Cited 18 times in
Role of scarf and its binding target proteins in epidermal calcium homeostasis
DC Field | Value | Language |
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dc.contributor.author | 이승헌 | - |
dc.date.accessioned | 2014-12-21T16:43:07Z | - |
dc.date.available | 2014-12-21T16:43:07Z | - |
dc.date.issued | 2007 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/96220 | - |
dc.description.abstract | The novel Ca2+-binding protein, Scarf (skin calmodulin-related factor) belongs to the calmodulin-like protein family and is expressed in the differentiated layers of the epidermis. To determine the roles of Scarf during stratification, we set out to identify the binding target proteins by affinity chromatography and subsequent analysis by mass spectrometry. Several binding factors, including 14-3-3s, annexins, calreticulin, ERp72 (endoplasmic reticulum protein 72), and nucleolin, were identified, and their interactions with Scarf were corroborated by co-immunoprecipitation and co-localization analyses. To further understand the functions of Scarf in epidermis in vivo, we altered the epidermal Ca2+ gradient by acute barrier disruption. The change in the expression levels of Scarf and its binding target proteins were determined by immunohistochemistry and Western blot analysis. The expression of Scarf, annexins, calreticulin, and ERp72 were up-regulated by Ca2+ gradient disruption, whereas the expression of 14-3-3s and nucleolin was reduced. Because annexins, calreticulin, and ERp72 have been implicated in Ca2+-induced cellular trafficking, including the secretion of lamellar bodies and Ca2+ homeostasis, we propose that the interaction of Scarf with these proteins might be crucial in the process of barrier restoration. On the other hand, down-regulation of 14-3-3s and nucleolin is potentially involved in the process of keratinocyte differentiation and growth inhibition. The calcium-dependent localization and up-regulation of Scarf and its binding target proteins were studied in mouse keratinocytes treated with ionomycin and during the wound-healing process. We found increased expression and nuclear presence of Scarf in the epidermis of the wound edge 4 and 7 days post-wounding, entailing the role of Scarf in barrier restoration. Our results suggest that Scarf plays a critical role as a Ca2+ sensor, potentially regulating the function of its binding target proteins in a Ca2+-dependent manner in the process of restoration of epidermal Ca2+ gradient as well as during epidermal barrier formation. | - |
dc.description.statementOfResponsibility | open | - |
dc.format.extent | 18645~18653 | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.subject.MESH | Animals | - |
dc.subject.MESH | Calcium/metabolism* | - |
dc.subject.MESH | Calcium-Binding Proteins/metabolism | - |
dc.subject.MESH | Calcium-Binding Proteins/physiology* | - |
dc.subject.MESH | Calpain | - |
dc.subject.MESH | Cell Differentiation | - |
dc.subject.MESH | Chromatography, Affinity | - |
dc.subject.MESH | Epidermis/metabolism | - |
dc.subject.MESH | Gene Expression Regulation* | - |
dc.subject.MESH | Homeostasis | - |
dc.subject.MESH | Mass Spectrometry | - |
dc.subject.MESH | Membrane Glycoproteins/metabolism | - |
dc.subject.MESH | Mice | - |
dc.subject.MESH | Microscopy, Confocal | - |
dc.subject.MESH | Protein Binding | - |
dc.subject.MESH | Up-Regulation | - |
dc.subject.MESH | Wound Healing | - |
dc.title | Role of scarf and its binding target proteins in epidermal calcium homeostasis | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Dermatology (피부과학) | - |
dc.contributor.googleauthor | Joonsung Hwang | - |
dc.contributor.googleauthor | Alexandr Kalinin | - |
dc.contributor.googleauthor | Maria I. Morasso | - |
dc.contributor.googleauthor | Seung Hun Lee | - |
dc.contributor.googleauthor | Marjana Tomic-Canic | - |
dc.contributor.googleauthor | Olivera Stojadinovic | - |
dc.contributor.googleauthor | Min Jung Kim | - |
dc.contributor.googleauthor | D. Eric Anderson | - |
dc.contributor.googleauthor | Meeyul Hwang | - |
dc.identifier.doi | 10.1074/jbc.M702035200 | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A02931 | - |
dc.relation.journalcode | J01258 | - |
dc.identifier.eissn | 1083-351X | - |
dc.identifier.pmid | 17470426 | - |
dc.contributor.alternativeName | Lee, Seung Hun | - |
dc.contributor.affiliatedAuthor | Lee, Seung Hun | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 282 | - |
dc.citation.number | 25 | - |
dc.citation.startPage | 18645 | - |
dc.citation.endPage | 18653 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.282(25) : 18645-18653, 2007 | - |
dc.identifier.rimsid | 34986 | - |
dc.type.rims | ART | - |
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