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Functional analysis of membrane-associated scaffolding tight junction (TJ) proteins in tumorigenic characteristics of B16-F10 mouse melanoma cells.

ABSTRACT: Functional analysis of membrane-associated scaffolding tight junction (TJ) proteins in tumorigenic characteristics of B16-F10 mouse melanoma cells.

PROVIDER: PRJNA1002240 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25516874_1.fastq.gz	Fastqsanger.gz
	SRR25516874_2.fastq.gz	Fastqsanger.gz
	SRR25516875_1.fastq.gz	Fastqsanger.gz
	SRR25516875_2.fastq.gz	Fastqsanger.gz
	SRR25516876_1.fastq.gz	Fastqsanger.gz

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Functional analysis of membrane-associated scaffolding tight junction (TJ) proteins in tumorigenic characteristics of B16-F10 mouse melanoma cells.

Project description:Tight junction (TJ) proteins (Tjps), Tjp1 and Tjp2, are tight junction-associated scaffold proteins that bind to the transmembrane proteins of tight junctions and the underlying cytoskeleton. In this study, we first analyzed the tumorigenic characteristics of B16-F10 melanoma cells, including cell proliferation, migration, invasion, metastatic potential, and the expression patterns of related proteins, after the CRISPR-Cas9-mediated knockout (KO) of Tjp genes. The proliferation of Tjp1 and Tjp2 KO cells significantly increased in vitro. Other tumorigenic characteristics, including migration and invasion, were significantly enhanced in Tjp1 and Tjp2 KO cells.

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Project description:Tight junctions (TJs) are cell-cell adhesion structures that function as barriers between epithelial cells to avoid dehydration, regulate ion permeability and prevent invasion of bacteria and viruses. Disruption of TJs is causative of various inflammatory diseases including inflammatory bowel diseases (IBD), atopic dermatitis and asthma. We identified TJ-inducing small peptides from mouse peritoneum-conditioned medium. The peptides, which we designate junction-inducing peptide like a zipper (Jipper), are 35-40 residue peptides corresponding to the C-terminal region of alpha1-antitrypsin (A1AT), the serine protease inhibitor abundant in circulating blood. Both mouse and human synthetic Jippers, as well as the human A1AT C-terminal peptides cleaved by matrix metalloproteinases (MMPs), induces TJs at cell-cell boundary of epithelial cells. Our study identifies the TJ-inducing peptides in mammalian tissues, and provides a basis for a clinically relevant strategy against TJ barrier-disrupted diseases.

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