Carbohydrate characterization of quail primordial germ cells during migration and gonadal differentiation

J Anat. 2007 Jan;210(1):98-111. doi: 10.1111/j.1469-7580.2006.00668.x.

Abstract

A selection of lectins were used to study changes in the distribution of sugar residues in primordial germ cells (PGCs) during gonadal colonization and differentiation. Although the cytochemical characteristics of PGCs have been described in the chick, little is known about such characteristics in other avian species of interest to experimental biology. Therefore, we studied embryos of Japanese quail (Coturnix coturnix japonica) by light and laser confocal scanning microscopy, using the QH1 antibody as a tool to identify PGCs in both sexes and at all stages. LEA, WGA and RCA-I bound to PGCs in a similar way to QH1. LEA was the best marker for all stages. The presence of acid phosphatase and the intense reaction of LEA, WGA, RCA-I and WFA at the cell surface were shown to be a useful tool in the study of the migratory PGCs of the quail. Quails were sexed histologically in younger embryos than in chick; results were confirmed by PCR. The lectin-binding pattern changed drastically in differentiated gonads. Cell surface reactivity was almost entirely lost. Quail differentiating oogonia showed a characteristic binding pattern to QH1 and to the lectins WGA, RCA-I and WFA. Binding was observed in intense spots in the Golgi complex, and there was a specific PNA reaction. These results suggest that some selective sugar binding sites on the PGCs play a significant role in their migration, colonization and maturation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase / analysis
  • Animals
  • Carbohydrates / analysis*
  • Cell Differentiation
  • Cell Movement
  • Coturnix*
  • Female
  • Germ Cells / chemistry*
  • Histocytochemistry
  • Immunohistochemistry
  • Male
  • Microscopy, Immunoelectron
  • Plant Lectins
  • Quail / embryology*
  • Sex Differentiation

Substances

  • Carbohydrates
  • Plant Lectins
  • Acid Phosphatase