Bovine coronary artery endothelial cells

Rosolowsky, M. and Campbell, W. B., Synthesis of hydroxyeicosatetraenoic (HETES) and epoxyeicosatrienoic acids (EETS) by cultured bovine coronary artery endothelial cells, Biochim. Biophys. Acta, 1299, 267, 1996. 

The applicability of polyphosphazenes in TE has been tested several times with osteoblasts, see Section 4.3.1 such evaluations have also been performed with endothelial cells (EC). Nair and coworkers chose bovine coronary artery endothelial cells (BCAEC) and investigated the usability of nonwoven NF meshs based on electrospun PNmPh as scaffolds (see Section 4.2.1.1 and Figure 4.4). Figure 4.19 demonstrates clearly that the NF mats support the adhesion of the BCAEC. 

BCAEC Bovine coronary artery endothelial cells... 

The regulation of eNOS activity by phosphorylation is a well documented subject as the eNOS protein possess several consensus sequences for phosphorylation by protein kinase A (PKA), protein kinase C (PKC), protein kinase B (Akt/PKB) and AMP-activated protein kinase (AMPK). The eNOS enzyme has been reported to be phosphorylated on threonine, serine and t50 osine residues in response to various agonists. Many studies have shown that phosphorylation of eNOS on serine 1177 leads to an activation of eNOS [26-29], whereas phosphorylation on threonine 495 inactivates eNOS as this site is in the Ca Vcalmodulin binding domain [26]. Fleming et al. (2001) demonstrated that bradykinin (100 nM) increased eNOS activity in both porcine coronary artery endothelial cells (PCAE) and HUVEC via dephosphorylation of threonine 495 and phosphorylation of serine 1177 [30]. The bradykinin-induced phosphorylation of serine 1177 was abolished in the presence of a calmodulin dependent kinase II inhibitor whilst the dephosphorylation of threonine 495 was abolished by a protein phosphatase I inhibitor [30]. Harris et al. (2001) documented in BAEC that bradykinin (1 pM)-induced eNOS activity was mediated by activation of Akt/PKB [31] (see section 1.2.2) resulting in NOS phosphorylation at serine 1179 (bovine sequence) and a de-phosphorylation at threonine 497 mediated by calcineurin phosphatase. Typically, phosphorylation of eNOS at either of these sites is coordinated with dephosphorylation at the alternate site. 

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