Alicia is the III Initiative (inflammation, Immunology & Infectious Diseases) Symposium Spring 2018 Poster Winner Here is her abstract.
Signal-Dependent Golgi Formation and De Novo Glycosylation in Human Platelets
Background
Golgi are necessary for post-translational modification of proteins, including glycosylation, in nucleated cells. Platelets actively translate proteins. Nevertheless, whether golgi form in platelets under signal-dependent conditions has not previously been examined.
Methods
Platelets were isolated from human donors and allowed to adhere to matrices in the presence and absence of inhibitors. TEM, immunocytochemistry (ICC), and immunoblot identified golgi formation. Click-it reaction chemistry identified de novo glycosylation events.
Results
Golgi formation was triggered by platelet adhesion and blocked by specific inhibitors of golgi reassembly (e.g. NMS-873, which inhibits valosin containing protein). Formed golgi in platelets were visible by TEM and ICC 2 hours after adhesion. Golgi formation was regulated by integrin activation but independent of platelet shape change. Golgi stacks in platelets were shown to be functional by labeling de novo glycosylation events. Glycosylation was increased under conditions where golgi formation was increased. De novo glycosylation occurred as early as 2 hours after platelet adhesion and continued to increase for up to 8 hours, indicating sustained golgi function.
Conclusions
Adhesion triggers golgi formation and de novo glycosylation in human platelets. These findings highlight that although they are anucleate, platelets form golgi by a signal-dependent mechanism and participate in post-translational events.
