A recent study published on January 28, 2025, reveals how exogenous expression of Late Embryogenesis Abundant (LEA) proteins can bolster cold tolerance in mammalian cells by reducing oxidative stress, akin to the well-known antioxidant, Vitamin E. The findings suggest significant potential for improving cell preservation techniques.
The research, conducted by scientists at various institutions, focused on sheep embryonic fibroblasts, which were subjected to low-temperature conditions meant to mimic cold stress. The study revealed intriguing insights, showing LEA proteins could preserve cell viability during cold exposure and resume normal metabolic activity upon warming.
LEA proteins are known for their protective role across various extremophiles and plants under harsh environments. They function by stabilizing proteins, acting as hydration buffers, and maintaining membrane integrity. This study builds on their function, demonstrating for the first time their effectiveness within mammalian systems against cold stress.
During the experiment, two LEA proteins, WCOR410 from wheat and RAB17 from maize, were expressed within the sheep fibroblasts. Over the course of days spent at temperatures of 4°C and 10°C, the viability of the LEA-expressing cells was measured against control groups. Notably, after three days at 4°C, treated cells exhibited significantly higher viability rates compared to the control cells, which almost entirely perished under similar conditions.
Results showed LEA proteins not only improve survival rates but play a key role by mitigating the overproduction of reactive oxygen species (ROS) often triggered by cold exposure. The reduced ROS levels significantly connect LEA proteins with maintaining cellular and mitochondrial integrity, highlighting their dual function as protective agents against both oxidative stress and thermal damage.
"The expression of LEA proteins in mammalian cells exerted cold-protective effect similar to Vitamin E," the researchers noted, underlining the comparative effectiveness of these proteins to traditional antioxidants.
While Vitamin E showed promise during the experiment, the LEA proteins were particularly effective at fostering long-term cell viability, particularly at lower temperatures where cellular apoptosis typically accelerates due to cold-induced stress. The enhanced metabolic activity observed among the LEA-expressing cells points toward their potential for practical applications—most prominently, the preservation of biological materials and tissues intended for transplant.
The experiments conducted illustrated how LEA-positive cells retained more stable mitochondrial morphology after exposure to cold stress, unlike the control groups, which exhibited typical cold-related mitochondrial damage. The cellular metabolism results were similarly favorable, establishing LEA proteins as capable stabilizers during cold-induced metabolic dormancy.
This study suggests exciting avenues for future exploration, not only for improving the efficacy of cryopreservation techniques but also for broader applications within regenerative medicine. The implication of these findings highlights the significance of oxidative stress management, offering insight on new therapeutic strategies to safeguard cell viability under adverse conditions.
Lead researcher, Martina Lo Sterzo, emphasized the broader impact of their findings: "These findings suggest LEA proteins mimic the antioxidant action of Vitamin E, underscoring their potential as valuable tools for introducing cold-resistance strategies in mammalian systems." This reflects the importance of integrating plant-derived proteins for enhancing resilience within mammalian cell samples.
With continued research, the potential for LEA proteins to be utilized as biotechnological tools for improving cell storage and resilience presents a promising frontier for agricultural and medical sciences alike.