UGGT1 retains proinsulin in the endoplasmic reticulum in an arginine dependent manner
We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucos...
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| Published in | Biochemical and biophysical research communications Vol. 527; no. 3; pp. 668 - 675 |
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| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier Inc
30.06.2020
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| Abstract | We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L- and d-arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion.
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•UGGT1 binds to proinsulin in the absence of arginine.•Arginine competes with proinsulin and binds to UGGT1 in the ER.•Released proinsulin moves to Golgi apparatus and secretory vesicles to secrete. |
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| AbstractList | We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L- and d-arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion. We sought to clarify a pathway by which L - and D -arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L - and D -arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion. We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L- and d-arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion. [Display omitted] •UGGT1 binds to proinsulin in the absence of arginine.•Arginine competes with proinsulin and binds to UGGT1 in the ER.•Released proinsulin moves to Golgi apparatus and secretory vesicles to secrete. We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L- and d-arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion.We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1) Using affinity magnetic nanobeads technology, we identified that proinsulin is retained in the endoplasmic reticulum (ER) through UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) when arginine availability is limited. (2) L- and d-arginine release proinsulin from UGGT1 through competition with proinsulin and promote exit of proinsulin from the ER to Golgi apparatus. The ability of arginine to release proinsulin from UGGT1 closely correlates with arginine-induced insulin secretion in several models of β cells indicating that UGGT1-proinsulin interaction regulates arginine-induced insulin secretion. |
| Author | Imai, Yoichi Handa, Hiroshi Masaike, Yuka Imai, Takeshi Hiramoto, Masaki Cho, Jaeyong Sakamoto, Satoshi Imai, Yumi |
| AuthorAffiliation | 6 Department of Internal Medicine, Fraternal Order of Eagles Diabetes Research Center, University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA 3 Department of Nanoparticle Translational Research, Tokyo Medical University, Shinjyuku, Tokyo 160-8402, Japan 4 School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Kanagawa 223-8503, Japan 1 Department Aging Intervention, National Center for Geriatrics and Gerontology, Obu, Aichi 474-8511, Japan 2 Department of Biochemistry, Tokyo Medical University, Shinjyuku, Tokyo 160-8402, Japan 5 Department of Hematology/Oncology, Research Hospital, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan |
| AuthorAffiliation_xml | – name: 5 Department of Hematology/Oncology, Research Hospital, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan – name: 2 Department of Biochemistry, Tokyo Medical University, Shinjyuku, Tokyo 160-8402, Japan – name: 6 Department of Internal Medicine, Fraternal Order of Eagles Diabetes Research Center, University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA – name: 3 Department of Nanoparticle Translational Research, Tokyo Medical University, Shinjyuku, Tokyo 160-8402, Japan – name: 1 Department Aging Intervention, National Center for Geriatrics and Gerontology, Obu, Aichi 474-8511, Japan – name: 4 School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Kanagawa 223-8503, Japan |
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| Snippet | We sought to clarify a pathway by which L- and dD-arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings. (1)... We sought to clarify a pathway by which L - and D -arginine simulate insulin secretion in mice and cell lines and obtained the following novel two findings.... |
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| SubjectTerms | Animals Arginine Arginine - metabolism Cells, Cultured Endoplasmic endoplasmic reticulum Endoplasmic Reticulum - metabolism Glucosyltransferases - metabolism Golgi apparatus HEK293 Cells Humans Insulin Insulin Secretion Insulin-Secreting Cells - metabolism magnetism Male Mice Mice, Transgenic Models, Molecular proinsulin Proinsulin - metabolism Reticulum UGGT1 |
| Title | UGGT1 retains proinsulin in the endoplasmic reticulum in an arginine dependent manner |
| URI | https://dx.doi.org/10.1016/j.bbrc.2020.04.158 https://www.ncbi.nlm.nih.gov/pubmed/32423812 https://www.proquest.com/docview/2404639041 https://www.proquest.com/docview/2524327704 https://pubmed.ncbi.nlm.nih.gov/PMC7863631 |
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