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)

Physiological profiles of 42 middle-aged female marathoners (MAM) (means age = 38.2 yr) were compared with those of 9 young female marathoners (YM) (means age = 25.2 yr), 10 middle-aged female 10-km runners (MATK) (means age = 33.1 yr), and 37 middle-aged sedentary women (MAS) (means age = 38.8 yr). The groups were equivalent for height, maximum heart rate, and hematocrit, and, after adjusting for body size, hemoglobin concentration, lipids, and lipoproteins. Compared to the runners, MAS subjects had significantly higher resting heart rates and significantly lower treadmill performance times, maximum exercise minute ventilation, and VO2max. Compared to YM subjects, MATK runners had higher resting heart rates and lower treadmill performance times, and compared to both groups of marathoners, MATK runners had lower VO2max, but only when expressed relative to body weight. The YM and MAM subjects did not differ from each other except for resting heart rate values, which were higher in the MAM. These data suggest that runners have more favorable cardiorespiratory profiles than do sedentary women, but that lipid and lipoprotein values may be affected more by body size than by activity level.
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PMID:Comparative physiological profiles among young and middle-aged female distance runners. 670 82

We recently cloned the cDNA which encodes a novel megakaryocyte-associated tyrosine kinase termed MATK. In this study, we have cloned and characterized the human MATK gene as well as the murine homolog of human MATK cDNA and performed functional studies of its translated product. Comparison of the deduced amino acid sequences of human and murine MATK cDNAs revealed 85% homology, indicating that MATK is highly conserved in mouse and human. The human gene consists of 13 exons interrupted by 12 introns. The genetic units which encode the SH3 and SH2 domains are located on separate exons. The putative ATP binding site (GXGXXG) is localized on exon 7, and the entire catalytic domain is subdivided into seven exons (7-13). Somatic cell hybrid analysis indicated that human MATK gene is located on chromosome 19 while the murine Matk gene is located on chromosome 10. The immediate 5'-flanking region was highly rich in GC sequences, and potential cis-acting elements were identified including several SP1, GATA-1, APRE, and APRE1. Antisense oligonucleotides directed against MATK mRNA sequences significantly inhibited megakaryocyte progenitor proliferation. Functional studies indicated that MATK can phosphorylate the carboxyl-terminal conserved tyrosine of the Src protein. These results support the notion that MATK acts as a regulator of p60c-src in megakaryocytic cells and participates in the pathways regulating growth of cells of this lineage.
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PMID:Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product. 753 Feb 49

We have cloned a protein tyrosine kinase, MATK, which is expressed abundantly in megakaryocytes and the brain. We investigated whether MATK participates in the c-Kit ligand/stem cell factor (KL/SCF) signaling pathway in the megakaryocytic cell line CMK. After KL/SCF stimulation, five major proteins of molecular masses of 145, 113, 92, 76, and 63 kDa were rapidly and transiently tyrosine-phosphorylated in a time-dependent manner, peaking within 5 min, and returning to basal levels within 60 min. To study the role of MATK in the KL/SCF signaling pathway, glutathione S-transferase (GST) fusion proteins containing SH2 and SH3 domains of MATK were cloned, expressed in Escherichia coli, and purified. MATK-SH2, but not MATK-SH3, precipitated the tyrosine-phosphorylated c-Kit (molecular mass of 145 kDa) in KL/SCF-stimulated CMK cells. Other GST fusion proteins containing the SH2 domain of p85 of phosphatidylinositol 3-kinase, phospholipase C gamma-1, and ras-GAP also precipitated c-Kit. The tyrosine-phosphorylated c-Kit was co-immunoprecipitated with anti-MATK and anti-p85 antibodies in KL/SCF-stimulated CMK cells, but not in granulocyte-macrophage colony stimulating factor or interleukin-6-stimulated cells, suggesting receptor specificity. These results indicate that MATK associates with the c-Kit receptor following specific stimulation by KL/SCF via its SH2 domain and likely participates in transduction of growth signals induced by this cytokine in megakaryocytes.
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PMID:The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit. 753 44

Protein-tyrosine kinases, such as HER-2/ErbB-2, have been specifically linked to breast cancer. The Csk-homologous kinase (CHK), formerly MATK, is a tyrosine kinase that contains the Src homology 2 and 3 (SH2 and SH3) domains and demonstrates homology ( approximately 50%) to the Csk tyrosine kinase. Like Csk, CHK is able to phosphorylate and inactivate Src family kinases. In this report, we investigated whether CHK is expressed in breast cancer tissues and whether it participates in the ErbB-2 signaling pathway in T47D and MCF-7 breast cancer cell lines. Immunostaining of the CHK protein in breast tissues demonstrated that primary invasive ductal carcinomas, stage II (13 of 15 cases) and stage I (8 of 15 cases), expressed the CHK protein, while this protein was not detected in the adjacent normal tissues from the same patients. To study the role of CHK in the ErbB-2 signaling pathway, glutathione S-transferase fusion proteins containing the SH2 and SH3 domains of CHK were generated. CHK-SH2 and CHK-SH3-SH2, but not CHK-SH3 or CHK-NH2-SH3, precipitated the tyrosine-phosphorylated ErbB-2 upon stimulation with heregulin. EGF or interleukin-6 stimulation of T47D cells failed to induce CHK-SH2 association with ErbB-2, the EGF-receptor, or the interleukin-6 receptor. In vivo association of the tyrosine-phosphorylated ErbB-2 with CHK was observed in co-immunoprecipitation studies with anti-CHK antibodies. EGF-R, ErbB-3, and ErbB-4 were not detected in the CHK immunoprecipitates or in the precipitates of the GST-SH2 fusion proteins of CHK, suggesting that the association of CHK with ErbB-2 upon heregulin stimulation is receptor-specific (ErbB-2) and ligand-specific (heregulin). These results indicate that CHK might participate in signaling in breast cancer cells by associating, via its SH2 domain, with ErbB-2 following heregulin stimulation.
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PMID:Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells. 899 72

The Csk homologous kinase (CHK), formerly MATK, has previously been shown to bind to activated c-KIT. In this report, we characterize the binding of SH2(CHK) to specific phosphotyrosine sites on the c-KIT protein sequence. Phosphopeptide inhibition of the in vitro interaction of SH2(CHK)-glutathione S-transferase fusion protein/c-KIT from SCF/KL-treated Mo7e megakaryocytic cells indicated that two sites on c-KIT were able to bind SH2(CHK). These sites were the Tyr568/570 diphosphorylated sequence and the monophosphorylated Tyr721 sequence. To confirm this, we precipitated native CHK from cellular extracts using phosphorylated peptides linked to Affi-Gel 15. In addition, purified SH2(CHK)-glutathione S-transferase fusion protein was precipitated with the same peptide beads. All of the peptide bead-binding studies were consistent with the direct binding of SH2(CHK) to phosphorylated Tyr568/570 and Tyr721 sites. Binding of FYN and SHC to the diphosphorylated Tyr568/570 site was observed, while binding of Csk to this site was not observed. The SH2(CHK) binding to the two sites is direct and not through phosphorylated intermediates such as FYN or SHC. Site-directed mutagenesis of the full-length c-KIT cDNA followed by transient transfection indicated that only the Tyr568/570, and not the Tyr721, is able to bind SH2(CHK). This indicates that CHK binds to the same site on c-KIT to which FYN binds, possibly bringing the two into proximity on associated c-KIT subunits and leading to the down-regulation of FYN by CHK.
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PMID:Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. 903 10

The nuclear 18S rRNA and chloroplast MATK genes of 18 samples of Panax notoginseng and its processed material Sanqi (Radix Notoginseng) were analyzed. The two genes, regardless of cultivar origin, were found to be identical to genotype R1 and M1, respectively, of the published sequences (GenBank accession no. D85171 and AB027526). This phenomenon implies that the species is highly conserved, which is probably caused by the use of the same strain in cultivation and the lack of active mutation in these two genes.
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PMID:Detection of genetic homogeneity of Panax notoginseng cultivars by sequencing nuclear 18S rRNA and plastid matK genes. 1688 Oct 18

The rapidly evolving chloroplast matK gene has nucleotide and amino acid substitution rates suggestive of progression toward a pseudogene state. However, molecular evidence has demonstrated that matK is expressed and functional. We explore in this paper the underlying factors behind the mode and tempo of matK evolution that allow this protein coding gene to accommodate such elevated rates of substitution and yet maintain functionality. Conservative amino acid replacement may reconcile the fast evolutionary rate in matK with conservation in protein function. Based on this premise, we have examined putative amino acid sequences for MATK from across green plants to determine constraint on this protein as indicated by variation in composition of amino acid side chain category. Amino acids in the MATK ORF were divided into six categories based on chemical properties of their side chains: nonpolar, uncharged (pH 7), basic, acidic, aromatic, and "special" (amino acids that specifically affect protein structure, i.e., proline, glycine, and cysteine). The amount of standard deviation (SD) in side chain composition was used as a measure of variation and constraint, where a low SD implied high evolutionary constraint and a high SD implied low constraint. Further, we used secondary structure prediction to evaluate if conservation observed in side chain composition was reflected in stable predicted structure. The results of this study demonstrate evolutionary constraint on MATK, identify three regions of functional importance, show highly conserved secondary structure, and support the putative function of MATK as a group II intron maturase.
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PMID:Evaluating evolutionary constraint on the rapidly evolving gene matK using protein composition. 1809 13

FALLOPIA MULTIFLORA (Thunb.) Harald . has been widely and discriminatingly used in China for the study and treatment of anemia, swirl, deobstruent, pyrosis, insomnia, amnesia, atheroma and also for regulating immune functions. However, there is still confusion about the herbal drug's botanical origins and the phylogenetic relationship between the cultivars and the wild relatives. In order to develop an efficient method for identification, a molecular analysis was performed based on 18 S rRNA gene and partial MATK gene sequences. The 18 S rRNA gene sequences of F. MULTIFLORA were 1809 bp in length and were highly conserved, indicating that the cultivars and the wild F. MULTIFLORA have the same botanical origin. Based on our 18 S rRNA gene sequences analysis, F. MULTIFLORA could be easily distinguished at the DNA level from adulterants and some herbs with similar components. The MATK gene partial sequences were found to span 1271 bp. The phylogenetic relation of F. MULTIFLORA based on the MATK gene showed that all samples in this paper were divided into four clades. The sequences of the partial MATK gene had many permutations, which were related to the geographical distributions of the samples. MATK gene sequences provided valuable information for the identification of F. MULTIFLORA. New taxonomic information could be obtained to authenticate the botanical origin of the F. MULTIFLORA, the species and the medicines made of it.
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PMID:Genetic variation and identification of cultivated Fallopia multiflora and its wild relatives by using chloroplast matK and 18S rRNA gene sequences. 1875 18

Preclinical and clinical studies demonstrate that the omega-3 fatty acids docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA) as a triacylglycerol (TAG) or an ethyl ester are protective against cardiovascular disease. Both have significant TAG-lowering effects. We developed a concentrated ethyl ester of DHA (MATK-90, 900 mg/g) using microalgae as its source. This study evaluated the effects that different doses of MATK-90 had on lipid levels and clinical parameters in male Wistar rats fed a high-fructose diet used to induce hypertriglyceridemia (TAG > or = 300 mg/dL). Effects of MATK-90 were compared to those produced by a pharmaceutical product (Lovaza, formerly Omacor, P-OM3; 465 mg EPA + 375 mg DHA), a TAG oil used in food (DHASCO, algal-DHA, 40% DHA by weight), and a control (corn oil). Doses of MATK-90 (0.6, 1.3, 2.5, 5.0 g kg(-1) day(-1)), algal-DHA (2 g DHA kg(-1) day(-1)), and P-OM3 (5.0 g kg(-1) day(-1)) were administered by oral gavage for 28 days. A significant dose-related decrease was observed in TAG and cholesterol levels in all but the lowest dose of MATK-90 treatment group vs. control. The high-dose group of MATK-90 and the P-OM3 group produced similar reductions in TAG levels.
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PMID:The hypolipidemic effect of an ethyl ester of algal-docosahexaenoic acid in rats fed a high-fructose diet. 1965 88

In this study, we tested the applicability of the core DNA barcode MATK for identifying species within the Fabaceae family. Based on an evaluation of genetic variation, DNA barcoding gaps, and species discrimination power, MATK is a useful barcode for Fabaceae species. Of 1355 plant samples collected from 1079 species belonging to 409 diverse genera, MATK precisely identified approximately 80 % and 96 % of them at the species and genus levels, respectively. Therefore, our research indicates that the MATK region is a valuable marker for plant species within Fabaceae.
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PMID:Identification of Fabaceae plants using the DNA barcode matK. 2054 96


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