Rat Anti-Mouse E-selectin (CD62E) Monoclonal antibody, clone 9A9 Functional Grade

The Sele river plain is located along the western Tyrrhenian margin of the southern Apennine Chain and is confined seaward by a straight sandy coast formed during the Last Interglacial and the Holocene. The coastal plain is characterised by beach-dune ridges which interfinger landwards with lagoon and fluvio-palustrine deposits. This belt, which progressively grew up, represents the evolution of a barrier-lagoon system alternatively shifting landwards and seawards. The knowledge on the Holocene evolution of the Sele river coastal plain, along the coast of the Poseidonia-Paestum archaeological area, was improved by the drilling of two new cores and the collection of several archaeo-tephro-stratigraphic data. The area experienced the Holocene marine transgression which cut high cliffs in the travertine deposits. During the second half of the Holocene, the shoreline shifted seawards and a lagoon-beach bar system (Fossa Lupata-Laura) formed. The archaeological remains (VI cent. b.c.) and the Agnano Monte Spina tephra layer (4.1 ky BP) constrain chronologically this morpho-sedimentary system. After the VI cent. b.c., and mostly after the deposition of the 79 a.d. tephra layer, the shoreline shifted seawards and an additional beach ridge formed, while the flat area at the back (Fossa Lupata) was rapidly aggraded and dried up.

The vascular endothelium provides a unique interaction plane for plasma proteins and leukocytes in inflammation. The pro-inflammatory cytokines Tumor Necrosis Factor alpha (TNF alpha) and interleukin 1 beta (IL-1 beta) have a profound effect on endothelial cells, which includes increased levels of adhesion molecules and a disrupted barrier function. To assess the endothelial response to these cytokines at the protein level, we evaluated changes in the whole proteome, cell surface proteome and phosphoproteome after 24 h of cytokine treatment. The effects of TNF alpha and IL-1 beta on endothelial cells were strikingly similar and included changes in proteins not previously associated with endothelial inflammation. Temporal profiling revealed time-dependent proteomic changes, including a limited number of early responsive proteins such as adhesion receptors ICAM1 and SELE. In addition, this approach uncovered a greater number of late responsive proteins, including proteins related to self-antigen peptide presentation, and a transient increase in ferritin. Peptide-based cell surface proteomics revealed extensive changes at the cell surface, which were in agreement with the whole proteome. In addition, site-specific changes within ITGA5 and ICAM1 were detected. Combined, our integrated proteomic data provide detailed information on endothelial inflammation, emphasize the role of the extracellular matrix therein, and include potential targets for therapeutic intervention. Significance: Pro-inflammatory cytokines induce the expression of cell adhesion molecules in vascular endothelial cells. These molecules mediate the adhesion and migration of immune cells across the vessel wall, which is a key process to resolve infections in the underlying tissue. Dysregulation of endothelial inflammation can contribute to vascular diseases and the vascular endothelium is therefore an attractive target to control inflammation. Current strategies targeting endothelial adhesion molecules, including PECAM, CD99, ICAM1 and VCAM1 do not completely prevent transmigration. To identify additional therapeutic targets, we mapped the endothelial proteome after pro-inflammatory cytokine treatment. In addition to the whole proteome, we assessed the surface proteome to focus on cell adhesion molecules, and the phosphoproteome to uncover protein activation states. Here, we present an integrated overview of affected processes which further improves our understanding of endothelial inflammation and may eventually aid in therapeutic intervention of imbalanced inflammation.