Molecular Human Reproduction, Vol. 7, No. 12, 1173-1178,
December 2001
© 2001 European Society of Human Reproduction and Embryology
Implantation and pregnancy |
From maternal glucose to fetal glycogen: expression of key regulators in the human placenta
1 Institute of Histology and Embryology, University of Graz, Harrachgasse 21, A-8010 Graz, Austria, 2 Institute of Histology and Embryology, Akdeniz University, 07070 Kampus Antalya, Turkey, 3 Department of Obstetrics and Gynaecology, University of Graz, Auenbruggerplatz 14, A-8036 Graz and 4 Institute of Zoology, University of Graz, Universitätsplatz 3, A-8010 Graz, Austria
The present study investigated the expression of glycogenin, the protein primer for glycogen synthesis, and the high affinity glucose transporter isoform GLUT3 as a further potential regulator of cellular glycogen metabolism, in first trimester and term human placenta using immunohistochemistry and Western blotting. At term, glycogenin was most abundant in the endothelium of fetal vessels. Trophoblast as well as basal decidual cells were moderately stained. The glycogenin distribution pattern in first trimester placentae resembled that at term, but reactivity was generally less intense. Extravillous trophoblast and villous cytotrophoblast were the major sites of GLUT3 expression. Endothelial cells were also strongly labelled with the GLUT3 antiserum. Western blotting identified both free and glucosylated glycogenin, as well as a 48 kDa band reacting with GLUT3 antiserum in placental villous tissue. Glycogenin immunoreactivity remained unaffected by amylolytic glycogen digestion, although preceding electron microscopical examination demonstrated the presence of glycogen. These data may indicate that placental glycogenin can be recycled from the immature glycogen or that it is located on the surface of the glycogen molecule. In conclusion, the co-expression of glycogenin with GLUT3 might enable glycogen-storing cells to exchange glucose quite effectively according to prevailing metabolic demands of glycogen synthesis or degradation.
glucose transport/GLUT/glycogen/glycogenin/placenta
5 To whom correspondence should be addressed. E-mail: tom.hahn{at}kfunigraz.ac.at
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  I. A. Simpson, D. Dwyer, D. Malide, K. H. Moley, A. Travis, and S. J. Vannucci The facilitative glucose transporter GLUT3: 20 years of distinction Am J Physiol Endocrinol Metab, August 1, 2008; 295(2): E242 - E253. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. Desoye and S. Hauguel-de Mouzon The Human Placenta in Gestational Diabetes Mellitus: The insulin and cytokine network Diabetes Care, July 1, 2007; 30(Supplement_2): S120 - S126. [Full Text] [PDF]
|
|
|
|
|
|
A. Ganguly, R. A. McKnight, S. Raychaudhuri, B.-C. Shin, Z. Ma, K. Moley, and S. U. Devaskar Glucose transporter isoform-3 mutations cause early pregnancy loss and fetal growth restriction Am J Physiol Endocrinol Metab, May 1, 2007; 292(5): E1241 - E1255. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Belkacemi, G. E. Lash, S. K. Macdonald-Goodfellow, J. D. Caldwell, and C. H. Graham Inhibition of Human Trophoblast Invasiveness by High Glucose Concentrations J. Clin. Endocrinol. Metab., August 1, 2005; 90(8): 4846 - 4851. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. O. Carayannopoulos, A. Schlein, A. Wyman, M. Chi, C. Keembiyehetty, and K. H. Moley GLUT9 Is Differentially Expressed and Targeted in the Preimplantation Embryo Endocrinology, March 1, 2004; 145(3): 1435 - 1443. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. von Wolff, S. Ursel, U. Hahn, R. Steldinger, and T. Strowitzki Glucose Transporter Proteins (GLUT) in Human Endometrium: Expression, Regulation, and Function throughout the Menstrual Cycle and in Early Pregnancy J. Clin. Endocrinol. Metab., August 1, 2003; 88(8): 3885 - 3892. [Abstract] [Full Text] [PDF]
|
|