Quantitative Proteomics for Investigation of Secreted Factors: Focus on Muscle Secretome

Henningsen, J.; Blagoev, Blagoy; Kratchmarova, Irina

doi:10.5772/30820

Cited by 1 publication

(1 citation statement)

References 99 publications

(111 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our study has provided solid evidence supporting a novel role of SEMA6A in apoptosis, which can inhibit the growth of lung cancer cells in vitro and in vivo and is regulated by the integral SEMA domain. Previous studies showed that specific protease-induced shedding separates part of the extracellular domain from semaphorins on the plasma membrane, including semaphorin 4 , and semaphorin 5 30 – 32 . Therefore, the extracellular region of SEMA6A may act as a safety pin, which when removed through proteolytic shedding (“uncapped” SEMA6A ) , induces apoptosis.…”

Section: Discussionmentioning

confidence: 99%

The extracellular SEMA domain attenuates intracellular apoptotic signaling of semaphorin 6A in lung cancer cells

et al. 2018

View full text Add to dashboard Cite

Semaphorin 6A (SEMA6A), a membrane-bound protein, is downregulated in lung cancer tissue compared to its adjacent normal tissue. However, the functions of SEMA6A in lung cancer cells are still unclear. In the present study, full length SEMA6A and various truncations were transfected into lung cancer cells to investigate the role of the different domains of SEMA6A in cell proliferation and survival, apoptosis, and in vivo tumor growth. SEMA6A-induced cell signaling was explored using gene silencing, co-immunoprecipitation, and co-culture assays. Our results showed that overexpression of SEMA6A reduced the growth of lung cancer cells in vitro and in vivo, and silencing SEMA6A increased the proliferation of normal lung fibroblasts. Truncated SEMA6A lacking the SEMA domain or the extracellular region induced more apoptosis than full length SEMA6A, and reintroducing the SEMA domain attenuated the apoptosis. Fas-associated protein with death domain (FADD) bound to the cytosolic region of truncated SEMA6A and was involved in SEMA6A-associated cytosol-induced apoptosis. This study suggests a novel function of SEMA6A in inducing apoptosis via FADD binding in lung cancer cells.

show abstract

Section: Discussionmentioning

confidence: 99%