Abstract
BackgroundThe relevance of lysophosphatidylcholine acyltransferase1 (LPCAT1), a cytosolic enzyme in the remodeling pathway of phosphatidylcholine metabolism, in oral squamous cell carcinoma (OSCC) is unknown. We investigated LPCAT1 expression and its functional mechanism in OSCCs.MethodsWe analyzed LPCAT1 mRNA and protein expression levels in OSCC-derived cell lines. Immunohistochemistry was performed to identify correlations between LPCAT1 expression levels and primary OSCCs clinicopathological status. We established LPCAT1 knockdown models of the OSCC-derived cell lines (SAS, Ca9-22) for functional analysis and examined the association between LPCAT1 expression and the platelet-activating factor (PAF) concentration and PAF-receptor (PAFR) expression.ResultsLPCAT1 mRNA and protein were up-regulated significantly (p<0.05) in OSCC-derived cell lines compared with human normal oral keratinocytes. Immunohistochemistry showed significantly (p<0.05) elevated LPCAT1 expression in primary OSCCs compared with normal counterparts and a strong correlation between LPCAT1-positive OSCCs and tumoral size and regional lymph node metastasis. In LPCAT1 knockdown cells, cellular proliferation and invasiveness decreased significantly (p<0.05); cellular migration was inhibited compared with control cells. Down-regulation of LPCAT1 resulted in a decreased intercellular PAF concentration and PAFR expression.ConclusionLPCAT1 was overexpressed in OSCCs and correlated with cellular invasiveness and migration. LPCAT1 may contribute to tumoral growth and metastasis in oral cancer.
Highlights
Lysophosphatidylcholine acyltransferase1 (LPCAT1) is a cytosolic enzyme that catalyzes the conversion of lysophosphatidylcholine (LPC) to phosphatidylcholine (PC) in remodeling the pathway of PC biosynthesis
LPCAT1 mRNA and protein were up-regulated significantly (p
Immunohistochemistry showed significantly (p
Summary
Lysophosphatidylcholine acyltransferase (LPCAT1) is a cytosolic enzyme that catalyzes the conversion of lysophosphatidylcholine (LPC) to phosphatidylcholine (PC) in remodeling the pathway of PC biosynthesis. LPCAT2 is the first detected lyso-PAF acetyltransferase that catalyzes PAF biosynthesis in inflammatory cells such as macrophages, leukocytes, and neutrophils. This enzyme is Ca2+ dependent and activated in response to lipopolysaccharide or Toll-like receptor stimulation. LPCAT1, recently recognized as another lyso-PAF acetyltransferase, is predominantly expressed in lung tissue and its activity is Ca2+ independent. The relevance of lysophosphatidylcholine acyltransferase (LPCAT1), a cytosolic enzyme in the remodeling pathway of phosphatidylcholine metabolism, in oral squamous cell carcinoma (OSCC) is unknown. We investigated LPCAT1 expression and its functional mechanism in OSCCs
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