Abstract:
:Src-suppressed C kinase substrate (SSeCKS) plays a role in membrane-cytoskeletal remodeling to regulate mitogenesis, cell differentiation, and motility. Previous study showed that lipopolysaccharide (LPS) induced a selective and strong expression of SSeCKS in the vascular endothelial cells of lung. Here we show that LPS stimulation elevated expression of SSeCKS mRNA and protein in Rat pulmonary microvascular endothelial cell (RPMVEC). LPS potentiated SSeCKS phosphorylation in a time- and dose-dependent manner, and partly induced translocation of SSeCKS from the cytosol to the membrane after LPS challenge. The PKC inhibitor, Calphostin C, significantly decreased LPS-induced phosphorylation of SSeCKS, inhibited SSeCKS translocation and actin cytoskeleton reorganization after LPS challenge, suggesting that PKC may play a role in LPS-induced SSeCKS translocation and actin rearrangement. We conclude that SSeCKS is located downstream of PKC and that SSeCKS and PKC are both necessary for LPS-induced stress fiber formation.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Cheng C,Liu H,Ge H,Qian J,Qin J,Sun L,Chen M,Yan M,Shen Adoi
10.1007/s11010-007-9521-7subject
Has Abstractpub_date
2007-11-01 00:00:00pages
1-8issue
1-2eissn
0300-8177issn
1573-4919journal_volume
305pub_type
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