Abstract

Soybean agglutinin (SBA), is a non-fiber carbohydrate related protein and a major anti-nutritional factor. Integrins, transmembrane glycoproteins, are involved in many biological processes. Although recent work suggested that integrins are involved in SBA-induced cell-cycle alterations, no comprehensive study has reported whether integrins are involved in SBA-induced cell apoptosis (SCA) in IPEC-J2. The relationship between SBA and integrins are still unclear. We aimed to elucidate the effects of SBA on IPEC-J2 cell proliferation and cell apoptosis; to study the roles of integrins in IPEC-J2 normal cell apoptosis (NCA) and SCA; and to illustrate the relationship and connection type between SBA and integrins. Thus, IPEC-J2 cells were treated with SBA at the levels of 0, 0.125, 0.25, 0.5, 1.0 or 2.0 mg/mL to determine cell proliferation and cell apoptosis. The cells were divided into control, SBA treated groups, integrin inhibitor groups, and SBA + integrin inhibitor groups to determine the integrin function in SCA. The results showed that SBA significantly (p < 0.05) lowered cell proliferation and induced cell apoptosis in IPEC-J2 (p < 0.05). Inhibition of any integrin type induced the cell apoptosis (p < 0.05) and these integrins were involved in SCA (p < 0.05). Even SBA had no physical connection with integrins, an association was detected between SBA and α-actinin-2 ACTN2 (integrin-binding protein). Additionally, SBA reduced the mRNA expression of integrins by down regulating the gene expression level of ACTN2. We concluded an evidence for the anti-nutritional mechanism of SBA by ACTN2 with integrins. Further trials are needed to prove whether ACTN2 is the only protein for connecting SBA with integrin.

Highlights

  • Soybean agglutinin (SBA), known as lectin, is a major anti-nutritional factor that represents 5–7% in soybean

  • The results showed that the SBA could not induce cell apoptosis in addition of integrin inhibitors, indicating that integrins α2, α3, α6, β1 and β4 were involved in SBA-induced cell apoptosis (SCA) in IPEC-J2

  • The results showed that integrins had no direct association with SBA, which was different from Hadari et al [25], who indicated that Galectin-8, termed S-type lectins, can bind to integrin α3, α6 and β1 and inhibit cell adhesion and induce cell apoptosis

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Summary

Introduction

Soybean agglutinin (SBA), known as lectin, is a major anti-nutritional factor that represents 5–7% in soybean. As the structure of SBA has stable characteristics [1], such anti-nutritional factor can resist the enzymatic digestion, and induce deleterious toxic or side effects, including influencing immune response (T lymphocytes activation, inflammation and destroying cancerous cells), interaction between cell-to-cell, cell migration, apoptosis, division, cell proliferation, and signal transduction [1,2,3]. The specific binding of SBA to the intestinal epithelial cells surfaces is the precondition for deleterious toxic or side effects [6]. Weaned pigs supplemented high levels of SBA can bind to intestinal epithelial cell, reduce the epithelial tight junction protein (occludin) expression and increase the mucosal permeability [7]. Of SBA to the intestinal epithelial cells surfaces is the precondition for deleterious toxic or side effects [6]. Weaned pigs supplemented high levels of SBA can bind to intestinal Ienpt.itJ.hMeloila. Sl cci.el2l,01th8,e1n9,r5e8d7 uce the epithelial tight junction protein (occludin) expression and increas2eotfh1e8 mucosal permeability [7]

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