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1.
J Sports Med Phys Fitness ; 63(12): 1337-1342, 2023 Dec.
Article in English | MEDLINE | ID: mdl-37712927

ABSTRACT

BACKGROUND: Monitoring muscle damage in athletes assists not only coaches to adjust the training workload but also medical staff to prevent injury. Measuring blood myoglobin concentration can help evaluate muscle damage. The novel portable device utilized in this study allows for easy on-site measurement of myoglobin, providing real-time data on the player's muscle damage. This study investigated the relationship between external load (global positioning system parameters) and internal loads (myoglobin concentration and creatine kinase activity) in 15 male professional football players before and after a match. METHODS: Whole blood samples from participants' fingertips were collected before the match (baseline) and at 2, 16, and 40 h after the match. Myoglobin concentrations were measured using the IA-100 compact immunoassay system. Creatine kinase concentrations were measured in a clinical laboratory, and match loads were monitored using a global positioning system device. RESULTS: The mean myoglobin concentration was significantly higher at 2 h than at the other time points (P<0.05), and decreased to baseline levels within 16 h post-match. The mean creatine kinase concentration increased after the match but did not reach a significant level. Muscle damage monitored by myoglobin after football match-play was strongly associated with acceleration/deceleration metrics rather than the sprint/high-speed running distance. CONCLUSIONS: Our findings indicate that myoglobin is a more sensitive marker of muscle damage than creatine kinase after football match-play. Monitoring myoglobin in athletes can aid in determining their recovery status from the previous training load and help practitioners manage the training load.


Subject(s)
Athletic Performance , Muscles , Myoglobin , Soccer , Humans , Male , Acceleration , Athletic Performance/physiology , Creatine Kinase , Deceleration , Geographic Information Systems , Muscles/injuries , Myoglobin/blood , Soccer/physiology
2.
Pain ; 163(2): 299-307, 2022 02 01.
Article in English | MEDLINE | ID: mdl-33990108

ABSTRACT

ABSTRACT: Arthropods are the largest group of living organisms, and among them, mosquitoes spread parasites and viruses causing deadly diseases. They can easily spread these pathogens because of their painless skin piercing. Although the lack of pain is mainly due to the thinness of their fascicle, it is possible that mosquito saliva, which is discharged during their piercing, might also contribute to it. If mosquito saliva contains antinociceptive substances, it should act on the sensory neurons innervating the epidermis where there are several ion channels that can detect noxious stimuli, such as the transient receptor potential (TRP) channels. We found that mosquito head homogenates and mouse saliva inhibit TRP vanilloid 1 (TRPV1) and TRP ankyrin 1 (TRPA1) channels, either heterologously expressed in HEK293T cells or endogenously expressed in native mouse sensory neurons. Among the different substances contained in mosquito head homogenates or mouse saliva, we have also identified sialorphin as a candidate antinociceptive peptide because it showed similar inhibition effects on TRPV1 and TRPA1. Finally, we confirmed the antinociceptive effects of mosquito head homogenates, mouse saliva, and sialorphin in vivo by observing decreased pain-related behaviors in mice coinjected with these substances. Similar inhibitory effects of mosquito head homogenates and mouse saliva on TRPV1 and TRPA1 suggest that the antinociceptive effects of saliva are universal, which could explain why many animals including humans often lick their wounds. These findings would lead to the development of novel and safe antinociceptive agents.


Subject(s)
Analgesics , Culicidae , Pain , Saliva , TRPA1 Cation Channel , TRPV Cation Channels , Analgesics/metabolism , Animals , Culicidae/metabolism , HEK293 Cells , Humans , Mice , Pain/metabolism , Saliva/metabolism , Sensory Receptor Cells/metabolism , TRPA1 Cation Channel/antagonists & inhibitors , TRPA1 Cation Channel/metabolism , TRPV Cation Channels/antagonists & inhibitors , TRPV Cation Channels/metabolism
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