Effect of an artificial silk elastin-like protein on the migration and collagen production of mouse fibroblasts.

A silk elastin-like protein (SELP) is an artificial compound composing silk fibroin-like and elastin-like tandem repeats. The objective of this study is to evaluate the SELP effect on the migration, proliferation, and proteins production of L929 mouse fibroblasts. Upon culturing with different concentrations of SELP, the cells migration and their collagen production significantly enhanced in the SELP concentrations from 10(-3) to 10 μg/ml.

p120-Catenin is essential for N-cadherin-mediated formation of proper junctional structure, thereby establishing cell polarity in epithelial cells.

The role of p120-catenin in the function of classical cadherins is still enigmatic despite various studies. To elucidate its role, we examined the effect of p120-catenin on the N-cadherin-mediated localization of junctional proteins in epithelial cells in this study. Cadherin-deficient MIA PaCa-2 epithelial cells did not show linear localization of tight junction proteins ZO-1 and occludin.

The extracellular domains of E- and N-cadherin determine the scattered punctate localization in epithelial cells and the cytoplasmic domains modulate the localization.

The accumulation of classical cadherins is essential for their function, but the mechanism is poorly understood. Hence, we investigated the accumulation of E- and N-cadherin and the formation of cell junctions in epithelial cells. Immunostaining revealed a scattered dot-like accumulation of E- and N-cadherin throughout the lateral membrane in MDCK II and other epithelial cells.