دورية أكاديمية
The ADAMTS/Fibrillin Connection: Insights into the Biological Functions of ADAMTS10 and ADAMTS17 and Their Respective Sister Proteases.
العنوان: | The ADAMTS/Fibrillin Connection: Insights into the Biological Functions of ADAMTS10 and ADAMTS17 and Their Respective Sister Proteases. |
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المؤلفون: | Karoulias SZ; Orthopaedic Research Laboratories, Leni & Peter W. May Department of Orthopaedics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA., Taye N; Orthopaedic Research Laboratories, Leni & Peter W. May Department of Orthopaedics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA., Stanley S; Orthopaedic Research Laboratories, Leni & Peter W. May Department of Orthopaedics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA., Hubmacher D; Orthopaedic Research Laboratories, Leni & Peter W. May Department of Orthopaedics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. |
المصدر: | Biomolecules [Biomolecules] 2020 Apr 12; Vol. 10 (4). Date of Electronic Publication: 2020 Apr 12. |
نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review |
اللغة: | English |
بيانات الدورية: | Publisher: MDPI Country of Publication: Switzerland NLM ID: 101596414 Publication Model: Electronic Cited Medium: Internet ISSN: 2218-273X (Electronic) Linking ISSN: 2218273X NLM ISO Abbreviation: Biomolecules Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Basel, Switzerland : MDPI, 2011- |
مواضيع طبية MeSH: | ADAMTS Proteins/*metabolism , Fibrillins/*metabolism, ADAMTS Proteins/chemistry ; ADAMTS Proteins/genetics ; Animals ; Disease/genetics ; Humans ; Mutation/genetics ; Protein Processing, Post-Translational ; Substrate Specificity |
مستخلص: | Secreted a disintegrin-like and metalloprotease with thrombospondin type 1 motif (ADAMTS) proteases play crucial roles in tissue development and homeostasis. The biological and pathological functions of ADAMTS proteases are determined broadly by their respective substrates and their interactions with proteins in the pericellular and extracellular matrix. For some ADAMTS proteases, substrates have been identified and substrate cleavage has been implicated in tissue development and in disease. For other ADAMTS proteases, substrates were discovered in vitro, but the role of these proteases and the consequences of substrate cleavage in vivo remains to be established. Mutations in ADAMTS10 and ADAMTS17 cause Weill-Marchesani syndrome (WMS), a congenital syndromic disorder that affects the musculoskeletal system (short stature, pseudomuscular build, tight skin), the eyes (lens dislocation), and the heart (heart valve abnormalities). WMS can also be caused by mutations in fibrillin-1 ( FBN1 ), which suggests that ADAMTS10 and ADAMTS17 cooperate with fibrillin-1 in a common biological pathway during tissue development and homeostasis. Here, we compare and contrast the biochemical properties of ADAMTS10 and ADAMTS17 and we summarize recent findings indicating potential biological functions in connection with fibrillin microfibrils. We also compare ADAMTS10 and ADAMTS17 with their respective sister proteases, ADAMTS6 and ADAMTS19; both were recently linked to human disorders distinct from WMS. Finally, we propose a model for the interactions and roles of these four ADAMTS proteases in the extracellular matrix. |
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معلومات مُعتمدة: | AR070748 United States NH NIH HHS |
فهرسة مساهمة: | Keywords: ADAMTS proteases; Weill-Marchesani syndrome; extracellular matrix; fibrillin; lens dislocation; microfibrils; short stature |
المشرفين على المادة: | 0 (Fibrillins) EC 3.4.24.- (ADAMTS Proteins) |
تواريخ الأحداث: | Date Created: 20200416 Date Completed: 20210405 Latest Revision: 20210405 |
رمز التحديث: | 20240628 |
مُعرف محوري في PubMed: | PMC7226509 |
DOI: | 10.3390/biom10040596 |
PMID: | 32290605 |
قاعدة البيانات: | MEDLINE |
تدمد: | 2218-273X |
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DOI: | 10.3390/biom10040596 |