Brad K. Bendiak, Ph.D.
Assistant Professor of Cellular & Structural Biology
Department of Cellular & Structural
Biology
University of Colorado at Denver and Health Sciences Center
RC1 South Tower, Room 12-113
P.O. Box 6511 MS 8108
Aurora, Colorado 80045
Phone: 303.724-3453
Brad.Bendiak@uchsc.edu
EDUCATION/EXPERIENCE
HONORS AND AWARDS
Research Interests
The information that regulates
the way in which cells recognize and respond to their neighbors resides at the
area of contact between them. Cell surface carbohydrates, either conjugated to
 proteins
or lipids, are major components of the cell surface and are now known to have
crucial roles in cellular recognition events, including mammalian embryonic development,
regulation and mediation of the immune response, and cytokine localization. Changes
in their structures have been shown to correlate with various cancer cell metastases
and inherited diseases. The research interests of my laboratory focus on:
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Elucidation of new oligosaccharide structures of glycoproteins using nuclear
magnetic resonance (NMR) spectroscopy and mass spectrometry (MS). This includes
the development of new methods in NMR spectroscopy/derivatization specifically
tailored to oligosaccharide structural elucidation, and new procedures in liquid
chromatography-MS/MS for separating and profiling oligosaccharides from mixtures
and identifying candidates involved in interactions with proteins.
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Studies of glycoprotein-protein interaction. Our current interests are in the
specificity of oligosaccharide-protein interactions in the brain.
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We are continuing development of a chemical method for sequential degradation
of oligosaccharides from the reducing end. This work also includes developments
in reducing end-group analysis and end-group-linkage analysis.
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Regulation of glycoprotein biosynthesis. An understanding of glycosylation
is essentially an understanding of the control of expression, localization in
the cell, and regulation of the activities of glycosyltransferases, most of which
reside in the Golgi apparatus. We are interested in a number of fundamental aspects
of glycoprotein construction, and the flexibility of the system for generating
variation in oligosaccharide structures in different cell types.
Ultimately, each cell type is capable of tailoring the synthetic
system to generate the specific oligosaccharides it requires; coordination of
the biosynthetic machinery in each cell type is currently poorly understood, yet
plays a critical role in defining the unique structures found on the surfaces
of different cell types.
Selected Publications
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Bendiak, B., and Fang, T.T. Sequential removal
of monosaccharides from the reducing end of oligosaccharides. 4. End-group determination
of oligosaccharides: a gas chromatography-mass spectrometry-mass spectrometry
method for distinguishing between all D-aldohexoses and D-ketohexoses. Carbohydrate
Res., 327, 463-481 (2000).
[Abstract]
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Jones, D.N.M. and Bendiak, B. Novel multi-dimensional
heteronuclear NMR techniques for the study of 13C-O-acetylated oligosaccharides:
Expanding the dimensions for carbohydrate structures. J. Biomol. NMR, 15: 157-168
(1999).
[Abstract]
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Bendiak, B. Nuclear magnetic resonance spectroscopy
of peracetylated oligosaccharides having 13C-labeled carbonyl groups in lieu of
permethylation analysis for establishing linkage substitutions of sugars. Carbohydrate
Res., 315, 206-221 (1999).
[Abstract]
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Martensson, S., Levery, S.B., Fang, T.T., and Bendiak,
B. Neutral oligosaccharides of bovine submaxillary mucin. Use of lead tetraacetate
in the cold for establishing branch positions. Eur. J. Biochem. 258, 603-622 (1998).
[Abstract]
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Bendiak, B., Salyan, M.E. and Pantoja, M.
Sequential removal of monosaccharides from the reducing end of oligosaccharides.
2. Fundamental studies of a reaction between hydrazine compounds and sugars having
a glycosyl moiety on a carbon adjacent to a carbonyl group. J. Org. Chem., 60,
8245-8256 (1995).
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D'Agostaro, G.A.F., Zingoni, A., Moritz, R.L., Simpson, R.J., Schachter, H.
and Bendiak, B. Molecular cloning and expression
of cDNA encoding the rat UDP-N-acetylglucosamine:a-D-mannoside b-1,2-N-acetylglucosaminyltransferase
II. J. Biol. Chem. 270, 15211-15221 (1995)
[Abstract]
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Bendiak, B., Ward, L.D., and Simpson, R.J.
Proteins of the Golgi apparatus: Purification to homogeneity, N-terminal sequence,
and unusually large Stokes radius of the membrane-bound form of UDP-galactose:
N-acetylglucosamine b1-4galactosyltransferase from rat liver. Eur. J. Biochem.
216, 405-417 (1993).
[Abstract]
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Cumming, D.A., Hellerqvist, C.G. Harris-Brandts, M., Michnick, S.W., Carver,
J.P. and Bendiak, B. Structures of asparagines-linked
oligosaccharides of the glycoprotein fetuin having sialic acids linked to N-acetylglucosamine.
Biochemistry, 28, 6500-6512 (1989).
[Abstract]
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D'Agostaro, G.A.F., Bendiak, B., and Tropak,
M. Cloning of cDNA encoding the membrane-bound form of bovine b1-4 galactosyltransferase.
Eur. J. Biochem., 183, 211-217 (1989).
[Abstract]
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Bendiak, B. and Schachter, H. Control of
glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:a-D-mannoside
b1-2 N-acetylglucosaminyltransferase II from rat liver. J. Biol. Chem., 262, 5775-5783
(1987).
[Abstract]
Bibliography
Further
information about Dr. Bendiak
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