Composición corporal y somatotipo en triatletas universitarios

Introducción: el triatlón es un deporte de resistencia e individual que está formado por tres disciplinas diferentes: natación, ciclismo y carrera a pie. El objetivo del estudio es describir las características antropométricas en triatletas varones universitarios, además de analizar y describir la composición corporal y el somatotipo de dichos triatletas. Metodología: estudio observacional y descriptivo de las características antropométricas, la composición corporal y el somatotipo de 39 triatletas varones universitarios entre 24 ± 4,5 años, participantes en el campeonato de España universitario de triatlón, modalidad sprint (Alicante 2010), procedentes de diferentes universidades españolas. Según la técnicas de medición antropométrica adoptadas por la International Society for the Advancement of Kinanthropometry (ISAK) y el Grupo Español de Cineantropometría (GREC) por un evaluador acreditado ISAK de nivel II. Resultados: nos encontramos con deportistas de talla baja, en los que destacan valores inferiores a lo normal en los pliegues cutáneos subescapular, supraespinal, tricipital y bicipital, un porcentaje de masa muscular (45,27 ± 3,29%), de masa grasa (10,22 ± 2,92%) y de masa ósea (16,65 ± 1,34%) y un somatotipo en el que predomina la mesomorfia. Discusión: los triatletas y corredores presentan más baja talla que los ciclistas y nadadores. Los triatletas y ciclistas muestran un peso similar, siendo menor que el de los nadadores de fondo y mayor que el de los corredores de 10 km. Los pliegues cutáneos cresta ilíaca, abdominal y muslo frontal de los ciclistas son inferiores al de los triatletas. El porcentaje de masa grasa de triatletas corredores y nadadores son similares; sin embargo, el de la masa muscular de los triatletas suele ser inferior al de los ciclistas pero similar a las demás modalidades. El somatotipo del triatleta se asemeja al del ciclista (mesomorfo). El del corredor es mesomorfo-ectomorfo y el del nadador puede oscilar de mesomorfo a ectomorfo.

Muscle-Type Nicotinic Receptor Blockade by Diethylamine, the Hydrophilic Moiety of Lidocaine

Lidocaine bears in its structure both an aromatic ring and a terminal amine, which can be protonated at physiological pH, linked by an amide group. Since lidocaine causes multiple inhibitory actions on nicotinic acetylcholine receptors (nAChRs), this work was aimed to determine the inhibitory effects of diethylamine (DEA), a small molecule resembling the hydrophilic moiety of lidocaine, on Torpedo marmorata nAChRs microtransplanted to Xenopus oocytes. Similarly to lidocaine, DEA reversibly blocked acetylcholine-elicited currents (IACh) in a dose-dependent manner (IC50 close to 70 μM), but unlike lidocaine, DEA did not affect IACh desensitization. IACh inhibition by DEA was more pronounced at negative potentials, suggesting an open-channel blockade of nAChRs, although roughly 30% inhibition persisted at positive potentials, indicating additional binding sites outside the pore. DEA block of nAChRs in the resting state (closed channel) was confirmed by the enhanced IACh inhibition when pre-applying DEA before its co-application with ACh, as compared with solely DEA and ACh co-application. Virtual docking assays provide a plausible explanation to the experimental observations in terms of the involvement of different sets of drug binding sites. So, at the nAChR transmembrane (TM) domain, DEA and lidocaine shared binding sites within the channel pore, giving support to their open-channel blockade; besides, lidocaine, but not DEA, interacted with residues at cavities among the M1, M2, M3, and M4 segments of each subunit and also at intersubunit crevices. At the extracellular (EC) domain, DEA and lidocaine binding sites were broadly distributed, which aids to explain the closed channel blockade observed. Interestingly, some DEA clusters were located at the α-γ interphase of the EC domain, in a cavity near the orthosteric binding site pocket; by contrast, lidocaine contacted with all α-subunit loops conforming the ACh binding site, both in α-γ and α-δ and interphases, likely because of its larger size. Together, these results indicate that DEA mimics some, but not all, inhibitory actions of lidocaine on nAChRs and that even this small polar molecule acts by different mechanisms on this receptor. The presented results contribute to a better understanding of the structural determinants of nAChR modulation.