دورية أكاديمية
The human retroviral-like aspartic protease 1 (ASPRV1): from in vitro studies to clinical correlations.
| العنوان: | The human retroviral-like aspartic protease 1 (ASPRV1): from in vitro studies to clinical correlations. |
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| المؤلفون: | Mótyán JA; Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary. Electronic address: motyan.janos@med.unideb.hu., Tőzsér J; Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary. |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2024 Aug 02, pp. 107634. Date of Electronic Publication: 2024 Aug 02. |
| Publication Model: | Ahead of Print |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مستخلص: | The human retroviral-like aspartic protease 1 (ASPRV1) is a retroviral-like protein that was first identified in the skin due to its expression in the stratum granulosum layer of the epidermis. Accordingly, it is also referred to as skin-specific aspartic protease (SASPase). Similar to the retroviral polyproteins, the full-length ASPRV1 also undergoes self-proteolysis, the processing of the precursor is necessary for the auto-activation of the protease domain. ASPRV1's functions are well established at the level of the skin: it is part of the epidermal proteolytic network and has a significant contribution to skin moisturization via the limited proteolysis of filaggrin; its only natural protein substrate identified so far. Filaggrin and ASPRV1 are also specific for mammalians, these proteins provide unique features for the skins of these species, and the importance of filaggrin processing in hydration is proved by the fact that some ASPRV1 mutations are associated with skin diseases such as ichthyosis. ASPRV1 was also found to be expressed in macrophage-like neutrophil cells, indicating that its functions are not limited to the skin. In addition, differential expression of ASPRV1 was detected in many diseases, with yet unknown significance. The currently known enzymatic characteristics - that had been revealed mainly by in vitro studies - and correlations with pathogenic phenotypes imply potentially important functions in multiple cell types, which makes the protein a promising target of functional studies. In this review we describe the currently available knowledge and future perspective in regard to ASPRV1. Competing Interests: Conflicts of Interest: The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: ASPRV1; SASPase; aspartic protease; protease; proteolysis; skin; viral protein |
| تواريخ الأحداث: | Date Created: 20240804 Latest Revision: 20240804 |
| رمز التحديث: | 20240805 |
| DOI: | 10.1016/j.jbc.2024.107634 |
| PMID: | 39098535 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1083-351X |
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| DOI: | 10.1016/j.jbc.2024.107634 |