LRP1 is required for novobiocin-mediated fibronectin turnover:
- Boel, Natasha M-E, Hunter, Morgan C, Edkins, Adrienne L
- Authors: Boel, Natasha M-E , Hunter, Morgan C , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164896 , vital:41182 , DOI: 10.1038/s41598-018-29531-2
- Description: Fibronectin (FN) plays a major role in the stability and organization of the extracellular matrix (ECM). We have previously demonstrated that FN interacts directly with Hsp90, as well as showing that the Hsp90 inhibitor novobiocin results in FN turnover via a receptor mediated process. However, the receptor involved has not been previously identified. LRP1 is a ubiquitous receptor responsible for the internalisation of numerous ligands that binds both Hsp90 and FN, and therefore we investigated whether LRP1 was involved in novobiocin-mediated FN turnover.
- Full Text:
- Date Issued: 2018
- Authors: Boel, Natasha M-E , Hunter, Morgan C , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164896 , vital:41182 , DOI: 10.1038/s41598-018-29531-2
- Description: Fibronectin (FN) plays a major role in the stability and organization of the extracellular matrix (ECM). We have previously demonstrated that FN interacts directly with Hsp90, as well as showing that the Hsp90 inhibitor novobiocin results in FN turnover via a receptor mediated process. However, the receptor involved has not been previously identified. LRP1 is a ubiquitous receptor responsible for the internalisation of numerous ligands that binds both Hsp90 and FN, and therefore we investigated whether LRP1 was involved in novobiocin-mediated FN turnover.
- Full Text:
- Date Issued: 2018
Regulation of the extracellular matrix by heat shock proteins and molecular chaperones:
- Boel, Natasha M-E, Edkins, Adrienne L
- Authors: Boel, Natasha M-E , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164368 , vital:41112 , ISBN 978-3-319-69040-7 , DOI: 10.1007/978-3-319-69042-1_6
- Description: The extracellular matrix (ECM) serves as a scaffold for cells within tissues and is composed of an intricate network of glycoproteins, growth factors and matricellular proteins which cooperatively function in cell processes such as migration, adhesion and wound healing. ECM morphology is constantly undergoing remodelling (synthesis, assembly and degradation) during normal cell processes and when deregulated may contribute to disease. Heat shock proteins (Hsps) are involved in regulating processes that determine the assembly and degradation of the ECM at multiple levels, in both normal and diseased states. These roles include mediating the activation of ECM-degrading enzymes, maintaining matrix stability and clearing aggregated/misfolded proteins. Hsp may serve as chaperones and receptors or have cytokine-like functions. In this chapter, we review how Hsp90, Hsp70, Hsp40 and a number of ER resident chaperones contribute to ECM regulation. The role of the non-Hsp chaperones, SPARC and clusterin in the ECM is also discussed.
- Full Text:
- Date Issued: 2018
- Authors: Boel, Natasha M-E , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164368 , vital:41112 , ISBN 978-3-319-69040-7 , DOI: 10.1007/978-3-319-69042-1_6
- Description: The extracellular matrix (ECM) serves as a scaffold for cells within tissues and is composed of an intricate network of glycoproteins, growth factors and matricellular proteins which cooperatively function in cell processes such as migration, adhesion and wound healing. ECM morphology is constantly undergoing remodelling (synthesis, assembly and degradation) during normal cell processes and when deregulated may contribute to disease. Heat shock proteins (Hsps) are involved in regulating processes that determine the assembly and degradation of the ECM at multiple levels, in both normal and diseased states. These roles include mediating the activation of ECM-degrading enzymes, maintaining matrix stability and clearing aggregated/misfolded proteins. Hsp may serve as chaperones and receptors or have cytokine-like functions. In this chapter, we review how Hsp90, Hsp70, Hsp40 and a number of ER resident chaperones contribute to ECM regulation. The role of the non-Hsp chaperones, SPARC and clusterin in the ECM is also discussed.
- Full Text:
- Date Issued: 2018
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