English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Background Calpain, intracellular non-lysosomal calcium-dependent proteinase, is activated by a number of signaling pathways that lead to the elevation of intraplatelet calcium concentrations. Physiological roles of calpain, highly expressed in platelets, include regulation of platelet aggregation and adhesion, while excessive activation of calpain in such pathological disorders as diabetes could cause changes in platelet functions, resulting in platelet hyperactivation. Platelets from diabetic patients are also characterized by resistance to nitric oxide inhibition. Here we examined if calpain could regulate major cAMP and cGMP hydrolyzing phosphodiesterases (PDEs), PDE3A and PDE5, in human platelets.

Calcium/Calpain mediated regulation of cyclic nucleotide phosphodiesterases, PDE3A and PDE5, in human platelets