Publications by authors named "C Camy"

The Achilles tendon enthesis (ATE) anchors the Achilles tendon into the calcaneus through fibrocartilaginous tissue. The latter is enriched in type II collagen and proteoglycans (PGs), both of which give the enthesis its capacity to withstand compressive stress. Because unloading and reloading induce remodeling of the ATE fibrocartilage (Camy et al.

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The fibrocartilaginous tendon enthesis, i.e. the site where a tendon is attached to bone through a fibrocartilaginous tissue, is considered as a functionally graded interface.

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Article Synopsis
  • The study investigates how mechanical loading affects the structure and mechanical properties of the Achilles tendon enthesis after deconditioning from hindlimb suspension in mice.
  • Key findings include a severe reduction in the non-calcified fibrocartilage surface area and collagen disorganization after 14 days of unloading, but reloading for 6 days improved these features and enhanced collagen II expression.
  • The research highlights that unloading decreased the stiffness of the enthesis and changed the failure site, but reloading restored the original function, which is important for countermeasure exercises in spaceflight contexts.
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Exposure to chronic skeletal muscle disuse and unloading that astronauts experience results in muscle deconditioning and bone remodeling. Tendons involved in the transmission of force from muscles to skeleton are also affected. Understanding the changes that occur in muscle, tendon, and bone is an essential step toward limiting or preventing the deleterious effects of chronic reduction in mechanical load.

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Article Synopsis
  • The type VI secretion system (T6SS) functions like a nano-spear gun, using a spring mechanism to inject effectors into target cells, reshaping bacterial communities and manipulating host defenses.
  • The membrane complex (MC) involved in T6SS assembly is made up of three proteins, TssJ, TssM, and TssL, which are recruited in a specific order to facilitate effector delivery.
  • TagL, a protein associated with the T6SS in enteroaggregative bacteria, has a peptidoglycan-binding domain and an N-terminal region that interacts with TssL, playing a role in T6SS assembly but not in baseplate docking.
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