Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.10.2 (focal adhesion kinase)
44,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Concentrations of Tin (Sn) were determined in botanical, dietary and biological reference materials (RMs), and in human livers from Japanese and American subjects using atomic absorption spectrophotometry (AAS) and neutron activation analysis (NAA), either in the instrumental mode (INAA) or in the radiochemical mode (RNAA). The mean Sn concentrations (+/- 1 S.D.) found in various RMs are: total diet (NIST SRM-1548) 3.57 +/- 0.52 and 3.61 +/- 0.52 microgram/g by AAS and INAA, respectively; non-fat milk powder (NIST SRM-1549) 2.5 +/- 1.4 ng/g and 1.9 +/- 0.3 ng/g; bovine liver (NBS SRM-1577) 18 +/- 2 and 20 +/- 0.3 ng/g; and citrus leaves (NIST SRM-1542) 0.25 +/- 0.02 and 0.243 +/- 0.006 microgram/g by AAS and RNAA, respectively. These comparisons demonstrate good agreement between the two methods. In apple leaves (NIST SRM-1515) and peach leaves (NIST SRM-1547), the measured concentrations by AAS were 77.1 +/- 20 and 85 +/- 15 ng/g; interferences by 160Tb did not permit an accurate assessment by INAA at this concentration. The Sn results obtained for the American human liver specimens by RNAA ranged from 0.135-0.712 microgram/g wet weight, and the Sn concentrations in Japanese human liver specimens determined by AAS ranged from 0.078-1.122 microgram/g wet weight in 23 individuals. The results from this study show that it is feasible to use INAA/RNAA and AAS in combination to establish recommended values in RMs.
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PMID:Determination of tin in biological materials by atomic absorption spectrophotometry and neutron activation analysis. 801 37

Adhesion of human neuroblastoma cells (SK-N-SH clone SY5Y) to laminin or collagen type IV promotes tyrosine phosphorylation of a group of proteins with molecular mass ranging from 100 to 130 kDa and of a protein of 180 kDa. The same pattern of tyrosine phosphorylation was observed when SY5Y cells were allowed to adhere to culture dishes coated with monoclonal antibodies directed to the integrin subunits expressed in the cells, alpha 1, alpha 3, and beta 1, indicating that these receptors are responsible for this signaling mechanism. Using specific antibodies we identified the focal adhesion kinase p125FAK as a component of the 100- to 130-kDa phosphoproteins. Treatment with genistein or herbimycin A, two specific tyrosine kinase inhibitors, greatly reduced the tyrosine phosphorylation of the 100- to 130- and the 180-kDa proteins in response to laminin or collagen IV. Concomitantly, neurite outgrowth on the matrix proteins was strongly inhibited. This effect was observed in two distinct neuroblastoma cell lines, SY5Y and SK-N-BE. Genistein and herbimycin A treatment did not affect cell viability nor cause retraction of preformed neurites. These data suggest that matrix-induced tyrosine phosphorylation events are involved in neurite extension.
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PMID:Role of tyrosine phosphorylation in matrix-induced neurite outgrowth in human neuroblastoma cells. 808 34

Neurotransmitter receptors alter membrane excitability and synaptic efficacy by generating intracellular signals that ultimately change the properties of ion channels. Through expression studies in Xenopus oocytes and mammalian cells, we found that the G protein-coupled m1 muscarinic acetylcholine receptor potently suppresses a cloned delayed rectifier K+ channel through a pathway involving phospholipase C activation and direct tyrosine phosphorylation of the K+ channel. Furthermore, analysis of neuroblastoma cells revealed that a similar tyrosine kinase-dependent pathway links endogenous G protein-coupled receptors to suppression of the native RAK channel. These results suggest a novel mechanism by which neurotransmitters and hormones may regulate a specific type of K+ channel that is widely expressed in the mammalian brain and heart.
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PMID:Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptor. 826 14

The use of consensus values in external quality assessment schemes (EQAS) involves several problems and should preferably be replaced with target values obtained by methods of high metrological level. However, such values are difficult to obtain. In the present study we transferred values from the NIST (former NBS) certified reference serum SRM 909 to lyophilized and frozen test sera for various inorganic components using flame absorption or flame emission spectrometry. Enzyme values were assigned by laboratories of members of the former Scandinavian Enzyme Committee. The assignment was based on 2-4 determinations each day through 3 days of experiment. A total of 10 laboratories participated in the work. The results were utilized in a Danish EQAS. One practical concern is the fairly long time (9 months) which was needed for production, collection and compiling all data. To get an impression of how much dry chemistry analysers, e.g, could influence consensus values a Kodak Ektachem 700 XR was studied using lyophilized and frozen sera. The results are reported in the annex. On NIST SRM 909 the values found for sodium(I) were 6% too high even though the findings on frozen human sera were accurate. For aspartate aminotransferase a result three times the target values was found on a human lyophilized serum, while the values on the frozen sera only were slightly too high.
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PMID:A programme for assigning target values for external quality assessment schemes in countries with no authorized reference laboratories. Annex. Experiences with deviating results on Ektachem 700 XR. 846 50

In the current studies, we examined whether focal adhesion kinase (FAK) and paxillin play a role in insulin-like growth factor-I (IGF-I)-stimulated morphological changes in neuronal cells. In SH-SY5Y human neuroblastoma cells, 10 nM IGF-I enhanced the extension of lamellipodia within 30 min. Scanning electron microscopy and staining with rhodamine-phalloidin showed that these lamellipodia displayed ruffles, filopodia, and a distinct meshwork of actin filaments. Immunofluorescent staining identified focal concentrations of FAK, paxillin, and phosphotyrosine within the lamellipodia. Immunoprecipitation experiments revealed that FAK and paxillin are tyrosine-phosphorylated during IGF-I-stimulated lamellipodial extension. Maximal phosphorylation of FAK and paxillin was observed 15-30 min after the addition of 10 nM IGF-I, whereas maximal IGF-I receptor phosphorylation occurred within 5 min. FAK, paxillin, and IGF-I receptor tyrosine phosphorylation had similar concentration-response curves and were inhibited by the receptor blocking antibody alphaIR-3. These results indicate that FAK and paxillin are tyrosine-phosphorylated during IGF-I-stimulated lamellipodial advance and suggest that the tyrosine phosphorylation of these two proteins helps mediate IGF-I-stimulated cell and growth cone motility. These responses contrast directly with recent reports showing insulin-stimulated dephosphorylation of FAK and paxillin.
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PMID:Tyrosine phosphorylation of paxillin and focal adhesion kinase during insulin-like growth factor-I-stimulated lamellipodial advance. 903 May 91

The method described was developed to be applied in determination of selenium in biological matrices (plasma, urine and tissues) using ETA-AAS with Zeeman background correction. These matrices were obtained from non-fasting S.D. rats and Beagle dogs of both sexes in order to acquire data on the endogenous levels of selenium in these laboratory animals when fed with standard diets. For tissue digestion, a simple procedure using the strong organic base, Soluene 350, was adopted. Precision assays were carried out monitoring Se(IV) levels in spiked matrices (range from 25 to 200 ng) and obtaining relative standard deviations (RSD%) in the range from 3.2% to 14.5% (intra-day) and from 7.6% to 15.9% (inter-day). Accuracy assays gave relative errors (RE%) in the range from -6.5 to 4.2% (intra-day) and from -5.5% to 5.7% (inter-day). The validity of the method was checked on reference material (NBS SRM 1577 bovine liver) and the values obtained correlated with the certified ones. The detection limit assumed was 0.9 ng/ml, whereas the quantitation limit of selenium in matrices ranged from 2 to 5 ng/ml (or g), depending on the kind of sample.
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PMID:Determination of selenium in plasma, urine and tissues, of standard diet-fed rats and dogs by ETA-atomic absorption spectroscopy with Zeeman background correction. 903 61

In the current studies, we investigated the relationship between tyrosine phosphorylation and neurite formation. In SH-SY5Y neuroblastoma cells, the tyrosine kinase inhibitor methyl 2, 5-dihydroxycinnimate blocked neurite formation on laminin. This corresponded with inhibition of paxillin and focal adhesion kinase tyrosine phosphorylation as well as a disruption of actin filament organization and actin polymerization. This suggests that tyrosine phosphorylation helps direct changes in the actin cytoskeleton required for neurite formation.
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PMID:The tyrosine kinase inhibitor methyl 2,5-dihydroxycinnimate disrupts changes in the actin cytoskeleton required for neurite formation. 903 51

Axonal growth cones respond to adhesion molecules and extracellular matrix components by rapid morphological changes and growth rate modification. Neurite outgrowth mediated by the neural cell adhesion molecule (NCAM) requires the src family tyrosine kinase p59(fyn) in nerve growth cones, but the molecular basis for this interaction has not been defined. The NCAM140 isoform, which is found in migrating growth cones, selectively co-immunoprecipitated with p59(fyn) from nonionic detergent (Brij 96) extracts of early postnatal mouse cerebellum and transfected rat B35 neuroblastoma and COS-7 cells. p59(fyn) did not associate significantly with the NCAM180 isoform, which is found at sites of stable neural cell contacts, or with the glycophosphatidylinositol-linked NCAM120 isoform. pp60(c-)src, a tyrosine kinase that promotes neurite growth on the neuronal cell adhesion molecule L1, did not interact with any NCAM isoform. Whereas p59(fyn) was constitutively associated with NCAM140, the focal adhesion kinase p125(fak), a nonreceptor tyrosine kinase known to mediate integrin-dependent signaling, became recruited to the NCAM140-p59(fyn) complex when cells were reacted with antibodies against the extracellular region of NCAM. Treatment of cells with a soluble NCAM fusion protein or with NCAM antibodies caused a rapid and transient increase in tyrosine phosphorylation of p125(fak) and p59(fyn). These results suggest that NCAM140 binding interactions at the cell surface induce the assembly of a molecular complex of NCAM140, p125(fak), and p59(fyn) and activate the catalytic function of these tyrosine kinases, initiating a signaling cascade that may modulate growth cone migration.
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PMID:NCAM140 interacts with the focal adhesion kinase p125(fak) and the SRC-related tyrosine kinase p59(fyn). 907 53

Neuroblastoma is a tumour derived from the sympathoadrenal progenitors of the neural crest. It is one of the most malignant solid tumours in childhood with an annual incidence of 9.4 per 10(6) children under 15 years of age. Recent studies suggest that immunocytological detection of neuroblastoma cells in bone marrow and circulating neuroblasts during treatment may predict clinical outcome and correlate with tumour relapse. The present methods of diagnosing metastasis in neuroblastoma include histological, biochemical and immunohistological analysis. Morphological distinction between tumour cells and primitive lymphoblasts in bone marrow is often difficult, and these methods may also not always be sensitive enough for early detection of the residual and minimally circulating tumor cells. A sensitive assay for detection of such residual cells using two tissue-specific markers, NFM and SYN, by reverse transcriptase-polymerase chain reaction (RT-PCR) is reported here. Analysis of the specificity of this assay in three neuroblastoma cell lines, namely IMR 32, SK-N-SH and SY5Y showed positive expression while control peripheral blood mononuclear cells (HL 60) were negative. In reconstituted cell spiking tests, this method has the ability to detect 1-10(3) neuroblastoma cell in 10(7) normal peripheral blood mononuclear cells (PBMC), as shown by serial dilution and limiting dilution. The NFM marker was found to be a more sensitive marker. The specificity and sensitivity of this technique makes it suitable for future application in detection of minimally disseminated tumour cells in neuroblastoma patients.
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PMID:Detection of low numbers of neuroblastoma cells in vitro. 939 1

The mechanism whereby agonist occupancy of muscarinic cholinergic receptors elicits an increased tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin has been examined. Addition of oxotremorine-M to SH-SY5Y neuroblastoma cells resulted in rapid increases in the phosphorylation of FAK (t(1/2) = 2 min) and paxillin that were independent of integrin-extracellular matrix interactions, cell attachment, and the production of phosphoinositide-derived second messengers. In contrast, the increased tyrosine phosphorylations of FAK and paxillin were inhibited by inclusion of either cytochalasin D or mevastatin, agents that disrupt the cytoskeleton. Furthermore, phosphorylation of FAK and paxillin could be prevented by addition of either wortmannin or LY-294002, under conditions in which the synthesis of phosphatidylinositol 4-phosphate was markedly attenuated. These results indicate that muscarinic receptor-mediated increases in the tyrosine phosphorylation of FAK and paxillin in SH-SY5Y neuroblastoma cells depend on both the maintenance of an actin cytoskeleton and the ability of these cells to synthesize phosphoinositides.
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PMID:Cytoskeletal and phosphoinositide requirements for muscarinic receptor signaling to focal adhesion kinase and paxillin. 948 13


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