Correlation between leucine rich domain and the stability of LRWD1 protein in human NT2/D1 cells |
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| Institution: | 1. Department of Obstetrics and Gynecology, Chi-Mei Medical Center, Tainan, Taiwan;2. Department of Medicine, Taipei Medical University, Taipei, Taiwan;3. Department of Sport Management, Chia Nan University of Pharmacy and Science, Tainan, Taiwan;4. Department of Biological Sciences and Technology, National University of Tainan, Taiwan;5. Department of Biotechnology, Chia Nan University of Pharmacy and Science, Tainan, Taiwan;6. Division of Nephrology, Department of Internal Medicine, Kaohsiung Chang Gung Memorial Hospital and Chang Gung University College of Medicine, Kaohsiung, Taiwan;7. Department of Obstetrics & Gynecology, National Cheng Kung University Hospital, Tainan, Taiwan;8. Department of Biotechnology, College of Life Science, Kaohsiung Medical University, Kaohsiung, Taiwan;9. Department of Biomedical Science and Environmental Biology, College of Life Science, Kaohsiung Medical University, Kaohsiung, Taiwan;10. Department of Biological Science, National Sun Yat-sen University, Kaohsiung, Taiwan;1. Department of Anatomy, College of Medicine, Chosun University, Gwangju, Republic of Korea;2. Division of Natural Medical Sciences, Chosun University, Gwangju, Republic of Korea;3. Department of Pharmacology, College of Medicine, Chosun University, Gwangju, Republic of Korea;4. Department of Marine Life Science, School of Natural Sciences, Chosun University, Gwangju, Republic of Korea;5. Department of Anatomy, College of Medicine, Seonam University, Namwon, Jeollabuk-Do, Republic of Korea;6. Medical Course, School of Medicine, Jeju National University, Jeju-Do, Republic of Korea;7. Department of Anatomy, School of Medicine, Jeju National University, Jeju-Do, Republic of Korea;1. Department of Cardiology, Medical University of Bialystok, Bialystok, Poland;2. Department of Invasive Cardiology, Medical University of Bialystok, Bialystok, Poland;1. Department of Gastroenterology and Internal Medicine, Medical University of Bialystok, Bialystok, Poland;2. Department of Medical Pathomorphology, Medical University of Bialystok, Bialystok, Poland;3. Department of Gastroenterology and Internal Medicine, Regional Hospital, Bialystok, Poland;1. Department of Clinical Laboratory Diagnostics, Medical University of Bialystok, Bialystok, Poland;2. Department of Family Medicine and Community Nursing, Medical University of Bialystok, Bialystok, Poland;3. Department of Hematology, Clinical Hospital of the Medical University of Bialystok, Bialystok, Poland |
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| Abstract: | PurposeLRWD1 is a protein that contains LRR and WDs domains and is important in regulating spermatogenesis. However, the roles of LRR or WDs domains in the expression of LRWD1 remain unclear.Materials and methodsThe NT2/D1 cells separately transfected with full length of LRWD1 gene (LRWDWT) or genes with deleted sequences in the LRR domain (LRWD1ΔLRR), WD1 domain (LRWD1ΔWD1), WD2 domain (LRWD1ΔWD2), WD3 domain (LRWD1ΔWD3) and entire three WD domains (LRWD1Δ3×WD) were applied to investigate the expression levels of LRWD1 protein by either Western blot or flow cytometry. The associated proteins in these mutated LRWD1 proteins were identified by mass spectrometry.ResultsDeletion of the LRR domain significantly decreased the expression of LRWD1 protein. With the treatment of MG132, the LRR domain may functions in preventing LRWD1 protein from proteasome-mediated degradation. In the co-immunoprecipitation analysis, protein receptor of tumor necrosis factor 2 (TNFR2) was specifically observed to be associated with LRR-deficient LRWD1 protein.ConclusionsThe LRR domain is significantly correlated to the stability of LRWD1 protein. Determining if the stability is modulated by TNFR2 is worthy of further study. |
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| Keywords: | LRWD1 Leucine rich domain Spermatogenesis Co-immunoprecipitation Proteomics |
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