Abstract
Maspin is a mammary serine protease inhibitor that is encoded by human SERPINB5 gene, and inhibits invasion and metastasis of cancer cells as a tumor suppressor. We performed a systematic meta- and bioinformatics analysis through multiple online databases up to Feb 10, 2017. We found down-regulated maspin expression in gastric cancer, compared with normal mucosa and dysplasia (p < 0.05). Maspin expression was negatively correlated with depth of invasion, TNM staging and dedifferentiation of gastric cancer (p < 0.05). Nuclear maspin expression was higher in intestinal- than diffuse-type carcinoma (p < 0.05). An inverse association between maspin expression and unfavorable overall survival was found in patients with gastric cancer (p < 0.005). According to bioinformatics databases, SERPINB5 mRNA expression was higher in gastric cancer than normal tissues (p < 0.05), and negatively correlated with depth of invasion, TNM staging and dedifferentiation of gastric cancer (p < 0.05). According to KM plotter, we found that a higher SERPINB5 expression was positively correlated with overall and progression-free survival rates of all cancer patients, even stratified by aggressive parameters (p < 0.05). These findings indicated that maspin expression might be employed as a potential marker to indicate gastric carcinogenesis, subsequent progression, and even prognosis.
Highlights
Maspin is a mammary serine protease inhibitor that is encoded by human SERPINB5 gene, and inhibits invasion and metastasis of cancer cells [1, 2]
There appeared the comparison between maspin expression and clinicopathological characteristics of gastric cancer in 19 studies, including sex, depth of invasion, lymph node metastasis, TNM staging and Lauren’s classification
The authors discussed the prognostic significance of maspin expression in 3 articles [33, 35, 36]
Summary
Maspin is a mammary serine protease inhibitor that is encoded by human SERPINB5 gene, and inhibits invasion and metastasis of cancer cells [1, 2]. Cell surfaceassociated, and secretory protein with a reactive center loop that is incompatible with protease inhibition. Maspin has been found to inhibit angiogenesis by stopping the migration, mitogenesis and tube formation of endothelial cells, and to enhance apoptotic sensitivity of cancer cells to extracellular and intracellular stimuli through mitochondria pathway. Odero-Marah et al [7] found that maspin might inhibit cell motility by suppressing Rac and PAK1 activity, and promote cell adhesion via PI3K/ERK pathway. Khalkhali-Ellis et al [8] reported that secretory maspin could deposit in the extracellular milieu and be incorporated into the matrix for tissue remodeling to suppress invasion. Tamazato et al [9] demonstrated that EGFR signaling promoted maspin phosphorylation and nuclear localization, where it inhibited gene transcription directly or via histone deacetylase 1, including CSF-1, Bax, cytokeratin 18, and p21 [10,11,12]
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