Laminin 511-E8 Fragment Offers Superior Adhesion Properties for Gastric Cancer Cells Compared with Full-Length Laminin 511

Abstract

Background: The interaction between cancer cells and laminin (Ln) is a key event in tumor invasion and metastasis. Previously, we determined the effect of full-length Ln511 on gastric cancer cells. However, the interactions between the Ln511-E8 fragment, a truncated protein of Ln511, and gastric cancer cells have not been investigated. Methods: We investigated the adhesion properties of gastric cancer cells to full-length Ln511 and Ln511-E8 fragments. Results: The proliferation of four gastric cancer cell lines (SH-10-TC, MKN74, SC-6-JCK, and MKN45) was highest on the Ln511-E8 fragment. Further, a larger cytoplasm was observed in SH-10-TC and MKN74 cells cultured on full-length Ln511 or Ln511-E8 fragments. The percentage of adhesive cells was highest on the Ln511-E8 fragment in all four cell lines. Moreover, adhesion of the gastric cancer cells to Ln511-E8 fragment-coated plates was reduced by the Cdc42 GTPase inhibitor in a dose-dependent manner, suggesting the involvement of Cdc42 in the Ln511-E8 fragment-induced enhanced adhesion of gastric cancer cells. Conclusions: The Ln511-E8 fragment had a greater impact on the adhesion, morphology, and proliferation of gastric cancer cells than full-length laminin. Thus, the Ln511-E8 fragment is suitable for investigating the interaction between gastric cancer cells and extracellular matrices in tumor invasion and metastasis.

Heterogeneity and versatility of the extracellular matrix during the transition from pleomorphic adenoma to carcinoma ex pleomorphic adenoma: cumulative findings from basic research and new insights

“…About 16 laminin trimers are reported in vivo. The distribution of laminin isoforms depends on tissue type, and they are important for embryogenesis, organogenesis, angiogenesis, and tissue repair (100)(101)(102). In tumorigenesis, once activated, these proteins promote cell proliferation, migration, differentiation, and metastasis (98,99).…”

“…In tumorigenesis, once activated, these proteins promote cell proliferation, migration, differentiation, and metastasis ( 98 , 99 ). Indeed, laminin facilitates cell migration and invasion in invasive ductal breast cancer ( 103 ), gastric cancer ( 104 ), and bladder cancer ( 105 ). In addition, laminin may be correlated with the immune response in ovarian cancer ( 104 ).…”

“…Indeed, laminin facilitates cell migration and invasion in invasive ductal breast cancer ( 103 ), gastric cancer ( 104 ), and bladder cancer ( 105 ). In addition, laminin may be correlated with the immune response in ovarian cancer ( 104 ).…”

Cell-binding peptides on the material surface guide stem cell fate of adhesion, proliferation and differentiation

“…[71][72][73] The laminin molecules are named according to their heterotrimeric chain composition. Laminin-111 (laminin-1) is composed of a1, b1, and g1 chains; laminin-511 (laminin-10) consists of a5, b1, and g1 chains; 74,75 laminin-332 (laminin-5) is composed of a3, b3, and g2 chains; 76,77 and laminin-521 (laminin-11) contains a5, b2, and g1 chains. [78][79][80] Although xenogenic or allogenic ECM proteins such as native or recombinant laminin molecules are valuable for the culture of hPSCs, hPSC-derived cells and primary cells, ECM proteins should be produced from human cell lines or E. coli, which makes it difficult to chemically define the molecules mixed with ECM proteins after production.…”

“…71–73 The laminin molecules are named according to their heterotrimeric chain composition. Laminin-111 (laminin-1) is composed of α1, β1, and γ1 chains; laminin-511 (laminin-10) consists of α5, β1, and γ1 chains; 74,75 laminin-332 (laminin-5) is composed of α3, β3, and γ2 chains; 76,77 and laminin-521 (laminin-11) contains α5, β2, and γ1 chains. 78–80…”