Effect of hydra peptide morphogen on levels of?-endorphin and certain hormones in albino rat blood and adrenals

1991 ◽  
Vol 112 (4) ◽  
pp. 1510-1512
Author(s):  
N. B. Murzina ◽  
A. Yu. Khomichuk ◽  
S. S. Timoshin ◽  
G. G. Obukhova ◽  
O. A. Anosova ◽  
...  
1930 ◽  
Vol 45 (1) ◽  
pp. 59-67 ◽  
Author(s):  
Francis D. Gunn ◽  
Stuart L. Vaughan

Author(s):  
R. Carriere

The external orbital gland of the albino rat exhibits both sexual dimorphism and histological age changes. In males, many cells attain a remarkable degree of polyploidy and an increase of polyploid cell number constitutes the major age change until young adulthood. The acini of young adults have a small lumen and are composed of tall serous cells. Subsequently, many acini acquire a larger lumen with an irregular outline while numerous vacuoles accumulate throughout the secretory cells. At the same time, vesicular acini with a large lumen surrounded by pale-staining low cuboidal diploid cells begin to appear and their number increases throughout old age. The fine structure of external orbital glands from both sexes has been explored and in considering acinar cells from males, emphasis was given to the form of the Golgi membranes and to nuclear infoldings of cytoplasmic constituents.


1969 ◽  
Author(s):  
Leland E. Rhodes ◽  
Donovan E. Fleming
Keyword(s):  

1987 ◽  
Vol 58 (02) ◽  
pp. 786-789 ◽  
Author(s):  
O Behnke

SummaryAdhesion of rat blood platelets to native rat tail collagen fibrils was studied in the electron microscope under conditions that preserved collagen-associated proteoglycans (CAPG). The CAPG molecules were aligned in chain-like configurations that encircled the fibrils with a 65 nm period; they appeared to coat the fibrils completely and extended 60-100 nm away from the fibril. The initial platelet-fibril contact occurred between the platelet glycocalyx and the CAPG of the fibrils i.e. between two surfaces with net-negative charges. When close contact was established between the fibril surface proper and the platelet membrane, CAPG were not identified in the area of contact, and the collagen-platelet distance was reduced to a ~10-12 nm wide gap traversed by delicate links in register with fibril periodicities.


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