Studies on the actin-binding protein HS1 in platelets.
BACKGROUND
The platelet cytoskeleton mediates the dramatic change in platelet morphology that takes place upon activation and stabilizes thrombus formation. The Arp2/3 complex plays a vital role in these processes, providing the protrusive force for lamellipodia formation. The Arp2/3 complex is highly regulated by a number of actin-binding proteins including the haematopoietic-specific protein HS1 and its homologue cortactin. The present study investigates the role of HS1 in platelets using HS1-/- mice.


RESULTS
The present results demonstrate that HS1 is not required for platelet activation, shape change or aggregation. Platelets from HS1-/- mice spread normally on a variety of adhesion proteins and have normal F-actin and Arp2/3 complex distributions. Clot retraction, an actin-dependent process, is also normal in these mice. Platelet aggregation and secretion is indistinguishable between knock out and littermates and there is no increase in bleeding using the tail bleeding assay.


CONCLUSIONS
This study concludes that HS1 does not play a major role in platelet function. It is possible that a role for HS1 is masked by the presence of cortactin.
Thomas
Steven G
SG
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. s.thomas@bham.ac.uk
Calaminus
Simon D J
SD
Auger
Jocelyn M
JM
Watson
Stephen P
SP
Machesky
Laura M
LM
D000199:Actins / Q000378:metabolism; D000818:Animals; D001792:Blood Platelets / Q000166:cytology / Q000378:metabolism*; D048430:Cell Shape; D005838:Genotype; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D008840:Microfilament Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D015539:Platelet Activation; D013927:Thrombosis / Q000235:genetics / Q000378:metabolism / Q000473:pathology
D000199:Actins; D008840:Microfilament Proteins