Skip Navigation



Glycobiology Advance Access published online on April 2, 2003
Glycobiology, doi:10.1093/glycob/cwg066
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
13/8/591    most recent
cwg066v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Appenheimer, M. M.
Right arrow Articles by Lau, J. T.Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Appenheimer, M. M.
Right arrow Articles by Lau, J. T.Y.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on January 27, 2003
Revised on March 5, 2003
Accepted on March 5, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Biologic contribution of P1 promoter mediated expression of ST6Gal I sialyltransferase

Michelle M. Appenheimer 1, Ruea-Yea Huang 1, E.V. Chandrasekaran 2, Martin Dalziel 1, Yi Ping Hu 1, Paul D. Soloway 1, Sherry A. Wuensch 1, Khushi L. Matta 2, Joseph T.Y. Lau 1*

1 Department of Molecular and Cellular Biology, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, NY 14263
2 Department of Molecular and Cellular Biophysics, Roswell Park Cancer Institute

* To whom correspondence should be addressed. E-mail: joseph.lau{at}roswellpark.org.

Abstract

The synthesis of the common and well-documented Sia{alpha}2,6 to Gal{beta}1,4GlcNAc structure (Sia6LacNAc), is principally mediated by the sialyltransferase ST6Gal I, which is particularly highly expressed in liver, lactating mammary gland, intestinal epithelia of newborn animals, and in B cells. Multiple, independent promoters govern the expression of Siat1, the ST6Gal I gene. In liver, elevation of hepatic and serum ST6Gal is part of the acute phase reaction, the hepatic response to systemic trauma, and is governed by the inducible, liver-specific promoter-regulatory region, P1. A constitutive and non-tissue specific promoter, P3, mediates low level, basal hepatic Siat1 transcription.

We have generated a mouse specifically unable to utilize the transcriptional initiation site uniquely utilized in P1-mediated ST6Gal I expression. These animals, Siat1{Delta}P1, are viable and display reduced ST6Gal I mRNA in liver with concomitantly reduced sialyltransferase activities in liver and in serum. Siat1{Delta}P1 animals are unable to elevate hepatic Siat1 mRNA as part of the inflammatory response induced by turpentine. Surprisingly, serum glycoprotein components exhibit normal extent of sialylation, with no noticeable difference in binding to SNA, the {alpha}2,6-sialyl-specific lectin. Siat1{Delta}P1 animals also exhibit an outwardly normal B cell response. Upon intraperitoneal challenge with the pathogen Salmonella typhimurium, a significantly greater accumulation of neutrophils within the peritoneal space was observed in Siat1{Delta}P1 animals compared to wild-type mice. Siat1{Delta}P1 mice also exhibit a greater bacterial burden in liver and spleen, accompanied by more pronounced spleno-hepatomegaly and greater leukocyte infiltration into affected organs than their wild-type counterparts.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GlycobiologyHome page
S. Kitazume, R. Oka, K. Ogawa, S. Futakawa, Y. Hagiwara, H. Takikawa, M. Kato, A. Kasahara, E. Miyoshi, N. Taniguchi, et al.
Molecular insights into {beta}-galactoside {alpha}2,6-sialyltransferase secretion in vivo
Glycobiology, May 1, 2009; 19(5): 479 - 487.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
M. Hedlund, E. Ng, A. Varki, and N. M. Varki
{alpha}2-6 Linked Sialic Acids on N-Glycans Modulate Carcinoma Differentiation In vivo
Cancer Res., January 15, 2008; 68(2): 388 - 394.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
M. Nasirikenari, B. H. Segal, J. R. Ostberg, A. Urbasic, and J. T. Lau
Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I
Blood, November 15, 2006; 108(10): 3397 - 3405.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. K. Altheide, T. Hayakawa, T. S. Mikkelsen, S. Diaz, N. Varki, and A. Varki
System-wide Genomic and Biochemical Comparisons of Sialic Acid Biology Among Primates and Rodents: EVIDENCE FOR TWO MODES OF RAPID EVOLUTION
J. Biol. Chem., September 1, 2006; 281(35): 25689 - 25702.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. C. Seales, F. M. Shaikh, A. V. Woodard-Grice, P. Aggarwal, A. C. McBrayer, K. M. Hennessy, and S. L. Bellis
A Protein Kinase C/Ras/ERK Signaling Pathway Activates Myeloid Fibronectin Receptors by Altering {beta}1 Integrin Sialylation
J. Biol. Chem., November 11, 2005; 280(45): 37610 - 37615.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
Z. Yasukawa, C. Sato, and K. Kitajima
Inflammation-dependent changes in {alpha}2,3-, {alpha}2,6-, and {alpha}2,8-sialic acid glycotopes on serum glycoproteins in mice
Glycobiology, September 1, 2005; 15(9): 827 - 837.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
J. H. Marino, M. Hoffman, M. Meyer, and K. S. Miller
Sialyltransferase mRNA abundances in B cells are strictly controlled, correlated with cognate lectin binding, and differentially responsive to immune signaling in vitro
Glycobiology, December 1, 2004; 14(12): 1265 - 1274.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
F. Dall'Olio, M. Chiricolo, A. D'Errico, E. Gruppioni, A. Altimari, M. Fiorentino, and W. F. Grigioni
Expression of {beta}-galactoside {alpha}2,6 sialyltransferase and of {alpha}2,6-sialylated glycoconjugates in normal human liver, hepatocarcinoma, and cirrhosis
Glycobiology, January 1, 2004; 14(1): 39 - 49.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.