Philip G. Hargreaves

TL;DR: Collagen can activate platelets by a mechanism that is independent of integrin alpha 2 beta 1 and for which collagen tertiary and quaternary structures are sufficient alone for activity without the involvement of highly specific cell-recognition sequences.

TL;DR: It is demonstrated that increased proteolytic cleavage of IL‐6R, mediated by a non‐matrix‐type metalloproteinase, is likely to contribute to the elevated concentrations of sIL‐ 6R found in the serum of patients with MM.

TL;DR: Assessment of key effector mechanisms affected by type I and II antibodies of various isotypes in ADCC and antibody-dependent cellular-phagocytosis (ADCP) assays demonstrate that ADCP and ADCC are impaired by antigenic modulation and that AD CP is the main effector function employed in vivo.

TL;DR: Data suggest that soluble CD30 may have biological functions in vivo and bind to its ligand, CD153, with high affinity and block cell death signals generated by cell surface‐expressed CD30 effectively.

TL;DR: The data suggest that, in human platelets, occupation or clustering of the integrin α2β1 is neither sufficient nor necessary for activation of FAK, the fibrinogen receptor αIIbβ3 is not required for activationof FAK by collagen fibers, and both intracellular Ca2+ and protein kinase C activity are essential intermediaries ofFAK activation.