Composition and structure of the skin of dromedary (Camelus dromedarius, L. 1758) young adult from two Algerian populations

In the face of climate change, the eco-dromedary seems to adapt to meteorological constraints. This work compares the skin of the forehead, the hump, and the axillary part of two populations of Algerian dromedaries, namely the Sahraoui and Targui. We worked on six young adult dromedaries of two populations and two sexes genders. We removed the skin from the forehead, the hump, and the axillary part; they were fixed in 10% of formalin. After 48 hours of fixation, the different samples were subjected to different stages of histological techniques. Sections were stained with hematoxylineosin. After mounting the slides, we proceeded to microscopic observations and calculations of each layer of skin thickness. The different skin layers were similar in all body regions dromedaries for the two populations. By comparing the thickness of the skin layers of two sexes and two populations, we notice that the skin from the axillary part of male Sahraoui dromedary is the thickest with the measures 0.0413±0.0222 cm, 0.9789±0.1397 cm, and 2.8119±0.1266 cm for epidermis, dermis, and hypodermis, respectively. The thinnest skin was found in the forehead of the male Targui dromedary with 0.0494±0.0095 cm, 0.2191±0.0536 cm, and 0.3302±0.0835 cm for epidermis, dermis, and hypodermis, respectively. The thickness variation of the skin parts of dromedary between sexes in the same population and between the populations suggests an implication of the adaptation system of dromedary to climatic conditions.

Cucurbitacin I elicits the formation of actin/phospho-myosin II co-aggregates by stimulation of the RhoA/ROCK pathway and inhibition of LIM-kinase.

Cucurbitacins are cytotoxic triterpenoid sterols isolated from plants. One of their earliest cellular effect is the aggregation of actin associated with blockage of cell migration and division that eventually lead to apoptosis. We unravel here that cucurbitacin I actually induces the co-aggregation of actin with phospho-myosin II. This co-aggregation most probably results from the stimulation of the Rho/ROCK pathway and the direct inhibition of the LIMKinase. We further provide data that suggest that the formation of these co-aggregates is independent of a putative pro-oxidant status of cucurbitacin I. The results help to understand the impact of cucurbitacins on signal transduction and actin dynamics and open novel perspectives to use it as drug candidates for cancer research.