HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Manzella, S. M. Articles by Baenziger, J. U. Search for Related Content PubMed PubMed Citation Articles by Manzella, S. M. Articles by Baenziger, J. U. Social Bookmarking                      What's this?

Volume 272, Number 8, Issue of February 21, 1997 pp. 4775-4782
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Developmental Regulation of a Pregnancy-specific Oligosaccharide Structure, NeuAc2,6GalNAc1,4GlcNAc, on Select Members of the Rat Placental Prolactin Family

(Received for publication, August 19, 1996, and in revised form, November 14, 1996)

Stephen M. Manzella , Shylaja M. Dharmesh , Christopher B. Cohick ^¶ , Michael J. Soares ^¶ and Jacques U. Baenziger

From the  Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110 and the ^¶ Department of Physiology, University of Kansas Medical Center, Kansas City, Kansas 66103

Successful pregnancy is dependent upon an array of signaling proteins secreted by the trophoblast cells of the placenta. Among these is a group of proteins related to pituitary prolactin, known as the prolactin/growth hormone family. These proteins are expressed at specific times during gestation and synthesized in distinct trophoblast cell types in the rat placenta. We report here that select members of this family, prolactin-like protein (PLP-A), PLP-B, PLP-C, decidual/trophoblast PRP, and placental lactogen I variant, only which are expressed in the spongiotrophoblast, late in rat placental development bear Asn-linked oligosaccharides terminating with NeuAc2,6GalNAc1,4GlcNAc-R. This reflects the concurrent expression of these prolactin/growth hormone family members with the peptide-specific 1,4GalNAc-transferase and an 2,6-sialyltransferase, which can add sialic acid to terminal 1,4-linked GalNAc. We have determined that at least one of the prolactin-like proteins, PLP-A, is recognized by the protein-specific GalNAc-transferase. The presence of NeuAc2,6GalNAc1,4GlcNAc-R on only a limited number of glycoproteins synthesized by the spongiotrophoblasts between mid gestation and birth reflects the need for both the GalNAc-transferase and the peptide recognition determinant for efficient addition of GalNAc. Thus, expression of the GalNAc-transferase and specific members of the prolactin/growth hormone family is developmentally regulated in the rat placenta, suggesting a physiological role for the terminal NeuAc2,6GalNAc1,4GlcNAc-R sequence on Asn-linked oligosaccharides of these proteins.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				L. M. Steirer, E. I. Park, R. R. Townsend, and J. U. Baenziger The Asialoglycoprotein Receptor Regulates Levels of Plasma Glycoproteins Terminating with Sialic Acid {alpha}2,6-Galactose J. Biol. Chem., February 6, 2009; 284(6): 3777 - 3783. [Abstract] [Full Text] [PDF]

				E. Miller, D. Fiete, N. M. J. Blake, M. Beranek, E. L. Oates, Y. Mi, D. S. Roseman, and J. U. Baenziger A Necessary and Sufficient Determinant for Protein-selective Glycosylation in Vivo J. Biol. Chem., January 25, 2008; 283(4): 1985 - 1991. [Abstract] [Full Text] [PDF]

				E. I. Park, Y. Mi, C. Unverzagt, H.-J. Gabius, and J. U. Baenziger The asialoglycoprotein receptor clears glycoconjugates terminating with sialic acid{alpha}2,6GalNAc PNAS, November 22, 2005; 102(47): 17125 - 17129. [Abstract] [Full Text] [PDF]

				E. I. Park and J. U. Baenziger Closely Related Mammals Have Distinct Asialoglycoprotein Receptor Carbohydrate Specificities J. Biol. Chem., September 24, 2004; 279(39): 40954 - 40959. [Abstract] [Full Text] [PDF]

				E. I. Park, S. M. Manzella, and J. U. Baenziger Rapid Clearance of Sialylated Glycoproteins by the Asialoglycoprotein Receptor J. Biol. Chem., February 7, 2003; 278(7): 4597 - 4602. [Abstract] [Full Text] [PDF]

				K. Iwatsuki, M. Oda, W. Sun, S. Tanaka, T. Ogawa, and K. Shiota Molecular Cloning and Characterization of a New Member of the Rat Placental Prolactin (PRL) Family, PRL-Like Protein H Endocrinology, December 1, 1998; 139(12): 4976 - 4983. [Abstract] [Full Text] [PDF]

				G. Xia, M. R. Evers, H.-G. Kang, M. Schachner, and J. U. Baenziger Molecular Cloning and Expression of the Pituitary Glycoprotein Hormone N-Acetylgalactosamine-4-O-sulfotransferase J. Biol. Chem., December 1, 2000; 275(49): 38402 - 38409. [Abstract] [Full Text] [PDF]

				S. Toivonen, O. Aitio, and O. Renkonen alpha 2,3-Sialylation of Terminal GalNAcbeta 1-3Gal Determinants by ST3Gal II Reveals the Multifunctionality of the Enzyme. THE RESULTING Neu5Acalpha 2-3GalNAc LINKAGE IS RESISTANT TO SIALIDASES FROM NEWCASTLE DISEASE VIRUS AND STREPTOCOCCUS PNEUMONIAE J. Biol. Chem., September 28, 2001; 276(40): 37141 - 37148. [Abstract] [Full Text] [PDF]