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The endothelial lipase protein is promising urinary biomarker for diagnosis of gastric cancer.

Diagnostic pathology (2013-03-21)
Xueyan Dong, Guoqing Wang, Guoqing Zhang, Zhaohui Ni, Jian Suo, Juan Cui, Ai Cui, Qing Yang, Ying Xu, Fan Li
ZUSAMMENFASSUNG

Gastric cancer is one of the most common malignant tumors in the world. Finding effective diagnostic biomarkers in urine or serum would represent the most ideal solution to detecting gastric cancer during annual physical examination. This study was to evaluate the potential of endothelial lipase (EL) as a urinary biomarker for diagnosis of gastric cancer. The expression levels of EL was measured using Western blotting and immunohistochemical staining experiments on (tissue, serum, and urine) samples of gastric cancer patients versus healthy people. We also checked the EL levels in the urine samples of other cancer types (lung, colon and rectum cancers) and benign lesions (gastritis and gastric leiomyoma) to check if EL was specific to gastric cancer. We observed a clear separation between the EL expression levels in the urine samples of 90 gastric cancer patients and of 57 healthy volunteers. It was approximately 9.9 fold average decrease of the EL expression levels in the urine samples of gastric cancer compared to the healthy controls (P <0.0001), achieving a 0.967 AUC value for the ROC (receiver operating characteristic) curve, demonstrating it's highly accurate as a diagnostic marker for gastric cancer. Interestingly, the expression levels of EL in tissue and serum samples were not nearly as discriminative as in urine samples (P = 0.90 and P = 0.79). In immunohistochemical experiments, positive expression of the EL protein was found in 67% (8/12) of gastric adjacent noncancerous and in 58% (7/12) of gastric cancer samples. There was no significant statistical in the expression levels of this protein between the gastric cancer and the matching noncancerous tissues (P =0.67). The urinary EL as a highly accurate gastric cancer biomarker that is potentially applicable to the general screening with high sensitivity and specificity. The virtual slide(s) for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/4527331618757552.

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
Lipase aus Candida rugosa, Type VII, ≥700 unit/mg solid
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Lipase aus Schweinepankreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
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Lipase-Acrylharz aus Candida antarctica, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
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Lipase B Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~9 U/mg
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Lipase aus Schweinepankreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
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Lipase aus Aspergillus niger, powder (fine), ~200 U/g
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Lipase aus Aspergillus oryzae, solution, ≥100,000 U/g, white, beige
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Lipase aus Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
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Lipase aus Candida sp., recombinant, expressed in Aspergillus niger
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Lipase, immobilisiert aus Candida antarctica, beads, slightly brown, >2 U/mg
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Lipase aus Rhizomucor miehei, ≥20,000 U/g
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Lipase aus Pseudomonas cepacia, powder, light beige, ≥30 U/mg
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Lipase aus Weizenkeimen, Type I, lyophilized powder, 5-15 units/mg solid
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Lipase aus Rhizopus oryzae, powder (fine), ~10 U/mg
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Lipase aus Candida rugosa, powder, yellow-brown, ≥2 U/mg
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Lipase aus Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
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Lipase aus Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
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Lipase aus Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
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Lipase aus Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
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Lipase aus Rhizopus niveus, powder (fine), ≥1.5 U/mg
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Lipase A Candida antarctica, rekombinant aus Aspergillus oryzae, powder, beige, ~2 U/mg
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Lipase aus Mucor miehei, powder, slightly brown, ~1 U/mg
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Lipase aus Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)