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Post Doc/Research Assoc Position

baenziger at PATHBOX.WUSTL.EDU baenziger at PATHBOX.WUSTL.EDU
Thu Feb 22 11:28:26 EST 1996

Post Doc/Research Associate Position to Study Role of Glycosylation 
in Reproduction, Development, and Inflammation.
	Glycobiology is a rapidly growing field with an impact in many 
areas involving folding and assembly of newly synthesized 
glycoproteins, control of circulatory half life, targeting to 
tissues and organelles, and cellular recognition during inflammation 
and development.  My laboratory studies unique carbohydrate 
structures which serve a recognition function, glycosyltransferases 
which synthesize them, and how their recognition determinants 
interact with specific receptors. For example, we have found that 
structures containing GalNAc-4-SO4 are present on the pituitary 
glycoprotein hormones LH and TSH, playing a critical role in hormone 
activity via hormone clearance by a GalNAc-4-SO4-specific receptor 
in liver endothelial cells.  Using biochemical and molecular 
biologic approaches, we examine how glycosyltransferases recognize 
their target proteins to synthesize these structures, and how 
glycosyltransferase and receptor expression are regulated during 
development and hormonal cycles. We are also examining the roles 
played by these structures in recognition during inflammation and 
development. We have recently cloned two of these transferases and 
are embarking on studies directed at understanding regulation of 
expression, structural-function relationships, and biologic function 
in  vivo. 
	Interested candidates with experience in molecular biology and/or 
protein purification and characterization should contact:  Dr. 
Jacques U. Baenziger, Department of Pathology, Washington University 
Medical School, St. Louis, MO 63110 with a CV and references.
FAX 314-362-8888.  E-mail <Baenziger at Pathology.WUSTL.EDU> 

Recent Publications:

Hooper, L.V., Hindsgaul, O., and Baenziger, J.U.: Purification and 
characterization of the GalNAc-4-sulfotransferase responsible for 
sulfation of GalNAcb1,4-GlcNAc-bearing oligosaccharides.  J. Biol. 
Chem.  270:16327-16332, 1995.

Manzella, S.M., Beranek, M.C., Dharmesh, S.M., Swanson, P., and 
Baenziger, J.U.: Evolutionary conservation of sulfated 
oligosaccharides on vertebrate glycoprotein hormones that control 
circulatory half-life.  J. Biol. Chem. 270:21665-21671, 1995.

Mengeling, B.J., Manzella, S.M., and Baenziger, J.U.:  A cluster of 
basic amino acids within an a-helix is essential for a-subunit 
recognition by the glycoprotein hormone: 
N-acetylgalactosaminyltransferase.  Proc. Natl. Acad. Sci. USA 
92;502-506, 1995.

Baenziger, J.U.:  Protein-specific glycosyltransferases:  How and 
why they do it! 	FASEB J. 8:1019-1025, 1994.
Dharmesh, S.M. and Baenziger, J.U.:  Estrogen modulates expression 
of the glycosyltransferases which synthesize sulfated 
oligosaccharides on lutropin.  Proc. Natl. Acad. Sci. USA  
90:11127-11131, 1993.

Baenziger, J.U., Kumar, S., Brodbeck, R.M., Smith, P.L. and Beranek, 
M.C.: Circulatory half-life but not interaction with the LH/CG 
receptor is modulated by sulfation of bLH oligosaccharides. Proc. 
Natl. Acad. Sci. USA 89:334-338, 1992.

Fiete, D., Srivastava, V., Hindsgaul, O. and Baenziger, J.U.: A 
hepatic reticulo-endothelial cell receptor specific for 
S04-4GalNAcb1,4GlcNAcb1,2Mana that mediates rapid clearance of 
lutropin. Cell, 67:1103-1110, 1991.

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