Basement membrane heterogeneity during chick development as shown by tomato (Lycopersicon esculentum) lectin binding.
Basement membranes (BMs) constitute a distinct compartment of the extracellular matrix (ECM). All BMs show a similar structural appearance but differ in molecular composition. These variations have critical functional implications. The aim of this study is to establish the pattern of the tomato lectin (Lycopersicon esculentum agglutinin--LEA) binding sites in the BMs of the developing chick embryo (stages 4-21, Hamburger and Hamilton, 1951) in order to achieve a better understanding of the molecular heterogeneity of BMs. The study was performed with transmission electron microscopy (TEM) histochemistry, and confocal laser microscopy. TEM showed that LEA bound to the lamina densa and to the lamina fibroreticularis of the BMs. Through the period studied, most of the LEA binding appeared in the ectodermal BM and its derivatives. In the limb bud, LEA binding to the ectoderm BM was more intense in the ventral half than in the dorsal half. Furthermore, LEA allowed the early (HH16) detection of the transverse fibrillar tracts. In the lens and in the inner ear primordium, the BMs were LEA positive through the placode and cup stages. The binding was progressively reduced through the vesicle stage. The BMs of the olfactory primordium, and of the Rathke's pouch were positive. In contrast, the BMs of the developing central nervous system were negative. The BMs of both the paraxial and the lateral plates of the mesoderm were negative, whereas the notochord and the BM of the Wolffian duct were positive. The endodermal BM and its derivatives were negative. The ECM located between the fusing endocardial tubes, and the BM of the fusion zone of the paired aortae, were positive. This suggested an active role of the LEA-positive glycoproteins in the fusion of endothelia. Our results show the heterogeneity of the chick embryo BMs during development. In addition, LEA constitutes an excellent marker for the primordial germ cells.
Ojeda
J L
JL
Department of Anatomy and Cell Biology, Faculty of Medicine, University of Cantabria, Santander, Spain. ojedajl@unican.es
Icardo
J M
JM
D000818:Animals; D001485:Basement Membrane / Q000737:chemistry* / Q000196:embryology* / Q000378:metabolism / Q000648:ultrastructure; D001665:Binding Sites; D002319:Cardiovascular System / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D002490:Central Nervous System / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D002642:Chick Embryo; D004475:Ectoderm / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000737:chemistry / Q000648:ultrastructure; D005123:Eye / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D005260:Female; D006023:Glycoproteins / Q000032:analysis* / Q000378:metabolism; D006651:Histocytochemistry; D007668:Kidney / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D018613:Microscopy, Confocal; D046529:Microscopy, Electron, Transmission; D009833:Olfactory Pathways / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D010902:Pituitary Gland / Q000737:chemistry / Q000196:embryology / Q000648:ultrastructure; D037121:Plant Lectins / Q000032:analysis* / Q000378:metabolism; D011485:Protein Binding
D006023:Glycoproteins; D037121:Plant Lectins; C034981:tomato lectin