scholarly journals OBSERVATIONS ON FIBRILLOGENESIS IN THE CONNECTIVE TISSUE OF THE CHICK EMBRYO WITH THE AID OF SILVER IMPREGNATION

1956 ◽  
Vol 2 (4) ◽  
pp. 67-70 ◽  
Author(s):  
F. Wassermann ◽  
L. Kubota
Keyword(s):  
Chick Embryo ◽  
Connective Tissue ◽  
Silver Impregnation ◽  
The Body ◽  
Electron Microscopic ◽  
Stage Of Development ◽  
Impregnation Technique ◽  
Microscopic Demonstration ◽  
Neutral Formalin ◽  
Electron Microscopic Demonstration

A technique is described which combines silver impregnation and ultrathin sectioning for the electron microscopic demonstration of fibrils in the connective tissue of the chick embryo. The electron micrographs presented in this paper provide evidence for the specificity and completeness of the silver-impregnation technique. It has been shown that, in this particular tissue after fixation in neutral formalin and at the stage of development represented by our material, the argyrophil fibers are embedded in a material which is continuous with the body of the fibroblasts.

scholarly journals Distribution of fibroblast surface antigen in the developing chick embryo.

1975 ◽  
Vol 142 (1) ◽  
pp. 41-49 ◽  
Author(s):  
E Linder ◽  
A Vaheri ◽  
E Ruoslahti ◽  
J Wartiovaara
Keyword(s):  
Chick Embryo ◽  
Connective Tissue ◽  
Basement Membranes ◽  
Loose Connective Tissue ◽  
Extracellular Medium ◽  
Liver Sinusoids ◽  
Stage Of Development ◽  
Parenchymal Cells ◽  
Fibrillar Network

Fibroblast surface (SE) antigen is present in fibrillar surface structures of cultured normal fibroblasts, shed to the extracellular medium, and is also found in circulation (serum and plasma). Malignant fibroblasts (transformed by viruses) do not express SF antigen on the cell surface. In this study the in vivo differentiation and distribution of SF antigen has been investigated in the developing chick embryo using cryostat sections and immunofluorescence. The major findings were: (a) SF antigen was detectable in the loose connective tissue of very early (2-to 3-day old) embryos. (b) Condensation of SF antigen was seen in various boundary membranes such as the glomerular and tubular basement membranes of the kidney, the boundary membranes of the notochord, yolk sac, and vitelline membranes and liver sinusoids. (c) SF antigen was found to be cell-type specific. It was seen as a fibrillar network in the loose connective tissue of different organs but not in the parenchymal cells. It was not found in muscle cells at any stage of development. (d) The antigen was present in the undifferentiated mesenchymal cells of the kidney; but not found after their development into epithelial cells of the secretory tubules. (e) Both in vivo and in fibroblast cultures SF antigen was distributed as a fibrillar network. These data indicate that SF antigen is a "differentiation antigen" restricted to certain cells of mesenchymal origin and character, and that is accumulates in the connective tissue during embryogenesis.

scholarly journals Developmental changes in the type I procollagen processing pathway in chick-embryo cornea

1991 ◽  
Vol 276 (3) ◽  
pp. 777-784 ◽  
Author(s):  
S J Mellor ◽  
G L Atkins ◽  
D J S Hulmes
Keyword(s):  
Chick Embryo ◽  
Kinetic Model ◽  
Rate Constants ◽  
Collagen Fibril ◽  
Electrophoretic Analysis ◽  
Developmental Changes ◽  
Type I ◽  
Electron Microscopic ◽  
Type I Procollagen ◽  
Stage Of Development

Type I procollagen processing in chick-embryo corneas was studied at days 12, 14 and 17 of development. Pulse-chase experiments and electrophoretic analysis of salt-soluble extracts showed developmental changes in the processing pathway. A kinetic model was fitted to the data to determine rate constants for processing of both N- and C-propeptides. Data for pro alpha 1(I)-chain processing and pro alpha 2(I)-chain processing were fitted separately (where pro means procollagen). Between days 12 and 17 the relative flux through the pC-collagen (procollagen chain lacking the N-propeptide) and pN-collagen (procollagen chain lacking the C-propeptide) pathways increased approx. 4-fold. Pro alpha 1(I) chains and pro alpha 2(I) chains were processed by slightly different routes. Variations in the rate constants were compared with electron-microscopic measurements of collagen fibril diameters at each stage of development. Diameters increased by less than 10% over the period from 12 to 17 days. It was concluded that fibril diameters are relatively insensitive to the pathway of procollagen processing in the salt-soluble pool.

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