Actinin/genetics* ; Anemia ; Blood Platelets/pathology* ; Female ; Humans ; Male ; Megakaryocytes ; Mutation, Missense ; Pedigree ; Thrombocytopenia/genetics*

Genetic factors play a key role in human athletic ability, and endurance quality and explosive power quality are the important components of athletic ability. In this review, we aimed to reveal the biological genetic mechanism of human athletic ability at the molecular level through summarizing the relationship between genetic variants and human athletic ability, including endurance quality related genetic markers angiotensin converting enzyme (ACE) gene, creatine kinase MM (CKMM) gene and explosive power quality related genetic markers alpha actinin 3 (ACTN3) gene, angiotensinogen (AGT) gene and interleukin6 (IL6) gene. Meanwhile, we also summarized the distribution of allele frequencies among various populations.
Actinin/genetics* ; Athletic Performance ; Gene Frequency ; Genetic Markers ; Genotype ; Humans ; Polymorphism, Genetic

OBJECTIVE: To investigate the regulatory effect of zyxin on the distribution of platelet cytoskeleton. METHODS: Platelets were isolated from zyxin-knockout (Zyx RESULTS: After zyxin gene was knockout, the expressions of cytoskeleton proteins β-actin, α-actinin, filamin A, and myosin Ⅱ A in resting and Jas-induced platelets were significantly increased. In the platelet spreading on fibrinogen surface, F-actin was increased in Zyx CONCLUSION Zyxin significantly regulates the distribution of platelet cytoskeleton, which plays an important role in maintaining platelet cytoskeleton homeostasis.
Actinin ; Actins ; Animals ; Blood Platelets ; Cytoskeleton ; Mice ; Zyxin

BACKGROUND AND OBJECTIVES: Most studies in cardiac regeneration have explored bone marrow mesenchymal stem cells (BM-MSC) with variable therapeutic effects. Amniotic fluid MSC (AF-MSC) having extended self-renewal and multi-potent properties may be superior to bone marrow MSC (BM-MSC). However, a comparison of their cardiomyogenic potency has not been studied yet.METHODS: The 5-azacytidine (5-aza) treated AF-MSC and BM-MSC were evaluated for the expression of GATA-4, Nkx2.5 and ISL-1 transcripts and proteins by quantitative RT-PCR and Western blotting, respectively as well as for the expression of cardiomyogenic differentiation markers cardiac troponin-T (cTNT), beta myosin heavy chain (βMHC) and alpha sarcomeric actinin (ASA) by immunocytochemistry.RESULTS: The AF-MSC as compared to BM-MSC had significantly higher expression of GATA-4 (183.06±29.85 vs. 9.80±0.05; p<0.01), Nkx2.5 (8.3±1.4 vs. 1.82±0.32; p<0.05), and ISL-1 (39.59±4.05 vs. 4.36±0.39; p<0.01) genes as well as GATA-4 (2.01±0.5 vs. 0.6±0.1; p<0.05), NKx2.5 (1.9±0.14 vs. 0.8±0.2; p<0.01) and ISL-1 (1.7±0.3 vs. 0.9±0.1; p<0.05) proteins. The AF-MSC also had significantly elevated expression of cTNT (5.0×10⁴±0.6×10⁴ vs. 3.5 ×10⁴±0.8×10⁴; p<0.01), β-MHC (15.7×10⁴±0.9×10⁴ vs. 8.2×10⁴±0.6×10⁴; p<0.01) and ASA (18.6×10⁴±4.9×10⁴ vs. 13.1×10⁴±3.0×10⁴; p<0.05) than BM-MSC.CONCLUSIONS: Our data suggest that AF-MSC have greater cardiomyogenic potency than BM-MSC, and thus may be a better source of MSC for therapeutic applications in cardiac regenerative medicine.
Actinin ; Amniotic Fluid ; Antigens, Differentiation ; Azacitidine ; Blotting, Western ; Bone Marrow ; Female ; Humans ; Immunohistochemistry ; Mesenchymal Stromal Cells ; Regeneration ; Regenerative Medicine ; Therapeutic Uses ; Troponin T ; Ventricular Myosins

Cardiotrophin-1 (CT-1) activates a distinct form of cardiac muscle cell hypertrophy in which the sarcomeric units are assembled in series. The aim of the study was to determine the expression pattern of sarcomeric contractile protein α-actin, specialized cytoskeletal protein α-actinin and mitochondrial uncoupling protein-2 (UCP2) in myocardial remodeling induced by chronic exposure to CT-1. Kunming mice were intraperitoneally injected with carboxy-terminal polypeptide (CP) of CT-1 (CT-1-CP, 500 μg·kg(-1)· day(-1)) for 1, 2, 3 and 4 week (s), respectively (4 groups obtained according to the injection time, n=10 each, with 5 males and 5 females in each group). Those injected with physiological saline for 4 weeks served as controls (n=10, with 5 males and 5 females). The heart tissues of mice were harvested at 1, 2, 3 or 4 week (s). Immunohistochemistry (IHC) and Western blotting (WB) were used to detect the distribution and expression of sarcomeric α-actin, α-actinin and mitochondrial UCP2 in myocardial tissues. IHC showed that α-actin was mainly distributed around the nuclei of cardiomyocytes, α-actinin concentrated around the striae and UCP2 scattered rather evenly in the plasma. The expression of α-actin was slightly greater than that of α-actinin and UCP2 in the control group (IHC: χ(2)=6.125; WB: F=0.249, P>0.05) and it gradually decreased after exposure to CT-1-CP. There was no significant difference in the expression of α-actin between the control group and the CT-1-CP-treated groups (χ (2)=7.386, P>0.05). But Western blotting revealed significant difference in the expression of α-actin between the control group and the 4-week CT-1-CP-treated group (F=2.912; q=4.203, P<0.05). Moreover, it was found that the expression of α-actinin increased stepwise with the exposure time in CT-1-CP-treated groups and differed significantly between CT-1-CP-treated groups and the control group (ICH: χ (2)=21.977; WB: F=50.388; P<0.01). The expression of UCP2 was initially increased (WB: control group vs. 1- or 2-week group, q values: 5.603 and 9.995, respectively, P<0.01) and then decreased (WB: control group vs. 3-week group, q=4.742, P<0.01; control group vs. 4-week group, q=0.558, P>0.05). It was suggested that long-term exposure to CT-1-CP could lead to the alteration in the expression of sarcomeric α-actin, α-actinin and mitochondrial UCP2. The different expressions of sarcomeric structure proteins and mitochondrial UCP2 may be involved in myocardial remodeling.
Actinin ; biosynthesis ; Actins ; biosynthesis ; Animals ; Cardiomegaly ; chemically induced ; metabolism ; pathology ; Cytokines ; adverse effects ; pharmacology ; Female ; Gene Expression Regulation ; drug effects ; Ion Channels ; biosynthesis ; Male ; Mice ; Mitochondrial Proteins ; biosynthesis ; Myocardium ; metabolism ; pathology ; Sarcomeres ; metabolism ; pathology ; Uncoupling Protein 2

Actinin ; genetics ; Adolescent ; Adult ; Asian Continental Ancestry Group ; genetics ; Athletes ; Athletic Performance ; China ; Ethnic Groups ; genetics ; Female ; Humans ; Male ; Polymorphism, Genetic ; Young Adult

OBJECTIVETo investigate the expression of Junctophilin 1 (JP1) in cardiogenesis of mammalian.

METHODSCardiac differentiation of embryonic stem cells (ESCs) was generated by hanging drop method. Fetal heart was obtained from the rats aged d 14-20 of gestation. The expression of JP1 and JP2 during cardiogenesis of ESCs and rat embryos was analyzed by RT-PCR or Western blotting. Immunofluorescence staining was employed to reveal the distribution of JP1 and JP2 in embryoid body (EB), probing for merging of JP1 and JP2 and cardiac sarcomeric α-Actinin or Troponin-T. Percentage of JP1 and JP2-positive staining cells was analyzed quantitatively by FCS on d17.

RESULTSJP1 mRNA was up-regulated at the early stage (d 5-11) and then decreased. The expression of JP1 protein was up-regulated at the early stage (d 7-9), then decreased gradually and disappeared after d 15. While JP2 gene and protein expression increased in a time-dependent manner during cardiogenesis of rat embryos. The results of immunofluorescence staining showed that there was a parallel co-localization of JP2 with Troponin-T or α-Actinin on d17, while JP1 failed to express in the sarcomeric positive area at the same time point. Furthermore, FCS analysis showed that about 16.59% of cells were JP2-positive, while no cells were stained positively for JP1 in d17 EBs.

CONCLUSIONJP1 gene is expressed during the whole process of cardiogenesis, while JP1 protein only appears on the early stage. The expression of JP1 in cardiogenesis of ESCs is consistent with that of rat embryos.

Actinin ; genetics ; metabolism ; Animals ; Cell Differentiation ; Cell Line ; Embryonic Stem Cells ; cytology ; metabolism ; Heart ; embryology ; Membrane Proteins ; genetics ; metabolism ; Mice ; Mice, Inbred ICR ; Myocytes, Cardiac ; cytology ; metabolism ; RNA, Messenger ; genetics ; Rats ; Troponin T ; genetics ; metabolism

OBJECTIVETo explore the relationship between α-actinin content and cardiac function in rats during myocardial ischemia-reperfusion.

METHODSThirty-two rats were randomized equally into sham-operated group, 30 min ischemia group, 1 h ischemia group, and 1 h ischemia with 2 h reperfusion group. Acute myocardial ischemia was induced in the 3 ischemia groups by ligation of the left anterior descending coronary artery, and the cardiac functions were evaluated. The myocardial contents of α-actinin was measured by immunohistochemistry, and phospholipase C (PLC) and phosphatidylinositol-3-kinase (PI3K) contents were determined by ELISA after the operations.

RESULTSThe left ventricular systolic pressure (LVSP), +dp/dt max, and -dp/dt max tended to decrease during myocardial ischemia, and increased after reperfusion, and the left ventricular end-diastolic pressure (LVEDP) showed reverse changes. The levels of α-actinin decreased with prolonged ischemia, showing a significant difference in 1 h ischemia group from those in the other 3 groups. PI3K and PLC contents were significantly increased with prolonged myocardial ischemia. Stimulation by LY-294002 and U-73122 caused enhanced contraction of single cardiomyocytes, and also increased the fluorescence intensity of α-actinin in the cardiomyocytes compared with that in 1 h ischemia group.

CONCLUSIONSThe cardiac dysfunction during acute ischemia-reperfusion in rats may be related with the changes of myocardial α-actinin content, which are probably a result of increased PI3K and PLC contents in the ischemic myocardium.

Actinin ; metabolism ; Animals ; Myocardial Ischemia ; metabolism ; physiopathology ; Myocardial Reperfusion Injury ; metabolism ; physiopathology ; Myocardium ; metabolism ; Phosphatidylinositol 3-Kinase ; metabolism ; Rats ; Rats, Wistar ; Type C Phospholipases ; metabolism

The aim of this study is to investigate the effects of pulsed electromagnetic fields (PEMFs) on the induction of rat bone marrow mesenchymal stem cells (rBMSCs) to differentiate into cardiomyocytes-like cells in vitro. rBMSCs were randomly divided into PEMFs groups, 5-Azacytidine (5-Aza) groups and control groups. PEMFs groups were exposed to 50 Hz, 1 mT PEMFs for 30 min every day, lasting for 10 d, 15 d and 20 d, respectively. 5-Aza groups were induced by 10 micromol/L 5-Aza for 1 day, then the medium was changed to complete medium without 5-Aza. And control groups were only cultured with complete medium, rBMSCs growth status and morphological features were observed by inverted phase microscope every day. The mRNA expressions of cardiac troponin T (TNNT2) and alpha-actinin (ACTN2) were determined by Real-Time PCR. The results showed that rBMSCs were spindle, polygon or fusiform in control groups. The cells gradually got longer and grew close together after being stimulated by PEMFs and 5-Aza, and with the extension of induction time, the tendency became obvious. At 20th day after PEMFs or 5-Aza treatment, rBMSCs gathered like a long chain, got much longer obviously at the high magnification, and some of them even fused with their neighbors. Compared with control groups, the levels of TNNT2 mRNA expression in 5-Aza groups were 19.40 fold (P < 0.01), 21.02 fold (P < 0.01) and 2.38 fold at 10 d, 15 d, 20 d and the levels of ACTN2 mRNA expression in 5-Aza groups were 6.64 fold (P < 0.01), 6.67 fold (P < 0.01) and 0.76 fold at 10 d, 15 d, 20 d. However, the levels of TNNT2 mRNA expression in PEMFs groups were 15.78 fold (P < 0.01), 6.73 fold (P < 0.05) and 2.73 fold (P < 0.01) of control groups at 10 d, 15 d, 20 d and the levels of ACTN2 mRNA expression in PEMFs groups were 4.93 fold (P < 0.01), 1.89 fold and 0.64 fold, respectively. Compared with 5-Aza groups, the levels of TNNT2 mRNA expression in PEMFs groups were 0.81 fold, 0.32 fold (P < 0.01) and 1.15 fold at 10 d, 15 d, 20 d and the levels of ACTN2 mRNA expression in PEMFs groups were 0.74 fold, 0.28 fold (P < 0.01) and 0.83 fold at 10 d, 15 d, 20 d. PEMFs could contribute to the induction of rat marrow rBMSCs to differentiate into cardiomyocytes-like cells in vitro, and the best exposure time might be 10 days, but further investigation is still needed.
Actinin ; genetics ; metabolism ; Animals ; Bone Marrow Cells ; cytology ; radiation effects ; Cell Differentiation ; radiation effects ; Cells, Cultured ; Electromagnetic Fields ; Mesenchymal Stromal Cells ; cytology ; radiation effects ; Myocytes, Cardiac ; cytology ; radiation effects ; RNA, Messenger ; genetics ; metabolism ; Rats ; Rats, Sprague-Dawley

PURPOSE:This study was designed to clarify the mechanism of proteinuria in nephrotic syndrome patients by using puromycin aminonucleoside (PAN) nephrosis model. METHODS:Following administration of various concentrations of PAN and antioxidants we observed the changes of podocyte cytoskeletons in cultured rat glomerular epithelial cells (GEpC) by method of scanning electron microscope, reactive oxyten species (ROS) analysis, permeability assay, confocal microscope, and Western blot assay. RESULTS:PAN not only induced the ultrastructural changes of GEpC, such as shortening and fusion of microvilli, but also separated the intercellular gaps and linear ZO-1. PAN induced oxidative stresses in time and dose dependent manners and increases of intercellular permeability in anti-oxidants inhibitable manners. High concentration of PAN induced not only actin polymerization and disorganization, but also the conglomerulation and internal dislocation of alpha-actinin protein. The intensities of fluorescences of ZO-1 protein were diminished and internalized by PAN in a dose-dependent manner, which were inhibited by anti anti-oxidants. CONCLUSION:PAN induced the changes of podocytes cytoskeleton and junctional barriers by way of increasing ROS in GEpC that resulted in increasing their permeability in a antioxidatn-inhibitable manner. Glomerular hyperpermeability induced by PAN mediateing through oxidative stresses is thought to take part in the mechanism of proteinuria in nephrotic syndrome. (Korean J Pediatr 2008;51:54-61)
Actinin ; Actins ; Animals ; Antioxidants ; Ascorbic Acid ; Blotting, Western ; Cytoskeleton ; Dislocations ; Electrons ; Epithelial Cells ; Glycyrrhetinic Acid ; Humans ; Microvilli ; Nephrosis ; Nephrotic Syndrome ; Oxidative Stress ; Permeability ; Podocytes ; Polymerization ; Polymers ; Proteinuria ; Puromycin ; Puromycin Aminonucleoside ; Rats