No abstract available.
Hair* ; Protein-Tyrosine Kinases* ; Tyrosine*

No abstract available.
Protein-Tyrosine Kinases*

No abstract available.
Introns* ; Point Mutation* ; Protein-Tyrosine Kinases* ; Tyrosine*

Humans ; Histiocytosis ; Receptor Protein-Tyrosine Kinases

No abstract available.
Protein-Tyrosine Kinases ; Pulmonary Disease, Chronic Obstructive ; Tyrosine

Nuclear factor kappaB (NF- kappaB) activation is modulated by various protein kinases. Activation of NF- kappaB is known to be important in the regulation of cell viability. The present study investigated the effect of inhibitors of protein tyrosine kinase (PTK), protein kinase C (PKC) and protein kinase A (PKA) on NF- kappaB activity and the viability of bovine cerebral endothelial cells (BCECs). In serum-deprivation-induced BCEC death, low doses of TNF alpha showed a protective effect. TNF alpha induced NF- kappaB activation within 4 h in serum-deprivation. PTK inhibitors (herbimycin A and genistein) and PKC inhibitor (calphostin C) prevented NF- kappaB activation stimulated by TNF alpha. Likewise, these inhibitors prevented the protective effect of TNF alpha. In contrast to TNF alpha-stimulated NF- kappaB activity, basal NF- kappaB activity of BCECs in media containing serum was suppressed only by calphostin C, but not by herbimycin A. As well BCEC death was also induced only by calphostin C in serum-condition. H 89, a PKA inhibitor, did not affect the basal and TNF alpha-stimulated NF- kappaB activities and the protective effect of TNF alpha on cell death. These data suggest that modulation of NF- kappaB activation could be a possible mechanism for regulating cell viability by protein kinases in BCECs.
Cell Death* ; Cell Survival ; Cyclic AMP-Dependent Protein Kinases ; Endothelial Cells* ; Protein Kinase C ; Protein Kinases* ; Protein-Tyrosine Kinases

BACKGROUND/AIMS: Gastric motor function in patients with advanced gastric cancer (AGC) may dependent upon the extent, depth of invasion, and/or location of cancer. The network of interstitial cell of Cajal (ICC) acts as a pacemaker cell to produce the slow wave, and tyrosine kinase receptor, c-kit plays an important role in development and function of the ICC. We investigated the gastric motor function in patients with advanced gastric cancer, and examined the density of c-kit+ cells in circular muscle layer of the stomach to investigate a possible correlation between gastric motor function and the density of c-kit. METHODS: The subjects include 25 patients operated for non-obstructive AGC. Preoperative electrogastrography (EGG) and gastric emptying (GE) scan were performed in all patients. The frozen samples of circular muscle without cancer infiltration in midantrum and midbody, greater curvature were prepared from resected tissue and immunohistochemistry for c-kit was performed. The density of c-kit was quantitatively analyzed. RESULTS: Several GE parameters including T(1/2) were deranged in patients with AGC, especially antral lesion. There was no significant difference in GE parameters or frequency of slow wave between antrum and body in AGC. The density of c-kit in antrum was greater trend than that in body. No correlation was found among the density of c-kit, T(1/2) and the slow wave frequency. CONCLUSIONS: We observed a delayed gastric emptying in patients with advanced gastric cancer, especially antral lesion without any abnormalities in myoelectrical activity. No correlation was found among T(1/2), slow wave frequency and c-kit density in patients with advanced gastric cancer.
Gastric Emptying ; Humans ; Immunohistochemistry ; Protein-Tyrosine Kinases ; Stomach ; Stomach Neoplasms*

BACKGROUND: The activation of phospholipase C(PLC) is one of the early cellular events in various growth process, including malignant transformation. PLC-gamma1 is activated through direct interaction with growth factor receptor tyrosine kinase. MATERIAL AND METHODS: Using immunoblot assay, we evaluated overexpression of PLC-gamma1 expression in twenty human breast cancer tissues. It was also determined whether there was any connection between other prognostic factors(numbers of metastatic axillary nodes, nuclear and histological grade, c-erbB2, p53 and E-cadherin) and the overexpression of PLC-gamma1 protein. RESULTS: Seventeen of 20 breast cancer tissues showed overexpression of PLC-gamma1, which was corresponded to that seen on the immunohistochemistry( kappa= 0.8275, p = 0.003). Of 3 tumor markers, immunohistochemically determined, positive expression of E-cadherin only was associated with PLC-gamma1 protein overexpression in a range of statistical significance (p=0.045, kappa=0.607). CONCLUSION: PLC-gamma1 overexpression might be pathogenic trigger involved in breast cancer and the relationship between expression of E-cadherin and PLC-gamma1 would require further elucidation.
Breast Neoplasms ; Cadherins ; Humans ; Phospholipases* ; Protein-Tyrosine Kinases ; Biomarkers, Tumor

Sorafenib is a well-known approved systemic therapeutic agent used in patients with advanced hepatocellular carcinoma (HCC). Regorafenib and nivolumab are approved as second-line therapeutic drugs in patients showing disease progression after sorafenib therapy. However, there is no established third- or fourth-line therapy in patients with progression after regorafenib or nivolumab treatment. Recently, the combination of tyrosine kinase inhibitors (TKIs) and immune checkpoint inhibitors (ICPIs) has been attempted as a first-line treatment strategy in advanced HCC patients based on the hypothesis that combination therapy may overcome resistance in ICPI monotherapy. On the basis of this suggestion, we herein describe the case of an HCC patient demonstrating macrovascular invasion, whereby partial remission was achieved via the combination of sorafenib and nivolumab following disease progression after nivolumab therapy. Further studies on the combination of TKIs and ICPIs are necessary to determine ways to manage HCC patients showing disease progression after ICPI therapy.
Carcinoma, Hepatocellular ; Disease Progression ; Humans ; Protein-Tyrosine Kinases

Humans ; Lymphoma, Large-Cell, Anaplastic ; Receptor Protein-Tyrosine Kinases