Platelets.
Publisher:
Churchill Livingstone,. London : Informa Healthcare
Frequency: Eight no. a year, 2000-
Country: England
Language: English
Author(s):
British Library. Medical Information Service.
Start Year:1990 -
ISSN:
0953-7104 (Print)
1369-1635 (Electronic)
0953-7104 (Linking)
1369-1635 (Electronic)
0953-7104 (Linking)
Impact Factor
3.2
2022
| NLM ID: | 9208117 |
| (DNLM): | SR0064701(s) |
| (OCoLC): | 25526070 |
| Coden: | PLTEEF |
| LCCN: | sn 92033274 |
| Classification: | W1 PL235 |
The secretory mechanisms in equine platelets are independent of cytoskeletal polymerization and occur through membrane fusion. Studies in animal models are useful to understand the basic mechanisms involved in hemostasis and the functional differences among species. Ultrastructural observations led us to predict differences in the activation and secretion mechanisms between equine and human platelets. The potential mechanisms involved have been comparatively explored in the present study. Equine and human platelets were activated with thrombin (0.5 U/ml) and collagen (20 µg/ml), for 90 seconds, and samples processed to evaluate: i) ultrastructural changes, by electron microscopy, ii) actin polymerization and cy...
The ultrastructure of camel blood platelets: a comparative study with human, bovine, and equine cells. Previous studies indicated that the camel has a very active haemostatic mechanism with a short bleeding time and thrombocytosis. However, platelet function, when tested by agonist-induced aggregation and PFA 100 closure time, showed marked inhibition compared to humans. Since camels are also far more resistant to long exposure to excessive heat and high body temperature than humans, it seemed worthwhile to explore fundamental morphological differences between human and camel platelets and those from other species. The present study has examined the ultrastructure of camel platelets and compare...
Effects of P2Y(1) and P2Y(12) receptor antagonists on ADP-induced shape change of equine platelets: comparison with human platelets. Platelet activation by adenosine 5' -diphosphate (ADP) is via both P2Y(1 )and P2Y(12) receptors and leads to shape change and aggregation. The effects on ADP-induced platelet shape change of two P2Y(1) antagonists, adenosine 3'-phosphate, 5'-phosphosulfate (A3P5PS) and 2-deoxy-N(6)-methyladenosine 3', 5'-diphosphate (MRS-2179) and a P2Y(12) antagonist 2-propylthio-D-beta,gamma-dichloromethylene-adenosine 5'-triphosphate (AR-C67085MX) were determined by turbidimetric aggregometry and scanning electron microscopy (SEM) on equine and human platelets. The platelet aggregation was inhibited during ...
The inhibition of adenylate cyclase in equine platelets by collagen and by platelet-activating factor. Equine platelet aggregation was stimulated by collagen fibres or platelet-activating factor. The action of both ligands was blocked by forskolin or prostaglandin E(1) agents which are known to activate adenylate cyclase. Equine platelet membranes were found to contain adenylate cyclase activity which was inhibited in dose-dependent fashion by both collagen and platelet-activating factor. Platelet-activating factor-induced inhibition was antagonised by WEB2086.
The amino Acid sequence glutamine-628 to valine-646 within the A1 repeat domain mediates binding of von Willebrand factor to bovine brain sulfatides and equine tendon collagen. von Willebrand Factor (vWF) is a multifunctional glycoprotein in plasma and vascular subendothelial matrix which plays a major role in cellular adhesion. vWFdependent adhesion of platelets to the subendothelium at high shear rates involves a specific platelet membrane receptor, the glycoprotein (GP) Ib-IX complex. We have previously purified a 39/34-kiloDalton (kDa) dispase fragment of vWF (Leu-480/Val-481 to Gly-718) and demonstrated that this fragment contains the binding site for the GP Ib-IX complex [Andrews R K, et al. Biochemistry 1989; 28: 8326-83361. vWF also mediates agglutination of ...