Calcium–Collagen Coupling is Vital for Biomineralization Schedule. Issue 15 (27th May 2021)
- Record Type:
- Journal Article
- Title:
- Calcium–Collagen Coupling is Vital for Biomineralization Schedule. Issue 15 (27th May 2021)
- Main Title:
- Calcium–Collagen Coupling is Vital for Biomineralization Schedule
- Authors:
- Zhang, Jinglun
Ji, Yaoting
Jiang, Shuting
Shi, Miusi
Cai, Wenjin
Miron, Richard J.
Zhang, Yufeng - Abstract:
- Abstract: Biomineralization is a chemical reaction that occurs in organisms in which collagen initiates and guides the growth and crystallization of matched apatite minerals. However, there is little known about the demand pattern for calcium salts and collagen needed by biomineralization. In this study, natural bone biomineralization is analyzed, and a novel interplay between calcium concentration and collagen production is observed. Any quantitative change in one of the entities causes a corresponding change in the other. Translocation‐associated membrane protein 2 (TRAM2) is identified as an intermediate factor whose silencing disrupts this relationship and causes poor mineralization. TRAM2 directly interacts with the sarcoplasmic/endoplasmic reticulum calcium ATPase 2b (SERCA2b) and modulates SERCA2b activity to couple calcium enrichment with collagen biosynthesis. Collectively, these findings indicate that osteoblasts can independently and directly regulate the process of biomineralization via this coupling. This knowledge has significant implications for the developmentally inspired design of biomaterials for bone regenerative applications. Abstract : This study clarifies the biological demand pattern of osteoblasts for ER Ca 2+ concentration and collagen biosynthesis and demonstrates that the translocation‐associated membrane protein 2‐sarcoplasmic/endoplasmic reticulum calcium ATPase 2b (TRAM2‐SERCA2b) regulatory complex can mediate the two‐way relationship duringAbstract: Biomineralization is a chemical reaction that occurs in organisms in which collagen initiates and guides the growth and crystallization of matched apatite minerals. However, there is little known about the demand pattern for calcium salts and collagen needed by biomineralization. In this study, natural bone biomineralization is analyzed, and a novel interplay between calcium concentration and collagen production is observed. Any quantitative change in one of the entities causes a corresponding change in the other. Translocation‐associated membrane protein 2 (TRAM2) is identified as an intermediate factor whose silencing disrupts this relationship and causes poor mineralization. TRAM2 directly interacts with the sarcoplasmic/endoplasmic reticulum calcium ATPase 2b (SERCA2b) and modulates SERCA2b activity to couple calcium enrichment with collagen biosynthesis. Collectively, these findings indicate that osteoblasts can independently and directly regulate the process of biomineralization via this coupling. This knowledge has significant implications for the developmentally inspired design of biomaterials for bone regenerative applications. Abstract : This study clarifies the biological demand pattern of osteoblasts for ER Ca 2+ concentration and collagen biosynthesis and demonstrates that the translocation‐associated membrane protein 2‐sarcoplasmic/endoplasmic reticulum calcium ATPase 2b (TRAM2‐SERCA2b) regulatory complex can mediate the two‐way relationship during biomineralization. The synchronicity of ER morphology, TRAM2 expression patterns, and SERCA2b activity trends reveal the central position of ER during the entire process of biomineralization. … (more)
- Is Part Of:
- Advanced science. Volume 8:Issue 15(2021)
- Journal:
- Advanced science
- Issue:
- Volume 8:Issue 15(2021)
- Issue Display:
- Volume 8, Issue 15 (2021)
- Year:
- 2021
- Volume:
- 8
- Issue:
- 15
- Issue Sort Value:
- 2021-0008-0015-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2021-05-27
- Subjects:
- biomineralization -- bones -- bone biomaterials -- calcium–collagen coupling -- collagen
Science -- Periodicals
505 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2198-3844 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/advs.202100363 ↗
- Languages:
- English
- ISSNs:
- 2198-3844
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 26898.xml