دورية أكاديمية
A High-Throughput Assay for Collagen Secretion Suggests an Unanticipated Role for Hsp90 in Collagen Production.
| العنوان: | A High-Throughput Assay for Collagen Secretion Suggests an Unanticipated Role for Hsp90 in Collagen Production. |
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| المؤلفون: | Wong MY; Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., Doan ND; Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., DiChiara AS; Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., Papa LJ 3rd; Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., Cheah JH; High-Throughput Sciences Facility, Koch Institute for Integrative Cancer Research , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., Soule CK; High-Throughput Sciences Facility, Koch Institute for Integrative Cancer Research , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States., Watson N; W. M. Keck Microscopy Facility , The Whitehead Institute , Cambridge , Massachusetts 02142 , United States., Hulleman JD; Departments of Ophthalmology and Pharmacology , University of Texas Southwestern Medical Center , Dallas , Texas 75390 , United States., Shoulders MD; Department of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States. |
| المصدر: | Biochemistry [Biochemistry] 2018 May 15; Vol. 57 (19), pp. 2814-2827. Date of Electronic Publication: 2018 May 03. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | High-Throughput Screening Assays*, Collagen Type I/*chemistry , HSP90 Heat-Shock Proteins/*chemistry , Membrane Glycoproteins/*chemistry, Benzoquinones/pharmacology ; Cell Line ; Collagen Type I/biosynthesis ; Collagen Type I/metabolism ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; Humans ; Lactams, Macrocyclic/pharmacology ; Membrane Glycoproteins/antagonists & inhibitors ; Protein Isoforms/chemistry |
| مستخلص: | Collagen overproduction is a feature of fibrosis and cancer, while insufficient deposition of functional collagen molecules and/or the secretion of malformed collagen is common in genetic disorders like osteogenesis imperfecta. Collagen secretion is an appealing therapeutic target in these and other diseases, as secretion directly connects intracellular biosynthesis to collagen deposition and biological function in the extracellular matrix. However, small molecule and biological methods to tune collagen secretion are severely lacking. Their discovery could prove useful not only in the treatment of disease, but also in providing tools for better elucidating mechanisms of collagen biosynthesis. We developed a cell-based, high-throughput luminescent assay of collagen type I secretion and used it to screen for small molecules that selectively enhance or inhibit that process. Among several validated hits, the Hsp90 inhibitor 17-allylaminogeldanamycin (17-AAG) robustly decreases the secretion of collagen-I by our model cell line and by human primary cells. In these systems, 17-AAG and other pan-isoform Hsp90 inhibitors reduce collagen-I secretion post-translationally and are not global inhibitors of protein secretion. Surprisingly, the consequences of Hsp90 inhibitors cannot be attributed to inhibition of the endoplasmic reticulum's Hsp90 isoform, Grp94. Instead, collagen-I secretion likely depends on the activity of cytosolic Hsp90 chaperones, even though such chaperones cannot directly engage nascent collagen molecules. Our results highlight the value of a cell-based high-throughput screen for selective modulators of collagen secretion and suggest an unanticipated role for cytosolic Hsp90 in collagen secretion. |
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| معلومات مُعتمدة: | R01 AR071443 United States AR NIAMS NIH HHS; P30 CA014051 United States CA NCI NIH HHS; F31 AR067615 United States AR NIAMS NIH HHS; P30 EY020799 United States EY NEI NIH HHS; R03 AR067503 United States AR NIAMS NIH HHS |
| المشرفين على المادة: | 0 (Benzoquinones) 0 (Collagen Type I) 0 (HSP90 Heat-Shock Proteins) 0 (Lactams, Macrocyclic) 0 (Membrane Glycoproteins) 0 (Protein Isoforms) 0 (endoplasmin) 4GY0AVT3L4 (tanespimycin) |
| تواريخ الأحداث: | Date Created: 20180421 Date Completed: 20180913 Latest Revision: 20240610 |
| رمز التحديث: | 20240610 |
| مُعرف محوري في PubMed: | PMC6231715 |
| DOI: | 10.1021/acs.biochem.8b00378 |
| PMID: | 29676157 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-4995 |
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| DOI: | 10.1021/acs.biochem.8b00378 |