Transcriptome analysis of molecular mechanism in inhibition of x-ray or carbon-ion induced lung fibrosis by Fc-Endostatin and its derived peptides

ABSTRACT: Endostatin is a naturally occurring 183-amino acid proteolytic fragment of collagen XVIII that localizes in the basement membrane around blood vessels. The anti-tumor properties of this protein have been extensively described, demarcating endostatin as an endogenous inhibitor of angiogenesis. Further, it supresses many signaling cascades such as pro-inflammatory NF-κB, coagulation and adhesion cascades. Yamaguchi et al. reported that endostatin via its C-terminal domain (E4 peptide) has elicit anti-fibrosis effects. However, the zinc binding domain has been previously confined to the N terminus (endostatin mP1 peptide) and was critical to numerous functions of the molecule. The present study aimed to better understand the impact of oligomerization (Fc-Endostatin) as well as N- vs. C-termin

ORGANISM(S): Mus musculus

SUBMITTER: Christian Schwager 

PROVIDER: E-MTAB-6414 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress