Kelley Thomas</A></TD></TR>
</TABLE>
<P><HR></P>
<H2><A NAME="Carlson"></A>Gerald M. Carlson</H2>
<P><A HREF="sRec04.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Marion Merrell Dow Missouri Professor and Head <BR>
Ph.D., Iowa State University<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 505 BSB<BR>
Phone: (816) 235-2235<BR>
E-mail: <A HREF="mailto:carlsongm@umkc.edu">carlsongm</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A> and <A HREF="gstuddir.html">Graduate Students</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Structure/function of phosphorylase kinase and its relationship to other protein kinases </LI>
<LI>Calmodulin and its protein targets; protein-protein interactions <LI>Chemical crosslinking </LI>
<LI>Control of energy metabolism in muscle and liver </LI><LI>Phosphoenolpyruvate carboxykinase and gluconeogenesis </LI>
</UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
Phosphorylase kinase (PhK), an enzyme of the cascade activation of glycogen breakdown, is among the most complex and largest enzymes known. Of its 1.34 million Da mass, 90% has a regulatory role. Through allosteric sites on its 3 regulatory subunits, PhK integrates metabolic (ADP), hormonal (cAMP and Ca<SUP>2+</SUP>) and neural Ca<SUP>2+</SUP>) signals, resulting in large changes in its activity. This activity change in response to diverse physiological signals allows for the tight control of glycogenolysis, and subsequent energy production, e.g. in skeletal muscle PhK activation by Ca<SUP>2+</SUP> couples contraction with energy production to sustain contraction.<BR>
We are determining, using a variety of approaches, the mechanisms for how these different signals alter intersubunit interactions and activity of PhK. Two-hybrid genetic screening, protein crosslinking and synthetic peptides are used to identify interacting regions of adjacent subunits. Immunoelectron microscopy with monoclonal antibodies is used to localize regions of subunits within PhK's overall tetrahedral structure. Immunochemistry and chemical modification are used to identify regions of the protein that are influenced by the allosteric effectors. Site-directed mutagenesis is used to define interacting residues between subunits and to introduce report groups.
This work will help define the relationship between quarternary structure and control of activity for this important regulatory enzyme of mammalian energy production.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This research is supported by a grant from the National Institutes of Health.
<HR>
<H2><A NAME="Bame"></A>Karen Bame</H2>
<P><A HREF="sRec26.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor<BR>
Ph.D., University of California-Los Angeles<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 407 BSB<BR>
Phone: (816) 235-2243 <BR>
E-mail: <A HREF="mailto:bamek@umkc.edu">bamek</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Metabolism of heparan sulfate proteoglycans in animal cells </LI>
<LI>Enzyme characterization and purification </LI>
<LI>Characterization of cleaved heparan sulfate glycosaminoglycans </LI>
</UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
My research uses genetic and biochemical techniques to study the catabolism of heparan sulfate proteoglycans in Chinese hamster ovary (CHO) cells. Proteoglycans are complex macromolecules found at the cell surface which act as receptors, are involved in cell-cell interactions, and promote or inhibit cell growth. Heparan sulfate proteoglycans at the cell surface are internalized, and the glycosaminoglycan chains are removed from the protein core and cleaved into smaller pieces by heparanases. Most of the cleaved glycosaminoglycans are completely degraded; however, some are secreted from the cell or are transported to other cellular locations, suggesting that, in addition to its role in proteoglycan degradation, chain cleavage may produce biologically active glycosaminoglycans.We have purified three different heparanase activities from CHO cells, suggesting that there may be a family of these enzymes responsible for heparan sulfate catabolism. We are now purifying the activities from rat liver to generate the quantities of protein necessary for sequencing, and use this information to clone the heparanase gene(s) from CHO cells. The ultimate goal of these experiments is to express the heparanase protein so that we can characterize the reaction mechanism.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This work is supported by the National Science Foundation, the University of Missouri Research Board, and Repligen Corp.
<HR>
<H2><A NAME="Crawford"></A>Douglas L. Crawford</H2>
<P><A HREF="sRec18.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Assistant Professor<BR>
Ph.D., Johns Hopkins University<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 416 SCB<BR>
Phone: (816) 235-2565 <BR>
E-mail: <A HREF="mailto:crawforddo@umkc.edu">crawforddo</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.<BR>
Laboratory <A HREF="http://sgi.bls.umkc.edu/funnylab/">HomePage <IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=22 HEIGHT=24 BORDER=0></A></P>
<H3>Research Areas</H3>
Molecular Evolution of Gene Expression
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
My research can be divided into two broad projects: (1) evolutionary variation in glycolysis: phylogenetic analyses of enzyme expression and its effect on metabolic flux and (2) analyses of promoter function and how natural sequence variation affects transcription.<BR>
We are quantifying the concentration of all ten glycolytic enzymes in heart ventricles from the different <I>Fundulus</I> populations and species and determining how this variation affects cardiac glycolytic flux. We then experimentally alter enzyme expression to quantify how this variation affects metabolism. These projects, combining phlyogenetic analyses of a physiological trait (glycolysis) with experimental assays, are an example of how my laboratory combines functional and evolutionary analyses.<BR>
Variation in mRNA transcription is an important evolutionary adaptation. My laboratory is interested in the molecular mechanisms responsible for this variation and are focusing our efforts on the <I>Ldh-B</I> promoter. There is considerable sequence variation in <I>Ldh-B</I> proximal promoter. Molecular analyses of this variation indicate that specific substitutions affect transcription processes. Evolutionary analyses indicated that the proximal promoter, specifically the nucleotide that affects transcription, is evolving by directional selection. This research has provided insights into the regulation of gene transcription that are not available from the study of standard laboratory organisms or synthetic promoters.
<HR>
<H2><A NAME="Gorski"></A>Jeffrey P. Gorski</H2>
<P><A HREF="sRec27.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor<BR>
Ph.D., University of Wisconsin-Madison<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 311 BSB <BR>
Phone: (816) 235-2537 <BR>
E-mail: <A HREF="mailto:gorskij@umkc.edu">gorskij</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
Woven bone represents primary bone formed directly from mesenchymal derived osteoblastic precursors in the absence of a calcified cartilage anlagen. Woven bone is rapidly formed in situations of elevated biomechanical strain or after surgical stimulation, e.g., long bone growth and development, strenuous exercise, and fracture. Resorption of woven bone occurs following fracture, after stress, during estrogen deficiency, and after loss of weight bearing (microgravity). Our working hypothesis proposes that the molecular composition of woven bone, as well as the responsiveness of osteoblasts synthesizing woven bone to stimuli, is different from that for more slowly synthesized lamellar bone, implying the existence of distinctive osteogenic mechanisms. The osteoid or extracellular matrix of woven is specifically enriched in bone sialoproteins bone acidic glycoprotein-75 and bone sialoprotein. Due to their restricted distribution and unusual structure, these bone sialoproteins are believed to mediate at least some of the unusual characteristics of woven bone. Our overall research focus is mechanisms controlling key events in the development, maturation, and normal or pathologic degradation of woven bone or primary bone. Projects underway seek to determine the function of osteoblast precursor and osteoblast cell surface and secreted components in formation, mineralization, and resorption of woven bone. In particular, bone acidic glycoprotein-75 is a target of molecular biological, cell biological, and genetic studies.
<HR>
<H2><A NAME="Hirschberg"></A>Rona Hirschberg</H2>
<P><A HREF="sRec23.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor and Associate Dean<BR>
Ph.D., University of Wisconsin- Madison<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 012 BSB<BR>
Phone: (816) 235-2596 <BR>
E-mail: <A HREF="mailto:hirschbergr@umkc.edu">hirschbergr</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Molecular biology</LI>
<LI>Microbiology</LI>
<LI>Molecular aspects of microbial pathogenicity</LI></UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
I am a microbiologist-molecular biologist. My research interests focus around two general themes: unusual bacteria and regulation of gene expression.<BR>
The primary research project in my lab is &quot;Pilin Genes and Their Role in Pathogenesis of <I>Eikenella corrodens</I>.&quot; This organism is associated with periodontal diseases. We would like to understand the role pili may play in attachment of the organism in the mouth and generation of subsequent problems. We are using a combination of molecular genetic, immunological, and animal studies to address these questions.<BR>
We have also identified cytotoxic effects produced by this organism. In the future we want to study this and investigate its role in pathogenesis. I am also interested in oral spirochetes.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This research is supported by a grant from the National Institutes of Health (National Institute of Dental Research).
<HR>
<H2><A NAME="Huang"></A>Chi-ming Huang</H2>
<P><A HREF="sRec38.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor<BR>
Ph.D., UCLA<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: M3-202 <BR>
Phone: (816) 235-2582 <BR>
E-mail: <A HREF="mailto:huangc@umkc.edu">huangc</A></P>
<H3>Research Areas</H3>
<UL><LI>Neurobiology of aging</LI>
<LI>Structural and functional aspects of age-related neurodegeneration and neuroplasticity</LI></UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
In the expanding elderly population, falls and movement-related accidents diminish sharply the quality of their lives and impose serious medical and economical consequences onto our society. Hip fracture in US alone is estimated at 6-10 billion dollars a year and is a major contributing factor leading to death in older people. Precise causes of motor function deterioration are multiple and complex but many lines of evidence have implicated the decline of central motor control as a major factor. Our overall aim is to advance understanding of this neurodegeneration. Specifically, we are investigating the age-related loss of cerebellar motor function.<BR>
In the cerebellar cortex, synapses between granule cells and Purkinje cells are strategic elements in its neuronal circuitry. These synapses, however, are vulnerable while exposed to mitochondrial oxidative stress, glutamate neurotransmission, and nitric oxide -- all recognized risk factors of age-related neurodegeneration. Our lab was among the first to document the dramatic vulnerability of cerebellar synapses during aging, which is more severe than most other brain structures. We anticipate future studies will lead to elucidation of underlying mechanisms as well as the design of rational therapeutic means for intervention.<BR>
Our research emphasizes both technology and concepts, employing a variety of interdisciplinary approaches. Interested students should expect training in a broad spectrum of theoretical as well as practical aspects of independent research.
<HR>
<H2><A NAME="LHF"></A>Lindsey Hutt-Fletcher</H2>
<P><A HREF="sRec11.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Professor<BR>
Ph.D., University of London<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 214 BSB <BR>
Phone: (816) 235-2575 <BR>
E-mail: <A HREF="mailto:huttfletcher@umkc.edu">huttfletcher</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A> and <A HREF="gstuddir.html">Graduate Students</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Virus cell interactions</LI>
<LI>Virus pathogenesis</LI></UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Long standing research interests are in virus cell interactions, virus pathogenesis and immune responses to viruses. The major focus of current work is on the pathogenesis and virology of Epstein-Barr virus (EBV), a ubiquitous human herpesvirus that establishes persistent infections in almost 100% of the world's population. Most people are infected subclinically with EBV in childhood. However, the virus also causes infectious mononucleosis and oral hairy leukoplakia and is strongly implicated in the pathogenesis of Burkitt's lymphoma, nasopharyngeal carcinoma, immunoblastic lymphomas of the immunosuppressed and some types of Hodgkin's Disease. We are studying how EBV enters and traffics between cells by determining the biochemical and functional characteristics of the virus proteins involved. Most recently we have determined that EBV uses HLA class II as a second receptor for entry into B cells and have identified the virus glycoprotein that is responsible for this interaction. A major effort is underway to derive viruses deleted for the expression of individual glycoproteins to explore the role(s) of each and to identify those which are essential for either entry into or egress from different cell types.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This research is supported by the National Institutes of Health.
<HR>
<H2><A NAME="Iriarte"></A>Ana J. Iriarte</H2>
<P><A HREF="sRec35.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor<BR>
Ph.D., University of Navarre, Spain<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 422 SCB <BR>
Phone: (816) 235-2259 <BR>
E-mail: <A HREF="mailto:iriartea@umkc.edu">iriartea</A></P>
<P>Laboratory <A HREF="faculty.html#MBB">Research Faculty</A>, <A HREF="pdocdir.html">Research Staff</A> and <A HREF="gstuddir.html">Graduate Students</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Enzyme structure and relationship of enzyme structure to function</LI>
<LI>Mechanisms of processing and transport of proteins across membranes</LI>
<LI>Protein folding and the role of molecular chaperones</LI></UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
Our research interests are focused on the analysis of protein folding mechanisms, protein structures in their native state, and the structural consequences of introducing alterations at selected regions in a protein. In this manner, strategic regions of a protein can be investigated as to their influence in maintaining protein structural stability and function as well as on its folding into the proper native conformation. We have
selected for our studies proteins which are well characterized structurally, the two isoenzymes of aspartate aminotransferase. The mechanisms of recognition, binding and translocation of proteins across biological membranes are also being investigated using as model the mitochondrial precursor of this protein. Our main interest resides on the study of the precursor structural requirements for import into mitochondria and the events associated with the initial interaction of the translocated protein with the membrane. The role of
certain heat shock proteins working as &quot;molecular chaperones&quot; in this translocation process as well as in the proper folding and assembly of the two isozymes is also being investigated.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This research is supported by grants from the National Institutes of Health.
<HR>
<H2><A NAME="MacQuarrie"></A>Ronald A. MacQuarrie</H2>
<P><BR>Professor<BR>Dean, School of Graduate Studies<BR>
Vice-Provost for Research<BR>
Ph.D., University of Oregon<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 342 AC<BR>
Phone: (816) 235-1301 <BR>
E-mail: <A HREF="mailto:macquarrie@umkc.edu">macquarrie</A></P>
<P>Professional <A HREF="http://www.umkc.edu/gfr/rm">HomePage <IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=22 HEIGHT=24 BORDER=0></A></P>
<H3>Research Areas</H3>
<UL><LI>Biochemistry</LI>
<LI>Structure and regulation of enzymes</LI>
<LI>Signal transduction mechanisms</LI>
<LI>Membrane structure and function</LI></UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
The major research project in this laboratory is concerned with the mechanisms of signal transduction across biological membranes. It is well established that cyclic processes of synthesis and degradation of membrane
phospholipids occur in response to certain physiological stimuli, including some which are initiated by hormones, neurotransmitters and growth factors. These processes originate with stereospecific binding to receptors on the
cell surface, followed by the release of potent regulators (second messengers) within the cell. These regulators include diacylglycerol, arachidonic acid, inositol triphosphate and lysophospholipids, all of which have diverse
effects on cellular activities. The long-range plan of this project is to elucidate the molecular details of the relationship between phospholipid metabolism and the transmission of these signals across the membranes.
Studies are underway to determine the properties and control of phospholipases and acyltransferases, which catalyze key reactions in the sequence of events leading to a cellular response. Some of these enzymes have been isolated and their properties studied and correlated with the known characteristics of biological membranes. Other aspects of this project are designed to determine how these enzymes are linked to the action of cell-surface receptors, and to determine the mechanism by which phospholipid-derived second messengers influence cell functions.
<HR>
<H2><A NAME="Mattingly"></A>Joseph Mattingly</H2>
<P><A HREF="sRec36.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Assistant Professor<BR>
Ph.D., University of Notre Dame<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 421 SCB <BR>
Phone: (816) 235-2258 <BR>
E-mail: <A HREF="mailto:mattinglyj@umkc.edu">mattinglyj</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Mechanism of the the hsp60 chaperonin family
<LI>Structure function relationships in the 14-3-3 protein family</UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Macromolecular interactions, particularly the mechanisms of protein folding and the basis for molecular chaperone selectivity in facilitating intracellular protein folding.
<HR>
<H2><A NAME="Morgan"></A>William T. Morgan</H2>
<P><A HREF="sRec17.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Professor<BR>
Ph.D., University of California-Santa Barbara<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 314 BSB <BR>
Phone: (816) 235-2587 <BR>
E-mail: <A HREF="mailto:morganwt@umkc.edu">morganwt</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Protein structure-function relationships</LI>
<LI>Regulation of blood clot formation and breakdown</LI>
<LI>Spectroscopic and biochemical analysis of ligand-protein and protein-receptor interactions</LI>
<LI>Use of monoclonal antibodies and site-directed mutagenesis to probe protein mechanisms of action</LI></UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
The transport of heme by hemopexin to tissues like liver is a specific, membrane receptor-mediated process. As a result, biologically useful iron is conserved and the accumulation of toxic heme is prevented. Our ultimate aim is to delineate the biochemical mechanisms of heme transport by hemopexin from initial binding of heme in the circulation to the specific interaction of hemopexin with its plasma membrane receptor. To attain this goal, a basic approach is being taken in which the hemopexin molecule and its receptor are being characterized in detail using physical, immunochemical and molecular biological techniques, e.g. site-directed mutagenesis of hemopexin and molecular cloning of the receptor.<BR>
Histidine-proline-rich glycoprotein (HPRG) is distinguished by its ability to interact with a variety of molecules involved with blood clot formation and breakdown. HPRG binds heparin and fibrinogen and modulates the activation of plasminogen by tissue plasminogen activator. The biological function of HPRG in hemostasis is being defined using physical, immunochemical and molecular biological techniques to characterize the ligand-binding functional domains of HPRG and to define its mechanisms of action in hemostasis. The current paradigm is that HPRG acts in plasminogen activation at the surfaces of endothelial cells, platelets or fibrin aggregates, and that HPRG is regulated by localized changes in pH, such as occur in ischemia or hypoxia. This information should aid the development of improved diagnostic and therapeutic measures in blood clotting.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This work is supported by grants from the National Institutes of Health, the American Heart Association, and the University of Missouri Research Board.
<HR>
<H2><A NAME="Morris"></A>Stephen J. Morris</H2>
<P><A HREF="sRec14.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Professor <BR>
Ph.D., Neurological Sciences, Stanford Medical School<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 412 BSB <BR>
Phone: (816) 235-2592 <BR>
E-mail: <A HREF="mailto:sjmorris@umkc.edu">sjmorris</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.<BR>
Laboratory <A HREF="http://sgi.bls.umkc.edu/sjmorris/">HomePage <IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=22 HEIGHT=24 BORDER=0></A></P>
<H3>Research Areas</H3>
Cell biology, cell biophysics, and digital imaging video microscopy. (Mechanisms of storage and release of neurotransmitters and neuromodulators; receptor-second messenger signal transduction; coincident signalling; viral protein catalyzed cell-cell fusion; intracellular ion activities).
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Besides typical cell biology methodology, we rely upon visualization of vital dyes in living cells using digital video microscopy. There are three main projects:
<OL><LI>The coupling of neurotransmitter receptors to inhibition of high voltage activated Ca<SUP>2+</SUP> channels.
<LI>Cell-cell fusion initiated by viral spike glycoproteins.
<LI>Rapid kinetics of cellular activities resolved by multi-parameter video imaging.</OL>
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This work is supported by grants from the National Science Foundation, the American Heart Association, and the Loeb Charitable Foundation.
<HR>
<H2><A NAME="Popov"></A>Kirill M. Popov</H2>
<P><A HREF="sRec39.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<P>Assistant Professor<BR>
Ph.D., Moscow State University, Russia<BR>
Office: SCB 415<BR>
Phone: (816) 235-2595<BR>
E-mail: <A HREF="mailto:popovk@umkc.edu">popovk</A></P>
<H3>Research Areas</H3>
<UL><LI>Molecular mechanisms of enzyme regulation by hormones
<LI>Protein/protein interactions
<LI>Molecular basis for isoenzyme functions</UL>
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
To survive, all living organisms have to burn some respiratory fuels. In humans, the average modern diet provides about 45-50% of total fuel mix in the form of carbohydrates, 33-43% as fat and 13-17% as protein. In well-oxygenated tissues the major determinant of carbohydrates oxidation seems to be the activity of the mitochondrial pyruvate dehydrogenase complex (PDC), which commits carbohydrates to further catabolism. This reaction is heavily regulated by a variety of nutritional and hormonal stimuli and two dedicated enzymes--pyruvate dehydrogenase kinase (PDK) that phosphorylates and inactivates PDC and pyruvate dehydrogenase phosphatase (PDP) that dephosphorylates and re-activates PDC. Thus the amount of active, dephosphorylated PDC in any particular tissue is coordinated. To complicate matters even further, it appears that, in humans, there are multiple isoenzymes of PDK and PDP and almost every tissue has its own subset of isoenzymes that differ in their properties and regulation. The objectives we currently pursue are: 1) to understand how both PDK and PDP function at the atomic level and how they manage to integrate a variety of metabolic stimuli; 2) to understand the molecular mechanisms responsible for regulation of kinase and phosphatase activities by hormones; and 3) to evaluate the molecular basis for abnormal regulation of PDC observed in diabetes, ischemia and sepsis.</P>
<P><B><FONT SIZE="+1">Research Support</FONT></B><BR>
This research is supported by a grant from the National Institutes of Health.</P>
<HR>
<H2><A NAME="Rider"></A>Virginia Rider</H2>
<P><A HREF="sRec08.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor<BR>
Ph.D., Arizona State University<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 215 BSB <BR>
Phone: (816) 235-2065 <BR>
E-mail: <A HREF="mailto:riderv@umkc.edu">riderv</A></P>
<P>Laboratory <A HREF="gstuddir.html">Graduate Students</A>.</P>
<H3>Research Areas</H3>
Molecular and cellular actions of estrogens and progestins in female reproduction and disease.
<P><B><FONT SIZE="+1">Current Interests</FONT></B><BR>
Estrogen and progesterone are steroid hormones that regulate a variety of cellular processes in target tissues by altering the rates of specific gene transcription. Current interests in the laboratory are focused on the mechanisms involved in hormone action at the cellular and molecular levels.<BR>
Progesterone is the only steroid hormone that is essential for the establishment of pregnancy in all mammalian species studied, but its mechanisms of action on target cells are poorly understood. The main focus of my laboratory is to provide greater insight into the question of how progestins control proliferation in normal target cells. Increased knowledge about the mechanisms of progesterone action will impact human, domestic animal and vertebrate wildlife reproduction.<BR>
Systemic <I>lupus erythematosus</I> (SLE) is an autoimmune disease that occurs more frequently in women of childbearing age (9:1 compared to men). We are studying the role of sex hormones in promoting immunological-inflammatory responses in autoimmune diseases using SLE as the model system. Recently we showed that calcineurin, a key player in T cell activation, increases significantly in response to estradiol in cultured lupus T cells but not in T cells from normal healthy women. Estradiol-dependent increases in calcineurin expression are postulated to alter the transcription of proinflammatory cytokine genes and molecules involved in T-B cell interactions
<HR>
<H2><A NAME="Schaefer"></A>Michael R. Schaefer</H2>
<P><A HREF="sRec10.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Assistant Professor <BR>
Ph.D., Texas A&amp;M University<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 213 BSB <BR>
Phone: (816) 235-2573 <BR>
E-mail: <A HREF="mailto:schaeferm@umkc.edu">schaeferm</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A> and <A HREF="gstuddir.html">Graduate Students</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Photoregulation of gene expression and cellular processes in cyanobacteria</LI>
<LI>Molecular mechanisms of bacterial sensory perception and signal transduction</LI></UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Light is a critical environmental factor for photosynthetic organisms. In addition to driving photosynthesis, it provides the information necessary for acclimation and development in response to changes in ambient conditions. Most photosynthetic organisms can modulate their photosynthetic capacity to accommodate fluctuations in light availability. Often, genes that encode components of the photosynthetic apparatus are under the control of wavelength-specific photoreceptors that initiate light-responsive signal transduction pathways. Although photoregulation of gene expression is well documented for different phototrophs, the molecular mechanisms by which photoreceptors communicate with the regulatory machinery of cells are not.<BR>
We seek to define the photoregulatory mechanism controlling chromatic adaptation by the cyanobacterium <I>Fremyella diplosiphon</I>. Chromatic adaptation is the process by which this organism senses changes in light quality and responds by altering the protein and pigment composition of the light-harvesting phycobilisome. Two approaches are being used to identify genes involved in chromatic adaptation. Both approaches are based on a collection of pigment mutants characterized by aberrant chromatic adaptation or altered phycobilisome structure. The first approach involves complementation of the different pigment mutants with a wild-type genomic DNA library. The second approach involves transposon-tagging of chromatic adaptation genes with endogenous transposon Tn<I>5469</I>. By characterizing the identified genes, a molecular framework for the chromatic adaptation photosensory and signaling mechanisms can be established.
<HR>
<H2><A NAME="Smith"></A>Ann Smith</H2>
<P><A HREF="sRec32.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Associate Professor <BR>
Ph.D., University of London, U.K.<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 313 BSB <BR>
Phone: (816) 235-2579 <BR>
E-mail: <A HREF="mailto:smithan@umkc.edu">smithan</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A>.</P>
<H3>Research Areas</H3>
<UL><LI>Coordinate and differential regulation of expression of proteins including heme oxygenase, hemopexin and metallothionein by heme, its iron and reactive oxygen species to maintain cellular homeostasis by cells in response to changes in intracellular heme and iron</LI>
<LI>Heme transport in liver, eye, the peripheral and central nervous systems</LI>
<LI>Receptor-mediated endocytosis of the antioxidant heme binder and transporter hemopexin</LI>
<LI>Structure-function relationships in ligand-protein and protein-receptor interactions</LI></UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Transferrin and hemopexin are a specific class of endocytotic systems where the transport protein recycles and the ligands, iron and heme, respectively, are bound to specific membrane proteins to facilitate the intracellular transport of these chemically-reactive, water-insoluble molecules. Hemopexin-mediated heme transport and sequestration of heme to minimize heme-mediated oxidative damage are important in the liver, placenta, eye, regenerating nerves and the central nervous system.<BR>
Most recent studies using micromolar concentrations of heme-hemopexin as a model for intravenous heme released in hemolysis, trauma and ischemia-reperfusion injury show a transient increase in cellular oxidation state associated with heme transport. The N-terminal c-Jun kinase also known as stress activated protein kinase (JNK/SAPK) is activated and hemopexin also induces the cyclin inhibitor p21<FONT SIZE="-1"><SUP>WAF/CIP1/SDI1</SUP></FONT> and the tumor suppressor p53 causing partial G2/M arrest not necrosis or apoptosis.<BR>
The emerging picture is that hemopexin is a cell survival factor leading also to the nuclear translocation of the transcription factor NFkB involved in the innate immune response. The hemopexin system is being used to define at the molecular level the pathway from the plasma membrane to the nucleus for protective gene regulation in response to this extracellular signal of danger via the hemopexin receptor.
<P><FONT SIZE="+1"><B>Research Support</B></FONT><BR>
This work is supported by grants from the National Institutes of Health.
<HR>
<H2><A NAME="KThomas"></A>W. Kelley Thomas</H2>
<P><A HREF="sRec15.html"><IMG ALT="see my slide" SRC="gif/slide.gif" WIDTH=18 HEIGHT=16 BORDER=0><FONT SIZE="1"> slide picture</FONT></A>
<BR>Assistant Professor <BR>
Ph.D., Simon Fraser University<BR>
<A HREF="faculty.html#MBB"><IMG ALT="address + phone" SRC="gif/mail.gif" WIDTH=28 HEIGHT=15 BORDER=0>
Office</A>: 216 BSB <BR>
Phone: (816) 235-2599 <BR>
E-mail: <A HREF="mailto:thomaske@umkc.edu">thomaske</A></P>
<P>Laboratory <A HREF="pdocdir.html">Research Staff</A> and <A HREF="gstuddir.html">Graduate Students</A>.</P>
<P><A HREF="http://cctr.umkc.edu/user/kthomas/index.html"><IMG ALT="visit my homepage" SRC="gif/home.gif" WIDTH=22 HEIGHT=24 BORDER=0> Laboratory</A> and
<A HREF="http://cctr.umkc.edu/user/kthomas/kt.html">Personal</A> HomePage</P>
<H3>Research Areas</H3>
<UL><LI>Mechanisms of evolutionary change</LI>
<LI>Molecular systematics of animals</LI>
<LI>Molecular estimation of genetic diversity</LI>
<LI>Conservation genetics</LI></UL>
<P><FONT SIZE="+1"><B>Current Interests</B></FONT><BR>
Our research investigates evolution at the molecular level with the goal of elucidating relationships among organisms and understanding the processes of genome evolution.
<BR>Recently, we have begun to employ the nematode (<I>C. elegans</I>) as a model organism for studies in evolution. <I>C. elegans</I> has become a useful model system for many areas of biology (e.g. reproduction, development, morphogenesis, neurobiology and genome organization). One of the first goals of our research is to determine the relationship of this famous nematode to other animals and provide a valuable evolutionary framework upon which our ever increasing knowledge of <I>C. elegans</I> can be placed. The phylum Nematoda, also called roundworms, is comprised of the most abundant, ubiquitous and genetically diverse multicellular organisms in the world. However, fundamental studies of evolution, ecology and biodiversity are dramatically impeded by an often inefficient system for the identification of individual nematodes and a vastly incomplete taxonomic inventory. One of the goals of this laboratory is to develop molecular tools for species identification.
<BR>Another area of investigation focuses on the role of genes important for controlling the rate of mutation and genome evolution, specifically, the mismatch repair genes and their role in maintaining replication fidelity in microsatellite loci.
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