{"title":"急性髓性白血病(AML-M5)细胞谱系中亚型特异性抗n - cor OSGEP蛋白酶的鉴定和表征","authors":"Sam Annie Jeyachristy, Eshan Rosly Nazem, Ramesh Thevendran, Ahsas Goyal, Kavita Goyal, Solayappan Maheswaran, Atreyi Pramanik, Gaurav Gupta, Neeraj Kumar Fuloria, Shivkanya Fuloria, Md Sadique Hussain","doi":"10.1007/s10529-025-03630-3","DOIUrl":null,"url":null,"abstract":"<p><p>Acute myeloid leukemia (AML) is a neoplastic disorder of the myeloid stem cell and is most commonly diagnosed in children and young adults. N-CoR is an essential protein that regulates transcriptional repression in normal myeloid cell development Mutations or loss of function in the N-CoR gene result in the abnormal expression of critical genes involved in cell proliferation, contributing to leukemogenic transformation and the development of malignancy in acute myeloid leukemia subtype M5 (AML-M5). This study was aimed to elucidate the mechanism of N-CoR degradation by O-sialo-glycoprotein endopeptidase (OSGEP), a protease that is active in AML-M5 cells only. The AML-M5-specific proteases were isolated using HPLC size exclusion chromatography and anti-N-CoR OSGEP antibodies. In vitro experiments were performed to test the degradation of recombinant N-CoR protein by OSGEP protease. The protease's identity and composition were analyzed via mass spectrometry. Study involved transfection studies using various cell lines to evaluate the subtype-specific activity of OSGEP based on N-CoR expression levels. Study findings revealed OSGEP protease to cleave N-CoR in AML-M5 cells. Mass spectrometry confirmed the identity and composition of a purified, functionally active form of the OSGEP protease. The transfection studies proved that N-CoR was the only protein of the two that OSGEP protease acted on selectively in AML-M5 cells thus proving its specificity in the subtype of cells. Findings of present study suggests that OSGEP protease-mediated N-CoR degradation is an important factor in the development of AML-M5. Current study highlights N-CoR degradation by OSGEP as a key molecular event in AML-M5 and proposes the N-CoR protease as a potential diagnostic and therapeutic biomarker for this leukemia subtype.</p>","PeriodicalId":8929,"journal":{"name":"Biotechnology Letters","volume":"47 5","pages":"90"},"PeriodicalIF":2.1000,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification and characterisation of subtype-specific anti-N-CoR OSGEP protease in acute myeloid leukaemia (AML-M5) cell lineage.\",\"authors\":\"Sam Annie Jeyachristy, Eshan Rosly Nazem, Ramesh Thevendran, Ahsas Goyal, Kavita Goyal, Solayappan Maheswaran, Atreyi Pramanik, Gaurav Gupta, Neeraj Kumar Fuloria, Shivkanya Fuloria, Md Sadique Hussain\",\"doi\":\"10.1007/s10529-025-03630-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Acute myeloid leukemia (AML) is a neoplastic disorder of the myeloid stem cell and is most commonly diagnosed in children and young adults. N-CoR is an essential protein that regulates transcriptional repression in normal myeloid cell development Mutations or loss of function in the N-CoR gene result in the abnormal expression of critical genes involved in cell proliferation, contributing to leukemogenic transformation and the development of malignancy in acute myeloid leukemia subtype M5 (AML-M5). This study was aimed to elucidate the mechanism of N-CoR degradation by O-sialo-glycoprotein endopeptidase (OSGEP), a protease that is active in AML-M5 cells only. The AML-M5-specific proteases were isolated using HPLC size exclusion chromatography and anti-N-CoR OSGEP antibodies. In vitro experiments were performed to test the degradation of recombinant N-CoR protein by OSGEP protease. The protease's identity and composition were analyzed via mass spectrometry. Study involved transfection studies using various cell lines to evaluate the subtype-specific activity of OSGEP based on N-CoR expression levels. Study findings revealed OSGEP protease to cleave N-CoR in AML-M5 cells. Mass spectrometry confirmed the identity and composition of a purified, functionally active form of the OSGEP protease. The transfection studies proved that N-CoR was the only protein of the two that OSGEP protease acted on selectively in AML-M5 cells thus proving its specificity in the subtype of cells. Findings of present study suggests that OSGEP protease-mediated N-CoR degradation is an important factor in the development of AML-M5. Current study highlights N-CoR degradation by OSGEP as a key molecular event in AML-M5 and proposes the N-CoR protease as a potential diagnostic and therapeutic biomarker for this leukemia subtype.</p>\",\"PeriodicalId\":8929,\"journal\":{\"name\":\"Biotechnology Letters\",\"volume\":\"47 5\",\"pages\":\"90\"},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2025-08-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biotechnology Letters\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1007/s10529-025-03630-3\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biotechnology Letters","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s10529-025-03630-3","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
Identification and characterisation of subtype-specific anti-N-CoR OSGEP protease in acute myeloid leukaemia (AML-M5) cell lineage.
Acute myeloid leukemia (AML) is a neoplastic disorder of the myeloid stem cell and is most commonly diagnosed in children and young adults. N-CoR is an essential protein that regulates transcriptional repression in normal myeloid cell development Mutations or loss of function in the N-CoR gene result in the abnormal expression of critical genes involved in cell proliferation, contributing to leukemogenic transformation and the development of malignancy in acute myeloid leukemia subtype M5 (AML-M5). This study was aimed to elucidate the mechanism of N-CoR degradation by O-sialo-glycoprotein endopeptidase (OSGEP), a protease that is active in AML-M5 cells only. The AML-M5-specific proteases were isolated using HPLC size exclusion chromatography and anti-N-CoR OSGEP antibodies. In vitro experiments were performed to test the degradation of recombinant N-CoR protein by OSGEP protease. The protease's identity and composition were analyzed via mass spectrometry. Study involved transfection studies using various cell lines to evaluate the subtype-specific activity of OSGEP based on N-CoR expression levels. Study findings revealed OSGEP protease to cleave N-CoR in AML-M5 cells. Mass spectrometry confirmed the identity and composition of a purified, functionally active form of the OSGEP protease. The transfection studies proved that N-CoR was the only protein of the two that OSGEP protease acted on selectively in AML-M5 cells thus proving its specificity in the subtype of cells. Findings of present study suggests that OSGEP protease-mediated N-CoR degradation is an important factor in the development of AML-M5. Current study highlights N-CoR degradation by OSGEP as a key molecular event in AML-M5 and proposes the N-CoR protease as a potential diagnostic and therapeutic biomarker for this leukemia subtype.
期刊介绍:
Biotechnology Letters is the world’s leading rapid-publication primary journal dedicated to biotechnology as a whole – that is to topics relating to actual or potential applications of biological reactions affected by microbial, plant or animal cells and biocatalysts derived from them.
All relevant aspects of molecular biology, genetics and cell biochemistry, of process and reactor design, of pre- and post-treatment steps, and of manufacturing or service operations are therefore included.
Contributions from industrial and academic laboratories are equally welcome. We also welcome contributions covering biotechnological aspects of regenerative medicine and biomaterials and also cancer biotechnology. Criteria for the acceptance of papers relate to our aim of publishing useful and informative results that will be of value to other workers in related fields.
The emphasis is very much on novelty and immediacy in order to justify rapid publication of authors’ results. It should be noted, however, that we do not normally publish papers (but this is not absolute) that deal with unidentified consortia of microorganisms (e.g. as in activated sludge) as these results may not be easily reproducible in other laboratories.
Papers describing the isolation and identification of microorganisms are not regarded as appropriate but such information can be appended as supporting information to a paper. Papers dealing with simple process development are usually considered to lack sufficient novelty or interest to warrant publication.