TY - JOUR
T1 - Egg jelly layers of Xenopus laevis are unique in ultrastructure and sugar distribution
AU - Bonnell, Barry S.
AU - Chandler, Douglas E.
PY - 1996/6
Y1 - 1996/6
N2 - Jelly coats surrounding the eggs of the South African clawed toad, Xenopus laevis, consist of three transparent, gelatinous layers: the innermost layer (J1), the middle layer (J2), and the outer layer (J3). The distribution of N- acetylglucosamine within these jelly coats, as probed with FITC-conjugated wheat germ agglutinin (WGA-FITC), and the matrix ultrastructure of each layer, as visualized in platinum replicas produced by the quick-freeze, deep- etch, and rotary shadowing technique, suggests that each layer has a unique fiber and glycoprotein composition. J1 extends nearly 200 μm from the egg surface and exhibits no WGA-FITC staining. Stereo images of platinum replicas indicates that J1 consists of a tightly knit network of 5-10 nm fibers decorated with 10-20 nm particulate components. In contrast, J2 is a relatively thin layer, extending only 25-40 μm from the outer aspect of J1. When visualized by confocal microscopy, J2 displays a multilayered WGA-FITC staining pattern. The ultrastructure of J2 consists of sheets of fine fibers that run parallel to one another and that can be identified by their ability to bind WGA-colloidal gold. The fibers of each sheet run at an oblique angle to fibers in neighboring layers. J3 extends 100 μm or more from J2. The WGA- FITC staining pattern shows high intensity in its outer region and less intensity in regions closer to J2. Like J1, the J3 ultrastructure consists of a network of 5-10 nm fibers, decorated with 10-20 nm particulate components. The results of these studies add to a growing body of information that suggests the jelly coats surrounding the eggs of many animals consist of a fibrous glycoprotein superstructure that acts as a scaffold to which globular glycoproteins are bound.
AB - Jelly coats surrounding the eggs of the South African clawed toad, Xenopus laevis, consist of three transparent, gelatinous layers: the innermost layer (J1), the middle layer (J2), and the outer layer (J3). The distribution of N- acetylglucosamine within these jelly coats, as probed with FITC-conjugated wheat germ agglutinin (WGA-FITC), and the matrix ultrastructure of each layer, as visualized in platinum replicas produced by the quick-freeze, deep- etch, and rotary shadowing technique, suggests that each layer has a unique fiber and glycoprotein composition. J1 extends nearly 200 μm from the egg surface and exhibits no WGA-FITC staining. Stereo images of platinum replicas indicates that J1 consists of a tightly knit network of 5-10 nm fibers decorated with 10-20 nm particulate components. In contrast, J2 is a relatively thin layer, extending only 25-40 μm from the outer aspect of J1. When visualized by confocal microscopy, J2 displays a multilayered WGA-FITC staining pattern. The ultrastructure of J2 consists of sheets of fine fibers that run parallel to one another and that can be identified by their ability to bind WGA-colloidal gold. The fibers of each sheet run at an oblique angle to fibers in neighboring layers. J3 extends 100 μm or more from J2. The WGA- FITC staining pattern shows high intensity in its outer region and less intensity in regions closer to J2. Like J1, the J3 ultrastructure consists of a network of 5-10 nm fibers, decorated with 10-20 nm particulate components. The results of these studies add to a growing body of information that suggests the jelly coats surrounding the eggs of many animals consist of a fibrous glycoprotein superstructure that acts as a scaffold to which globular glycoproteins are bound.
KW - Amphibian
KW - Egg jelly
KW - Extracellular matrix
KW - Fertilization
KW - Freeze-etching
KW - Lectin staining
KW - Quick-freezing
UR - http://www.scopus.com/inward/record.url?scp=0029898922&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029898922&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1098-2795(199606)44:2<212::AID-MRD10>3.0.CO;2-4
DO - 10.1002/(SICI)1098-2795(199606)44:2<212::AID-MRD10>3.0.CO;2-4
M3 - Article
C2 - 9115719
AN - SCOPUS:0029898922
SN - 1040-452X
VL - 44
SP - 212
EP - 220
JO - Molecular Reproduction and Development
JF - Molecular Reproduction and Development
IS - 2
ER -