<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(20)</volume><submitter>Chen P</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Monoclonal non-speciﬁc suppressor factor β (MNSFβ) is a ubiquitously expressed member of the ubiquitin-like family. It functions as a regulator of cell apoptosis and a potential tumor suppressor, playing a vital role in the processes of immune cell function and apoptosis.&lt;h4>Methods&lt;/h4>The present study constructed GFP-pMNSFβ swine umbilical vein endothelial cell (SUVEC) lines and investigated the function of porcine MNSFβ (pMNSFβ) in apoptosis, as well as its interactions with pBCL-G. Results revealed that stably expressed pMNSFβ protein in SUVEC lines significantly enhanced staurosporine (STS)-induced apoptosis. pMNSFβ proteins interacted with pBCL-G proteins and the expression of these interacting proteins synergized to further enhance STS-induced apoptosis.&lt;h4>Results&lt;/h4>GFP-pMNSFβ stably expressed SUVEC lines through transient transfection and neomycin screening methods. Over 90% of the SUVEC cultures expressed GFP signals, and 41.5 kDa GFP-pMNSFβ proteins were detected with western blotting methods. Annexin V-PE/PI staining and flow cytometry analyses showed that overexpression of pMNSFβ proteins significantly elevated STS-induced apoptosis rates. Co-immunoprecipitation methods revealed an interaction between pMNSFβ and pBCL-G proteins. BCL-G is a proapoptotic member of the BCL-2 family that has been shown to be misexpressed in human systemic lupus erythematosus, as well as mammary and prostate cancers. Here, we demonstrated that the co-expression and potential conjugation of pMNSFβ and pBCL-G proteins synergistically enhanced STS-induced apoptosis.&lt;h4>Conclusions&lt;/h4>The present study was the first to characterize the function of MNSFβ in porcine cells, and to clarify the function of MNSFβ in apoptosis. These results reveal that pMNSFβ is a potential molecular model for future investigations of diseases related to human MNSFβ dysfunction.</pubmed_abstract><journal>Annals of translational medicine</journal><pagination>1306</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7661876</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Porcine ubiquitin-like protein MNSFβ promotes cell apoptosis and covalently binds to BCL-G to enhance staurosporine-induced apoptosis.</pubmed_title><pmcid>PMC7661876</pmcid><pubmed_authors>Ji C</pubmed_authors><pubmed_authors>Chen P</pubmed_authors><pubmed_authors>Xu C</pubmed_authors><pubmed_authors>Wang X</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Wang J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Porcine ubiquitin-like protein MNSFβ promotes cell apoptosis and covalently binds to BCL-G to enhance staurosporine-induced apoptosis.</name><description>&lt;h4>Background&lt;/h4>Monoclonal non-speciﬁc suppressor factor β (MNSFβ) is a ubiquitously expressed member of the ubiquitin-like family. It functions as a regulator of cell apoptosis and a potential tumor suppressor, playing a vital role in the processes of immune cell function and apoptosis.&lt;h4>Methods&lt;/h4>The present study constructed GFP-pMNSFβ swine umbilical vein endothelial cell (SUVEC) lines and investigated the function of porcine MNSFβ (pMNSFβ) in apoptosis, as well as its interactions with pBCL-G. Results revealed that stably expressed pMNSFβ protein in SUVEC lines significantly enhanced staurosporine (STS)-induced apoptosis. pMNSFβ proteins interacted with pBCL-G proteins and the expression of these interacting proteins synergized to further enhance STS-induced apoptosis.&lt;h4>Results&lt;/h4>GFP-pMNSFβ stably expressed SUVEC lines through transient transfection and neomycin screening methods. Over 90% of the SUVEC cultures expressed GFP signals, and 41.5 kDa GFP-pMNSFβ proteins were detected with western blotting methods. Annexin V-PE/PI staining and flow cytometry analyses showed that overexpression of pMNSFβ proteins significantly elevated STS-induced apoptosis rates. Co-immunoprecipitation methods revealed an interaction between pMNSFβ and pBCL-G proteins. BCL-G is a proapoptotic member of the BCL-2 family that has been shown to be misexpressed in human systemic lupus erythematosus, as well as mammary and prostate cancers. Here, we demonstrated that the co-expression and potential conjugation of pMNSFβ and pBCL-G proteins synergistically enhanced STS-induced apoptosis.&lt;h4>Conclusions&lt;/h4>The present study was the first to characterize the function of MNSFβ in porcine cells, and to clarify the function of MNSFβ in apoptosis. These results reveal that pMNSFβ is a potential molecular model for future investigations of diseases related to human MNSFβ dysfunction.</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Oct</publication><modification>2024-11-12T14:17:58.179Z</modification><creation>2024-11-12T14:17:58.179Z</creation></dates><accession>S-EPMC7661876</accession><cross_references><pubmed>33209886</pubmed><doi>10.21037/atm-20-6348</doi></cross_references></HashMap>