Title : Angiotensin II stimulates calcium-dependent activation of c-Jun N-terminal kinase.

Pub. Date : 1995 Nov

PMID : 7565768






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Angiotensin II stimulates calcium-dependent activation of c-Jun N-terminal kinase. Calcium mitogen-activated protein kinase 8 Homo sapiens
2 JNK activation following Ang II stimulation did not involve calmodulin; either W-7 nor calmidizolium, in concentrations sufficient to inhibit Ca(2+)/calmodulin-dependent kinase II, blocked JNK activation by Ang II. w-7 nor calmidizolium mitogen-activated protein kinase 8 Homo sapiens
3 In contrast, genistein, in concentrations sufficient to inhibit Ca(2+)-dependent tyrosine phosphorylation, prevented Ang II and thapsigargin-induced JNK activation. Genistein mitogen-activated protein kinase 8 Homo sapiens
4 In contrast, genistein, in concentrations sufficient to inhibit Ca(2+)-dependent tyrosine phosphorylation, prevented Ang II and thapsigargin-induced JNK activation. Tyrosine mitogen-activated protein kinase 8 Homo sapiens
5 In contrast, genistein, in concentrations sufficient to inhibit Ca(2+)-dependent tyrosine phosphorylation, prevented Ang II and thapsigargin-induced JNK activation. Thapsigargin mitogen-activated protein kinase 8 Homo sapiens
6 The inhibition by genistein suggest that Ca(2+)-dependent tyrosine phosphorylation may modulate the JNK pathway in a cell type-specific manner, particularly in cells with a readily detectable Ca(2+)-regulated tyrosine kinase. Genistein mitogen-activated protein kinase 8 Homo sapiens
7 The inhibition by genistein suggest that Ca(2+)-dependent tyrosine phosphorylation may modulate the JNK pathway in a cell type-specific manner, particularly in cells with a readily detectable Ca(2+)-regulated tyrosine kinase. Tyrosine mitogen-activated protein kinase 8 Homo sapiens