scholarly journals Correction: An essential role of the mouse synapse-associated protein Syap1 in circuits for spontaneous motor activity and rotarod balance

Biology Open ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. bio048942
Author(s):  
Cora R. von Collenberg ◽  
Dominique Schmitt ◽  
Thomas Rü licke ◽  
Michael Sendtner ◽  
Robert Blum ◽  
...  
Biology Open ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. bio042366 ◽  
Author(s):  
Cora R. von Collenberg ◽  
Dominique Schmitt ◽  
Thomas Rülicke ◽  
Michael Sendtner ◽  
Robert Blum ◽  
...  

1986 ◽  
Vol 250 (3) ◽  
pp. H426-H433 ◽  
Author(s):  
J. Ludbrook ◽  
S. J. Potocnik

Systemic arterial pressure (SAP) and heart rate (HR) were continuously measured in rabbits during spontaneous motor activity such as postural change, exploration, grooming, and eating, and during interposed periods of inactivity within which SAP and HR were defined as basal. Six rabbits were observed for 2 h under each of 3 conditions of arterial baroreceptor afferents: all intact (B4); one carotid sinus intact (B1); all interrupted (B0). In B4, SAP and HR were above basal levels 82% of the time; in B1, 64% and 76% of the time, respectively; in B0, only 21% and 28% of the time, respectively. Supplementary experiments in another six rabbits established that the activity-associated falls of SAP in condition B0 were independent of HR, were not due to engagement of cardiac receptor reflexes, and were not abolished by autonomic ganglion blockade. We conclude that the transient rises of SAP and HR that occur during everyday activity are associated with partial or complete suppression of the reflex effects of arterial baroreceptor input, and we suggest that this is due to transient upward resetting of the arterial baroreflex.


2012 ◽  
Vol 50 (01) ◽  
Author(s):  
N Lange ◽  
S Sieber ◽  
A Erhardt ◽  
G Sass ◽  
HJ Kreienkamp ◽  
...  

1995 ◽  
Vol 74 (05) ◽  
pp. 1323-1328 ◽  
Author(s):  
Dominique Lasne ◽  
José Donato ◽  
Hervé Falet ◽  
Francine Rendu

SummarySynthetic peptides (TRAP or Thrombin Receptor Activating Peptide) corresponding to at least the first five aminoacids of the new N-terminal tail generated after thrombin proteolysis of its receptor are effective to mimic thrombin. We have studied two different TRAPs (SFLLR, and SFLLRN) in their effectiveness to induce the different platelet responses in comparison with thrombin. Using Indo-1/AM- labelled platelets, the maximum rise in cytoplasmic ionized calcium was lower with TRAPs than with thrombin. At threshold concentrations allowing maximal aggregation (50 μM SFLLR, 5 μM SFLLRN and 1 nM thrombin) the TRAPs-induced release reaction was about the same level as with thrombin, except when external calcium was removed by addition of 1 mM EDTA. In these conditions, the dense granule release induced by TRAPs was reduced by over 60%, that of lysosome release by 75%, compared to only 15% of reduction in the presence of thrombin. Thus calcium influx was more important for TRAPs-induced release than for thrombin-induced release. At strong concentrations giving maximal aggregation and release in the absence of secondary mediators (by pretreatment with ADP scavengers plus aspirin), SFLLRN mobilized less calcium, with a fast return towards the basal level and induced smaller lysosome release than did thrombin. The results further demonstrate the essential role of external calcium in triggering sustained and full platelet responses, and emphasize the major difference between TRAP and thrombin in mobilizing [Ca2+]j. Thus, apart from the proteolysis of the seven transmembrane receptor, another thrombin binding site or thrombin receptor interaction is required to obtain full and complete responses.


1979 ◽  
Vol 42 (04) ◽  
pp. 1193-1206 ◽  
Author(s):  
Barbara Nunn

SummaryThe hypothesis that platelet ADP is responsible for collagen-induced aggregation has been re-examined. It was found that the concentration of ADP obtaining in human PRP at the onset of aggregation was not sufficient to account for that aggregation. Furthermore, the time-course of collagen-induced release in human PRP was the same as that in sheep PRP where ADP does not cause release. These findings are not consistent with claims that ADP alone perpetuates a collagen-initiated release-aggregation-release sequence. The effects of high doses of collagen, which released 4-5 μM ADP, were not inhibited by 500 pM adenosine, a concentration that greatly reduced the effect of 300 μM ADP. Collagen caused aggregation in ADP-refractory PRP and in platelet suspensions unresponsive to 1 mM ADP. Thus human platelets can aggregate in response to collagen under circumstances in which they cannot respond to ADP. Apyrase inhibited aggregation and ATP release in platelet suspensions but not in human PRP. Evidence is presented that the means currently used to examine the role of ADP in aggregation require investigation.


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