scholarly journals Sodium-dependent accumulation of 5-hydroxytryptamine by rat blood platelets

1969 ◽  
Vol 37 (3) ◽  
pp. 680-688 ◽  
Author(s):  
J. M. SNEDDON
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.


Life Sciences ◽  
1980 ◽  
Vol 27 (20) ◽  
pp. 1881-1888 ◽  
Author(s):  
James K.T. Wang ◽  
Takashi Taniguchi ◽  
Sydney Spector

1975 ◽  
Vol 150 (1) ◽  
pp. 129-132 ◽  
Author(s):  
A H Drummond ◽  
J L Gordon

5-Hydroxytryptamine changes the shape of rat blood platelets by combination with a cinanserin-sensitive receptor which is not associated with the active uptake of 5-hydroxytryptamine. Binding of 5-hydroxy[3H]tryptamine to platelets at 4°C demonstrates the presence of three saturable sites, and the highest-affinity site is apparently this 5-hydroxytryptamine receptor.


1982 ◽  
Vol 31 (19) ◽  
pp. 3122-3124 ◽  
Author(s):  
Peter Turčáni ◽  
Marian Turčáni ◽  
Daniel Bartko

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