CaMKII protects MKP-1 from proteasome degradation in endothelial cells

Cellular Signalling

Volumn 26, Issue 10, 2014, Pages 2167-2174

  Ciccarelli, Michele ^a   Rusciano, Maria Rosaria ^b   Sorriento, Daniela ^b   Basilicata, Maria Felicia ^b   Santulli, Gaetano ^b   Campiglia, Pietro ^c   Bertamino, Alessia ^c   De Luca, Nicola ^b   Trimarco, Bruno ^b   Iaccarino, Guido ^a,d   Illario, Maddalena ^b  

^a UNIVERSITY OF SALERNO   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c UNIVERSITY OF SALERNO   (Italy)

^d IRCCS MULTIMEDICA   (Italy)

Author keywords

CaMKII; Endothelial cell; Phosphatases

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; DNA; DUAL SPECIFICITY PHOSPHATASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEASOME; PROTEIN MKP 1; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CALYCULIN A; CANTIDE; DUSP1 PROTEIN, RAT; ENZYME INHIBITOR; INSULIN; LEUPEPTIN; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 1; OLIGONUCLEOTIDE PHOSPHOROTHIOATE; OXAZOLE DERIVATIVE; PROTEIN BINDING; RAF PROTEIN;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL PROLIFERATION; CONTROLLED STUDY; DNA SYNTHESIS; ENDOTHELIUM CELL; ENZYME ACTIVATION; ENZYME DEGRADATION; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; GENE SILENCING; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RAT; ANIMAL; ANTAGONISTS AND INHIBITORS; AORTA; BIOSYNTHESIS; CHEMISTRY; CYTOLOGY; DRUG EFFECTS; GENETICS; METABOLISM; PHOSPHORYLATION; SIGNAL TRANSDUCTION;

ANIMALS; AORTA; CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE TYPE 2; CELL PROLIFERATION; CELLS, CULTURED; DNA; DUAL SPECIFICITY PHOSPHATASE 1; ENDOTHELIAL CELLS; ENZYME INHIBITORS; INSULIN; LEUPEPTINS; MAP KINASE SIGNALING SYSTEM; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; OXAZOLES; PHOSPHOROTHIOATE OLIGONUCLEOTIDES; PHOSPHORYLATION; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-RAF; RATS;

EID: 84904469075     PISSN: 08986568     EISSN: 18733913     Source Type: Journal    
DOI: 10.1016/j.cellsig.2014.06.009     Document Type: Article

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