Role of tyrosine kinase activity in 2,2′,2′-tripyridine-induced nitric oxide generation in macrophages

1999 ◽  
Vol 57 (12) ◽  
pp. 1367-1373 ◽  
Author(s):  
Bor-Sen Wang ◽  
Jen-Kun Lin ◽  
Shoei-Yn Lin-Shiau
Keyword(s):  
Nitric Oxide ◽  
Tyrosine Kinase ◽  
Kinase Activity ◽  
Tyrosine Kinase Activity

The Role of Anaplastic Lymphoma Kinase in Human Cancers

2013 ◽  
Vol 09 (02) ◽  
pp. 149 ◽  
Author(s):  
Alejandro García-Regalado ◽  
Claudia Haydée González-De la Rosa ◽  
◽  
Keyword(s):  
Tyrosine Kinase ◽  
Anaplastic Lymphoma Kinase ◽  
Kinase Activity ◽  
New Drugs ◽  
Tyrosine Kinase Activity ◽  
Mutant Proteins ◽  
Anaplastic Lymphoma ◽  
Attractive Therapeutic Target ◽  
Pathway Inhibition

The anaplastic lymphoma kinase (ALK) is a receptor with tyrosine kinase activity, which regulates the development and maintenance of the nervous system. Mutations or amplification in ALK promote tumorogenesis and progression of diverse types of cancer, which makes it an attractive therapeutic target against cancer diseases. Inhibition of its tyrosine kinase activity with small molecules, such as crizotinib, reveals tumor reversion; however, secondary mutations and amplification of the gene mediate resistance to treatment. In this article, we discuss the emerging role of possible therapeutic targets that could overcome the resistance to ALK inhibition in cancer, such as inhibition of other kinases involved in the pathway, inhibition of ALK mutant proteins through the development of new drugs based on its crystallography, and the use of antibodies against ALK.

Protein tyrosine kinase activity regulates nitric oxide synthase induction in rat hepatocytes

1997 ◽  
Vol 272 (2) ◽  
pp. G207-G214 ◽  
Author(s):  
D. R. Miller ◽  
J. M. Collier ◽  
R. E. Billings
Keyword(s):  
Nitric Oxide ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Rat Hepatocytes ◽  
Tnf Alpha ◽  
Tyrosine Kinase Activity ◽  
Protein Tyrosine ◽  
Oxide Synthase ◽  
Protein Tyrosine Kinase Activity

Regulation of induced nitric oxide synthase (NOS) in isolated rat hepatocytes is poorly understood. The specific protein tyrosine kinase inhibitor genistein was used to determine if NOS induction is dependent on protein tyrosine kinase activation. Genistein inhibited tumor necrosis factor-alpha (TNF-alpha)-stimulated induction of NOS activity and NOS protein in a dose-dependent manner. Genistein also impaired TNF-alpha-induced NOS mRNA accumulation, suggesting protein tyrosine kinase regulation of NOS induction occurred at the level of transcription-translation. Like TNF-alpha, genistein inhibited induction of NOS protein by a second proinflammatory cytokine, interleukin-1beta, suggesting similar activation mechanisms by proinflammatory cytokines. NOS induction by other stimuli, including phorbol 12-myristate 13-acetate and the superoxide-generating system xanthine/xanthine oxidase, was also inhibited by genistein. Finally, cytokine-stimulated protein tyrosine kinase activity in hepatocytes was demonstrated by increased tyrosine phosphorylation of five high molecular mass protein bands. Genistein inhibited this cytokine-induced phosphotyrosine increase. The commonality of genistein inhibition suggests that protein tyrosine kinase activity is critical for NOS induction by a variety of stimuli.

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