Inhibition of integrin αVβ6 changes fibril thickness of stromal collagen in experimental carcinomas View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

P. Olof Olsson, Renata Gustafsson, Alexei V. Salnikov, Maria Göthe, Kathrin S. Zeller, Tomas Friman, Bo Baldetorp, Louise A. Koopman, Paul H. Weinreb, Shelia M. Violette, Sebastian Kalamajski, Nils-Erik Heldin, Kristofer Rubin

ABSTRACT

BACKGROUND: Chemotherapeutic efficacy can be improved by targeting the structure and function of the extracellular matrix (ECM) in the carcinomal stroma. This can be accomplished by e.g. inhibiting TGF-β1 and -β3 or treating with Imatinib, which results in scarcer collagen fibril structure in xenografted human KAT-4/HT29 (KAT-4) colon adenocarcinoma. METHODS: The potential role of αVβ6 integrin-mediated activation of latent TGF-β was studied in cultured KAT-4 and Capan-2 human ductal pancreatic carcinoma cells as well as in xenograft carcinoma generated by these cells. The monoclonal αVβ6 integrin-specific monoclonal antibody 3G9 was used to inhibit the αVβ6 integrin activity. RESULTS: Both KAT-4 and Capan-2 cells expressed the αVβ6 integrin but only KAT-4 cells could utilize this integrin to activate latent TGF-β in vitro. Only when Capan-2 cells were co-cultured with human F99 fibroblasts was the integrin activation mechanism triggered, suggesting a more complex, fibroblast-dependent, activation pathway. In nude mice, a 10-day treatment with 3G9 reduced collagen fibril thickness and interstitial fluid pressure in KAT-4 but not in the more desmoplastic Capan-2 tumors that, to achieve a similar effect, required a prolonged 3G9 treatment. In contrast, a 10-day direct inhibition of TGF-β1 and -β3 reduced collagen fibril thickness in both tumor models. CONCLUSION: Our data demonstrate that the αVβ6-directed activation of latent TGF-β plays a pivotal role in modulating the stromal collagen network in carcinoma, but that the sensitivity to αVβ6 inhibition depends on the simultaneous presence of alternative paths for latent TGF-β activation and the extent of desmoplasia. More... »

PAGES

36

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/s12964-018-0249-7

DOI

http://dx.doi.org/10.1186/s12964-018-0249-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1105260045

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29966518


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