SIYUAN LIU, YUAN ZHAO, YU YU, DOU YE, QIAN WANG, ZHAOYAN WANG, ZUO LUAN^*

BIOCELL, Vol.48, No.7, pp. 1115-1126, 2024, DOI:10.32604/biocell.2024.050493

Abstract Introduction: Transplantation of mesenchymal stromal cells (MSCs) is a promising therapy for type 1 diabetes (T1D). However, whether the infused MSCs affect the endoplasmic reticulum stress or subsequent unfolded protein response in β cells remains unclear. Methods: To investigate this, we induced early-onset T1D in non-obese diabetic mice using streptozotocin. Subsequently, T1D mice were randomly assigned to receive either MSCs or phosphate-buffered saline. We observed the in vivo homing of MSCs and assessed their effectiveness by analyzing blood glucose levels, body weight, histopathology, pancreatic protein expression, and serum levels of cytokines, proinsulin, and C-peptide. Results: Infused MSCs… More > Graphic Abstract

XUAN SHI^1,2, YUFEN WANG¹, CHENYU LI¹, WANGSHU FU³, XINYUE ZHANG³, AIXIA GONG^1,*

BIOCELL, Vol.48, No.5, pp. 835-845, 2024, DOI:10.32604/biocell.2024.048076

Abstract Background: The incidence of colorectal cancer (CRC) has been increasing in recent years. Thus, the discovery of factors that can assist in alleviating CRC is urgently warranted. Methods: To identify a potential factor involved in the development of CRC, we screened the upregulated genes in tumor tissues through four datasets from an online database. The expression of reticulocalbin 1 (RCN1), a Ca-binding protein, was upregulated in the four datasets. Based on loss-of-function experiments, the effect of RCN1 on cell viability was assessed by Cell Counting Kit-8 (CCK-8) assay. The regulatory effect of RCN1 on apoptosis… More > Graphic Abstract

GIUSEPPINA AMODIO¹, VALENTINA PAGLIARA¹, PAOLO REMONDELLI^1,*, ORNELLA MOLTEDO²

BIOCELL, Vol.46, No.5, pp. 1131-1137, 2022, DOI:10.32604/biocell.2022.018638

Abstract The endoplasmic reticulum (ER) is the site of entry of all proteins that function in the secretory pathway including the extracellular environment. Because it controls the folding of newly synthesized secretory proteins, the ER is indispensable for the maintenance of proteostasis in the secretory pathway. Within the ER and, in part, in post-ER compartments, the quality control of protein folding is under the regulation of the unfolded protein response (UPR) pathways. The UPR strategy is to enhance protein folding, increase the ER degradation pathway of misfolded proteins, and allow the exit from the ER of More >