N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis
Extracellular matrix protein 1 (ECM1) is expressed in a wide variety of tissues and plays important roles in extracellular matrix formation. Additionally, ECM1 gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is n...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2014-01-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S221154631400093X |
| _version_ | 1828428576588824576 |
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| author | Shiho Uematsu Yuki Goto Takehiro Suzuki Yukiko Sasazawa Naoshi Dohmae Siro Simizu |
| author_facet | Shiho Uematsu Yuki Goto Takehiro Suzuki Yukiko Sasazawa Naoshi Dohmae Siro Simizu |
| author_sort | Shiho Uematsu |
| collection | DOAJ |
| description | Extracellular matrix protein 1 (ECM1) is expressed in a wide variety of tissues and plays important roles in extracellular matrix formation. Additionally, ECM1 gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is not established. Here, we showed that ECM1 gene mutation observed in LP patients significantly suppresses its secretion. As ECM1 has three putative N-glycosylation sites and most of mutated ECM1 observed in LP patients are defective in these N-glycosylation sites, we investigated the correlation between LP and N-glycosylation of ECM1. We identified that the Asn354 and Asn444 residues in ECM1 were N-glycosylated by mass spectrometry analysis. In addition, an N-linked glycan at Asn354 negatively regulated secretion of ECM1, contrary to LP patient-derived mutants. These results indicate that the defect of N-glycosylation in ECM1 is not involved in the aberration of secretion of LP-derived mutated ECM1. |
| first_indexed | 2024-12-10T17:19:45Z |
| format | Article |
| id | doaj.art-b60a02d96acd4eefb88a50423959af27 |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-10T17:19:45Z |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-b60a02d96acd4eefb88a50423959af272022-12-22T01:40:00ZengWileyFEBS Open Bio2211-54632014-01-014C87988510.1016/j.fob.2014.10.004N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosisShiho Uematsu0Yuki Goto1Takehiro Suzuki2Yukiko Sasazawa3Naoshi Dohmae4Siro Simizu5Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, JapanDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, JapanGlobal Research Cluster, RIKEN, Wako 351-0198, JapanDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, JapanGlobal Research Cluster, RIKEN, Wako 351-0198, JapanDepartment of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama 223-8522, JapanExtracellular matrix protein 1 (ECM1) is expressed in a wide variety of tissues and plays important roles in extracellular matrix formation. Additionally, ECM1 gene mutations cause lipoid proteinosis (LP), a rare skin condition of genetic origin. However, an effective therapeutic approach of LP is not established. Here, we showed that ECM1 gene mutation observed in LP patients significantly suppresses its secretion. As ECM1 has three putative N-glycosylation sites and most of mutated ECM1 observed in LP patients are defective in these N-glycosylation sites, we investigated the correlation between LP and N-glycosylation of ECM1. We identified that the Asn354 and Asn444 residues in ECM1 were N-glycosylated by mass spectrometry analysis. In addition, an N-linked glycan at Asn354 negatively regulated secretion of ECM1, contrary to LP patient-derived mutants. These results indicate that the defect of N-glycosylation in ECM1 is not involved in the aberration of secretion of LP-derived mutated ECM1.http://www.sciencedirect.com/science/article/pii/S221154631400093XExtracellular matrix protein 1Lipoid proteinosisN-GlycosylationSecretion |
| spellingShingle | Shiho Uematsu Yuki Goto Takehiro Suzuki Yukiko Sasazawa Naoshi Dohmae Siro Simizu N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis FEBS Open Bio Extracellular matrix protein 1 Lipoid proteinosis N-Glycosylation Secretion |
| title | N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis |
| title_full | N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis |
| title_fullStr | N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis |
| title_full_unstemmed | N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis |
| title_short | N-Glycosylation of extracellular matrix protein 1 (ECM1) regulates its secretion, which is unrelated to lipoid proteinosis |
| title_sort | n glycosylation of extracellular matrix protein 1 ecm1 regulates its secretion which is unrelated to lipoid proteinosis |
| topic | Extracellular matrix protein 1 Lipoid proteinosis N-Glycosylation Secretion |
| url | http://www.sciencedirect.com/science/article/pii/S221154631400093X |
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