Faculty Collaboration Database

Intracellular function in rehydrated lyophilized platelets. Br J Haematol 2000 Oct;111(1):167-74

Date

11/25/2000

Pubmed ID

11091197

DOI

10.1046/j.1365-2141.2000.02343.x

Scopus ID

2-s2.0-0033764135 (requires institutional sign-in at Scopus site)   30 Citations

Abstract

This study aimed to evaluate the effect of cross-linking and lyophilization on intracellular signalling processes in rehydrated, lyophilized (RL) platelets, which are under development as a platelet substitute for transfusion. Exposure of RL platelets to thrombin resulted in enhanced phosphorylation of several proteins, including 18 kDa and 42 kDa kinase substrates that were shown to be the substrates of myosin light chain and protein kinase C respectively. Cross-linking and lyophilization depleted the platelets of free cytoplasmic ADP and ATP, but had less effect on protein-bound nucleotides. The surface membrane of RL platelets was found to be permeable to poly dT probes less than approximately 3 kDa in size; larger nucleotide probes and proteins did not penetrate the surface membrane. Taken together, our results indicate that RL platelets retain some of the haemostatic stimulus-response functions of fresh platelets and are capable of feedback amplification in coagulation.

Author List

Fischer TH, Merricks EP, Russell KE, Raymer RA, White GC, Bode AP, Nichols TC, Read MS

Author

Gilbert C. White MD Professor in the Medicine department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Adenosine Diphosphate
Adenosine Triphosphate
Autoradiography
Blood Platelets
Blotting, Western
Cell Membrane
Cytoplasm
Freeze Drying
Humans
Myosin Light Chains
Oligonucleotide Probes
Permeability
Phosphorylation
Platelet Transfusion
Protein Kinase C
Signal Transduction
Thrombin