High impact information on PECAM1

• We have earlier reported rapid tyrosine phosphorylation of platelet endothelial cell adhesion molecule-1 (PECAM-1) in ECs exposed to FSS [1].
• Binding of the beads by itself or pulling on the cell surface using poly-l-coated beads did not induce phosphorylation of PECAM-1 and ERK [1].
• When PECAM-1 is tyrosine phosphorylated by FSS or osmotic changes, SHP-2 binds to it [1].
• Downstream activation of intracellular Ca(2+)-independent PLA(2) and/or cytosolic PLA(2) results in the production of arachidonic acid, which in turn serves as a precursor for prostaglandins that subsequently stimulate PECAM-1 expression and cell adhesion [2].
• Lactosylceramide recruits PKCalpha/epsilon and phospholipase A2 to stimulate PECAM-1 expression in human monocytes and adhesion to endothelial cells [2].

Biological context of PECAM1

• Platelet endothelial cell-adhesion molecule-1 (PECAM-1, CD31) is constitutively expressed by vascular endothelium and concentrates at intercellular junctions [3].
• Given that cytokine activation induces profound alterations in endothelial phenotype, studies sought to determine whether cytokine treatment modulated PECAM-1 mRNA and protein content in macro- and microvascular endothelial cells [3].
• Regulation of PECAM-1 expression on endothelial cells may modulate leukocyte trafficking, angiogenesis, and vascular permeability [3].
• Tie2 phosphorylation by flow was significantly inhibited by PECAM1 siRNA treatment [4].
• Platelet endothelial cell adhesion molecule, PECAM-1, modulates cell migration [5].

Anatomical context of PECAM1

• Northern blot analysis revealed expression of PECAM-1 mRNA transcripts in endothelial cells derived from bovine aorta, bovine glomeruli, and human umbilical vein under basal conditions [3].
• Thus, PECAM-1 transfected into a null cell appears to localize to sites of cell-cell contact, promote cell-cell adhesion, and diminish the rate of migration [5].
• Specifically, we transfected NIH/3T3 cells with the full length PECAM-1 molecule (two independent clones) [5].
• Fresh ECs and SMCs were enzymatically isolated, and their separation verified by immunofluorescent detection of alpha-actin and platelet/endothelium cell adhesion molecule (PECAM) proteins, respectively [6].
• Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) is constitutively expressed in endothelial cells, leukocytes, monocytes, lymphocytes, and platelets [7].

Associations of PECAM1 with chemical compounds

• Bromophenacyl bromide (a PLA(2) inhibitor) abrogated LacCer-induced PECAM-1 expression, and this was bypassed by arachidonic acid [2].
• We explored the role of a glycosphingolipid, lactosylceramide (LacCer), in modulating PECAM-1 expression and cell adhesion in human monocytes [2].
• Cells treated with AGM-1470 had a two- to sevenfold (median fivefold) increase in E-selectin mRNA compared with little or no increase in P-selectin, PECAM-1 and VCAM-1 mRNA [8].

Analytical, diagnostic and therapeutic context of PECAM1

• Immunoblots and quantitative indirect immunofluorescence indicated decreased total cellular and cell-surface PECAM-1 protein expression following cytokine treatment [3].
• Immunoprecipitation followed by immunoblotting of lyso-PC-treated BAEC identified p130 as bovine PECAM-1 [9].
• The endothelial cell surface expression of PECAM-1 was determined by flow cytometry (FCM) [10].
• Expression of PECAM-1 mRNA was measured by semi-quantitative reverse transcription-polymerase chain reaction (RT-PCR) with beta-actin as an internal standard, and sequencing of RT-PCR products was performed to confirm the specificity of amplification for PECAM-1 gene [10].

References