Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tetramethylpyrazine is the active ingredient of a Chinese herbal medicine. In this study, tetramethylpyrazine was tested for its activities in irradiated bone marrow stromal QXMSC1 cells. The proliferation of QXMSC1 cells was measured by MTS assay kit and flow cytometry. To identify proteins involved in the processes of cellular and molecular response of tetramethylpyrazine to irradiation damage, we comparatively analyzed the proteome of nonirradiated, irradiated and tetramethylpyrazine treated QXMSC1 cells. Reverse transcriptase polymerase chain reaction (RT-PCR) were used to validate the differentially expressed proteins. 20 Gy 60Co gamma irradition inhibited QMSC1 cells growth and tetramethylpyrazine could reverse of this action due to stimulating QXMSC1 cells from G1 to S progression. Proteomic analytical results showed that 18 spots were changed in irradiated QXMSC1 cells, and 15 spots matched with known proteins after database searching. The expression level of proteins such as translationally controlled tumor protein (TCTP), and galectin-3, were increased in irradiated QXMSC1 cells, while calmodulin, pyruvate kinase were decreased. Tetramethylpyrazine could prevent this change or reverse to some degree. The function of these proteins involves in hematopoiesis, cell cycle and signal transduction. The changes of these proteins were confirmed by RT-PCR at mRNA levels. This study suggested that stimulating proliferation via tetramethylpyrazine played an important role in the cure effect on irradiated QXMSC1 cells and was helpful to deeply understand the mechanism of tetramethylpyrazine at the molecular level.
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PMID:Proteomic analysis of the effects of tetramethylpyrazine on irradiated QXMSC1 cells. 1726 90

Blood-accessible molecular biomarkers are becoming highly attractive tools to assess disease progression and response to therapies in Duchenne muscular dystrophy (DMD) especially in very young patients for whom other outcome measures remain subjective and challenging. In this study, we have standardized a highly specific and reproducible multiplexing mass spectrometry method using the tandem mass tag (TMT) strategy in combination with depletion of abundant proteins from serum and high-pH reversed-phase peptide fractionation. Differential proteome profiling of 4 year-old DMD boys (n = 9) and age-matched healthy controls (n = 9) identified 38 elevated and 50 decreased serum proteins (adjusted P < 0.05, FDR <0.05) in the DMD group relative to the healthy control group. As expected, we confirmed previously reported biomarkers but also identified novel biomarkers. These included novel muscle injury-associated biomarkers such as telethonin, smoothelin-like protein 1, cofilin-1, and plectin, additional muscle-specific enzymes such as UTP-glucose-1-phosphate uridylyltransferase, aspartate aminotransferase, pyruvate kinase PKM, lactotransferrin, tissue alpha-l-fucosidase, pantetheinase, and ficolin-1, and some pro-inflammatory and cell adhesion-associated biomarkers such as leukosialin, macrophage receptor MARCO, vitronectin, galectin-3-binding protein, and ProSAAS. The workflow including serum depletion, sample processing, and mass spectrometry analysis was found to be reproducible and stable over time with CV < 20%. Furthermore, the method was found to be superior in terms of specificity compared to other multiplexing affinity-based methods. These findings demonstrate the specificity and reliability of TMT-based mass spectrometry methods in detection and identification of serum biomarkers in presymptomatic young DMD patients.
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PMID:Tandem Mass Tag-Based Serum Proteome Profiling for Biomarker Discovery in Young Duchenne Muscular Dystrophy Boys. 3311 Sep 78