Abstract
Colon cancer is one of the most common cancer types. Its positive correlation with general obesity has led to increasing amounts of research focusing on the role of adipokines in colon cancer development. Apelin is a peptide released by adipose tissue that could affect many cellular processes connected with carcinogenesis. In this study, we examined the role of apelin in the motility regulation of colon cancer cells. We showed that the effect of four different apelin peptides increased the ability of cancer cells to migrate and invade examined cells trough influencing migratory protrusions formation and actin cytoskeleton rearrangement. Additionally, using confocal microscopy, we noticed that apelin stimulated the proteolytic activity of cancer cells, especially increasing the level of membrane-type 1 matrix metalloprotease. Taken together, apelin increased the movement of colon cancer cells through several possible mechanisms. Moreover, better understanding the process through which apelin regulates cancer development is still necessary to the creation of novel anti-cancer therapy.
Highlights
Colon cancer is an aggressive disease that continues to have a considerable impact on global health
We examined the influence of apelin peptides on colon cancer cell motility
We examined the actin polymerisation state in the cytoplasmic fraction of colon cancer cells incubated with apelin
Summary
Colon cancer is an aggressive disease that continues to have a considerable impact on global health. Strong evidence shows that colorectal cancer is positively correlated with obesity. There are few plausible mechanisms that explain this correlation, including insulin resistance, chronic inflammation and altered levels of growth factors or adipokines [3]. For this reason, studies examining colon cancer biology and its correlation with obesity, which could help find new and more effective diagnostic and therapeutic targets, are still necessary. Apelin is a secreted peptide, synthetized as a 77-amino acid precursor called preproapelin, which belongs to the adipokine family. Preproapelin may generate several active fragments: a 36-amino acid peptide corresponding to the sequence 42–77 (apelin-36), a 17-amino acid peptide consistent with the sequence 61–77 (apelin-17) and a 13-amino acid peptide equivalent to the sequence 65–77
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