Evangelos Falidas1, Eirini Kitsiouli2, Despoina Spyropoulou3, Evangelos Tsiambas4, Asimina Kalogirou5, George Tsouvelas6, Stylianos Papadopoulos2, Michail Mitsis7, Marilena Lekka2, Sofianiki Mastronikoli8, Dimitrios Peschos9, Odysseas Dimas10, Konstantinos Vlachos7. 1. Department of Surgery, Halkida General Hospital, Halkida, Greece. 2. Laboratory of Biochemistry, Chemistry Department, University of Ioannina, Ioannina, Greece. 3. Department of Radiation Oncology, Medical School, University of Patras, Patras, Greece. 4. Department of Cytology, 417 VA (NIMTS) Hospital, Athens, Greece; tsiambasecyto@yahoo.gr. 5. Department of Pathology, Halkida General Hospital, Halkida, Greece. 6. Department of Nursing, University of West Attica, Athens, Greece. 7. Department of Surgery, University Hospital of Ioannina, University of Ioannina, Ioannina, Greece. 8. Brighton and Sussex Medical School, Brighton, U.K. 9. Department of Physiology, Medical School, University of Ioannina, Ioannina, Greece. 10. 2 Department of Internal Medicine, "Gennimatas" General Hospital, Athens, Greece.
Abstract
BACKGROUND/AIM: Phospholipases A2 represent a family of enzymes that regulate the metabolism of phospholipids by hydrolyzing them into fatty acids. Secretory phospholipase A2 (SPLA2) catalyzes the calcium-dependent 2-acyl groups hydrolysis to produce 3-sn-phosphoglycerides. This study aimed to investigate SPLA2 expression in colon adenocarcinoma (CA). MATERIALS AND METHODS: Thirty (n=30) formalin-fixed, paraffin-embedded primary CA tissue sections were used and analyzed. Immunohistochemistry was performed using an anti-SPLA2 antibody. Digital image analysis was also implemented for evaluating objectively the corresponding protein expression levels. RESULTS: Increased SPLA2 protein expression (high & moderate immunostaining levels) was observed in 23/30 (76.6%) cases, whereas 7/30 (23.4%) CA tissues demonstrated low protein levels. High expression levels were detected in 9/30 (30%) cases. SPLA2 overall expression was strongly associated with tumor diameter (p=0.004), whereas other statistically significant associations were not observed (stage: p=0.971, inflammatory infiltration: p=0.795; carcinoma location: p=0.340; differentiation grade: p=0.748; sex: p=0.369; ulceration: p=0.433). CONCLUSION: SPLA2 over-expression is observed in significant subsets of CAs correlating with advanced tumor growth progression (increased diameter). SPLA2 seems to influence endogenous cell responses by its crucial enzymatic activity and can potentially be a biomarker for monitoring CA patients. Copyright
BACKGROUND/AIM: Phospholipases A2 represent a family of enzymes that regulate the metabolism of phospholipids by hydrolyzing them into fatty acids. Secretory phospholipase A2 (SPLA2) catalyzes the calcium-dependent 2-acyl groups hydrolysis to produce 3-sn-phosphoglycerides. This study aimed to investigate SPLA2 expression in colon adenocarcinoma (CA). MATERIALS AND METHODS: Thirty (n=30) formalin-fixed, paraffin-embedded primary CA tissue sections were used and analyzed. Immunohistochemistry was performed using an anti-SPLA2 antibody. Digital image analysis was also implemented for evaluating objectively the corresponding protein expression levels. RESULTS: Increased SPLA2 protein expression (high & moderate immunostaining levels) was observed in 23/30 (76.6%) cases, whereas 7/30 (23.4%) CA tissues demonstrated low protein levels. High expression levels were detected in 9/30 (30%) cases. SPLA2 overall expression was strongly associated with tumor diameter (p=0.004), whereas other statistically significant associations were not observed (stage: p=0.971, inflammatory infiltration: p=0.795; carcinoma location: p=0.340; differentiation grade: p=0.748; sex: p=0.369; ulceration: p=0.433). CONCLUSION: SPLA2 over-expression is observed in significant subsets of CAs correlating with advanced tumor growth progression (increased diameter). SPLA2 seems to influence endogenous cell responses by its crucial enzymatic activity and can potentially be a biomarker for monitoring CA patients. Copyright
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