Glycated Collagen I (GC) impairs angiogenesis in vitro—A study using an innovative chamber for cell research

Abstract

Studies of cell-matrix, cell-cell interaction, or angiogenesis on different matrices require simultaneous comparison of read-out parameters from differently treated companion cells. The culture conditions (cell number, temperature, volume of culture medium) in different chambers are not completely equalized using conventional methods. It has been reported that cells growing in different environmental conditions may exhibit different proliferation patterns (2). Herein we describe an innovative chamber which could resolve this problem by significantly improving the standardization of experimental conditions. The chamber was manufactured from a standard cell culture well by its division with a septum into two sections. We utilized the chamber and recently developed topological analysis to examine the effects of glycated matrices on the capillary network by endothelial cells. Glycated Collagen I resulted in dose-dependent changes to all measured topological characteristics of the capillary-like network, such as the number of branching points, number of meshes and total capillary length. These differences were observed only in neighbored compartments coated with different matrices, but not in the compartments coated with the same matrix. The novel chamber brings an opportunity for better standardization of experimental conditions and simultaneous observation of different experimental groups, reducing the possible effect of any systematic error.

Impact of the non‐cellular tumor microenvironment on metastasis: Potential therapeutic and imaging opportunities

“…Interestingly, structurally altered collagen resulting from glycation may impact some of the steps in the angiogenic cascade. In this regard, glycated collagen type‐I inhibited endothelial cell cord formation in vitro as compared to non‐glycated collagen (Brodsky et al, 2006). To this end, studies have suggested that glycation near integrin binding RGD sites can impair integrin recognition thus potentially disrupting integrin signaling (Sakata et al, 2000).…”