8 results on '"Lin, Le"'
Search Results
2. The Expression and Potential Role of Tubulin Alpha 1b in Wilms’ Tumor
- Author
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Yi-Ge Luo, Gang Chen, Jin-Yan Lin, Song-Wu Liang, Jin-Han Gu, Zhi-Guang Huang, Li Gao, Shi-Shuo Wang, Peng Chen, Jun Wang, Jia-Bo Chen, Xia Yang, Qiong-Qian Xu, Lin-Le-Yi Liu, and Li-Ting Qin
- Subjects
Spliceosome ,General Immunology and Microbiology ,Article Subject ,Microarray analysis techniques ,Wilms' tumor ,General Medicine ,Cell cycle ,Biology ,medicine.disease ,Molecular biology ,Wilms Tumor ,General Biochemistry, Genetics and Molecular Biology ,Kidney Neoplasms ,Up-Regulation ,Gene Expression Regulation, Neoplastic ,Downregulation and upregulation ,Tubulin ,medicine ,Medicine ,Humans ,DNA mismatch repair ,KEGG ,Gene ,Research Article - Abstract
We explored the difference in expression of tubulin alpha 1b (TUBA1B) between Wilms’ tumor (WT) and normal tissues (NT) from in-house patients and databases, to determine TUBA1B expression in WT and the predictive pathways of coexpressed genes. In-house RNA-sequencing data were performed with WT and NT from three patients from our institute. Other four RNA-sequencing and microarray data were also downloaded from multiple public databases. The TUBA1B expression between WT and NT was analyzed by Student’s t-test and meta-analysis. The correlation between the expression of TUBA1B and other genes in each study was analyzed. Genes with p<0.05 and r>0.5 were considered as the coexpressing genes of TUBA1B. Overlapping the coexpressed genes of the five studies, including three in-house patients (3 WT vs. 3 NT), GTEx-TARGET (126 WT vs. 51 NT), GSE2172 (18 WT vs. 3 NT), GSE11024 (27 WT vs. 12 NT), and GSE73209 (32 WT vs. 6 NT), were performed with limma and VennDiagram packages in R software. The website of WEB-based GEne SeT AnaLysis toolkit were used to analyze the gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) functional annotations for the overlapped genes. The results showed that the relative expression of TUBA1B in WT tissues from in-house three patients was 280.0086, 141.7589, and 303.8292 and that in NT was 16.5836, 104.8141, and 12.79 (3 WT vs. 3 NT, p=0.0285, ROC=100%, SMD=2.74). Student’s t-test and meta-analysis in all studies revealed that the expression of TUBA1B was upregulated in WT tissues compared to that in NT (p<0.05, SMD=2.89, sROC=0.98). Finally, the research identified the expression of TUBA1B in WT tissues was significantly upregulated than that in NT. The coexpressed genes of TUBA1B were enriched in the pathway of DNA replication, mismatch repair, cell cycle, pathogenic Escherichia coli infection, and spliceosome.
- Published
- 2020
- Full Text
- View/download PDF
3. A physiological basis for variation in the contractile properties of isolated rat heart
- Author
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Lin Le, Saul Winegrad, A. Weisberg, and G. McClellan
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Male ,medicine.medical_specialty ,Physiology ,ATPase ,chemistry.chemical_element ,Stimulation ,Calcium-Transporting ATPases ,In Vitro Techniques ,Myosins ,Calcium ,Biology ,Contractility ,Isoprenaline ,Internal medicine ,Myosin ,Cyclic AMP ,medicine ,Animals ,Actin ,Myocardium ,Heart ,Rats, Inbred Strains ,Myocardial Contraction ,Actins ,Electric Stimulation ,Rats ,Endocrinology ,chemistry ,Biophysics ,biology.protein ,medicine.symptom ,Research Article ,medicine.drug ,Muscle contraction - Abstract
1. The maximum Ca(2+)-activated force, maximum velocity of unloaded shortening and both Ca(2+)- and actin-activated ATPase activities of myosin have been measured in detergent-skinned preparations of isolated bundles of rat right ventricle after exposure of the intact tissue to different conditions of superfusion, mechanical activity and temperature. 2. Maximum Ca(2+)-activated force per unit cross-sectional area decreases with increasing cross-sectional area, and, in the absence of electrical stimulation, with the duration of superfusion. Maximum velocity of unloaded shortening is not influenced by these differences. 3. Actin-activated ATPase activity of myosin decreases as cross-sectional area increases and duration of superfusion increases, but the extent of the decrease in enzymatic activity is less than that of developed force. Ca(2+)-activated ATPase activity is independent of these differences. 4. Actin-activated ATPase activity in cryostatic sections of quickly frozen tissue is not uniform across the transverse section. In thin bundles, it is highest in the centre and lowest at the edge of the section, which correspond, respectively, to the centre and the surface of the tissue bundle. Exposure of the tissue section to 1 microM-cyclic AMP increases the actin-activated ATPase activity of myosin with the largest increase in activity occurring at or near the surface of the bundle. 5. Ca(2+)-activated ATPase activity of myosin is uniform across the transverse section and is not changed by cyclic AMP. 6. Electrical stimulation, elevated Ca2+ concentration in the superfusion medium, or isoprenaline partially or completely reverse the decline in maximum Ca(2+)-activated force produced by prolonged superfusion of the bundle before its skinning. 7. These observations are similar in many ways to those made on frog skeletal muscles by Elzinga, Howarth, Rull, Wilson & Woledge (1989a). An explanation based on the existence of a physiological mechanism for regulating the properties of force generators is proposed. Regulation of the attachment of the cross-bridge to an actin filament may be the basis for the regulatory mechanism.
- Published
- 1991
4. Cyclic AMP regulation of myosin isozymes in mammalian cardiac muscle
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M Tucker, Lin Le, Saul Winegrad, and G. McClellan
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Electrophoresis ,Myosin light-chain kinase ,Physiology ,macromolecular substances ,Myosins ,Isozyme ,Contractility ,Myosin ,Cyclic AMP ,medicine ,Animals ,Phosphorylation ,biology ,Muscles ,Myocardium ,Cardiac muscle ,Articles ,Troponin ,Stimulation, Chemical ,Rats ,Cell biology ,Isoenzymes ,medicine.anatomical_structure ,Biochemistry ,biology.protein ,MYH7 ,medicine.symptom ,Muscle Contraction ,Muscle contraction - Abstract
Hyperpermeable cells from rat heart contain a cAMP-dependent system that can increase the maximum Ca-activated force (contractility) of the contractile proteins. In two different conditions where the relative concentration of the myosin isozymes changes, i.e., hypothyroidism and aging, the size of the increase in contractility from activation of the cAMP-regulated system varies closely with the relative concentration of V1, the isozyme of myosin with the greatest Ca- and actin-activated ATPase activity. The existence of another system for the regulation of the slow isozyme V3 has been demonstrated, and it may be inhibited by beta-adrenergic activity. The possibility of cAMP-dependent myosin regulation of contraction in addition to Ca regulation of troponin is considered. Phosphorylation of the contractile proteins themselves is not required for the increased contractility.
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- 1983
5. Modulation properties of myocardial contractile proteins
- Author
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G. McClellan, Lin Le, S. Winegrad, and S. Weindling
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Contraction (grammar) ,medicine.anatomical_structure ,Active force ,Chemistry ,Kinetics ,Biophysics ,Cardiac muscle ,medicine ,Atpase activity ,Calcium sensitivity ,Cardiac myosin ,Stimulation - Abstract
The development of the active force in the cardiac muscle is related to β-adrenergic stimulation which controls the number of Ca responsible V1 and V3 force generators. The latter influences the amount of tension that can be produced and by altering the ratio of the V1 and V3 force generators, it regulates the kinetics of the contraction.
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- 1987
6. Ca-independent regulation of cardiac myosin
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G. McClellan, Saul Winegrad, S. Weindling, Lin Le, Horowits R, and A. Weisberg
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medicine.medical_specialty ,Adrenergic receptor ,Cell ,Cardiac muscle ,chemistry.chemical_element ,Cardiac myosin ,Calcium ,Biology ,Isozyme ,Endocrinology ,medicine.anatomical_structure ,chemistry ,Internal medicine ,Myosin ,medicine ,Biophysics ,Atpase activity - Abstract
Calcium-independent regulation of the contractile proteins of cardiac muscle has been studied using hyperpermeable cells from rat ventricles and sections of quickly-frozen rat hearts. These preparations have been used to study maximum Ca-activated force, myosin ATPase activity and the maximum velocity of unloaded shortening. Beta adrenergic activity increases the amount of force and the ATPase activity in accordance with the concentration of the V1 isozyme of myosin. V3 activity is decreased at the same time. In tissues containing only V1, there is no change in maximum velocity in response to beta adrenergic stimulation. These results indicate that beta adrenergic stimulation recruits V1 force generators and probably regulates the transition between a Ca unresponsive and a Ca responsive force generator. This type of regulation provides the cell with the ability to operate along many different force-velocity relations.
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- 1987
7. Rapid response of the contractile proteins to hemodynamic changes*1
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Saul Winegrad, Norman S. Kato, Lin Le, G. McClellan, and Andrea S. Weisberg
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medicine.medical_specialty ,business.industry ,Internal medicine ,medicine ,Cardiology ,Hemodynamics ,Cardiology and Cardiovascular Medicine ,business ,Molecular Biology ,Rapid response - Published
- 1989
8. A new sexually transmitted infection (STI) in Geneva? Ciprofloxacin-resistant Neisseria gonorrhoeae, 2002-2005
- Author
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Lin Le, R Pastore, N Liassine, and C Aramburu
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Switzerland ,Population surveillance ,ciprofloxacin ,Neisseria gonorrhoeae ,Medicine - Published
- 2008
- Full Text
- View/download PDF
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