ABSTRACT
AIM: The present study aimed at investigating the effect of a 3-week training on biomarkers in professional soccer players during the preseason preparation-period. METHODS: Eight participants (age 22.5±2.2 yrs) were enrolled in the study. During the physical preparation period players have attended a training program (51.9 hours) formulated by coaches of "Equipe-Sicilia-2009". RESULTS: At rest, the lipid profile, the creatine kinase (CK), the lactic-acid dehydrogenase (LDH) and the expression of nuclear receptors peroxisome-proliferator-activated receptors (PPAR α/γ) were analyzed before starting and after 3 weeks of training. The plasma level of CK in our samples showed great variability already in the baseline: value was on average nearly 500 IU/l showed that a large amount of these athletes were a high responders. This biomarker showed a reduction (P<0.01) after 3 weeks of training. No modifications were found in the LDH plasma level, in the lipid profile and in the expression of mRNA of PPAR α/γ and also no significant person's correlations were found among variables. CONCLUSION: In conclusion, we retain that those basal biomarkers, except CK, are not able to assist coaches to better understand training adaptations and overreaching mechanisms during a 3-week of preseason preparation-period. More studies are necessary to confirm these results.
Subject(s)
Creatine Kinase/blood , L-Lactate Dehydrogenase/blood , PPAR alpha/blood , PPAR gamma/blood , Physical Education and Training , Soccer/physiology , Adult , Biomarkers/blood , Humans , PPAR alpha/genetics , PPAR gamma/genetics , RNA, Messenger/blood , Young AdultABSTRACT
Synthesis of H1° histone, in the developing rat brain, is also regulated at post-transcriptional level. Regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs); therefore, we searched for H1° mRNA-interacting proteins. With this aim, we used in vitro transcribed, biotinylated H1° RNA as bait to isolate, by a chromatographic approach, proteins which interact with this mRNA, in the nuclei of brain cells. Abundant RBPs, such as heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP A1, and molecular chaperones (heat shock cognate 70, Hsc70) were identified by mass spectrometry. Western blot analysis also revealed the presence of cold shock domain-containing protein 2 (CSD-C2, also known as PIPPin), a brain-enriched RBP previously described in our laboratory. Co-immunoprecipitation assays were performed to investigate the possibility that identified proteins interact with each other and with other nuclear proteins. We found that hnRNP K interacts with both hnRNP A1 and Hsc70 whereas there is no interaction between hnRNP A1 and Hsc70. Moreover, CSD-C2 interacts with hnRNP A1, Y box-binding protein 1 (YB-1), and hnRNP K. We also have indications that CSD-C2 interacts with Hsc70. Overall, we have contributed to the molecular characterization of a ribonucleoprotein particle possibly controlling H1° histone expression in the brain.