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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The Unfolded Protein Response: How Protein Folding Became a Restrictive Aspect for Innate Immunity and B Lymphocytes

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Author(s):
Costa, C. Z. F. [1] ; da Rosa, S. E. A. [1] ; de Camargo, M. M. [1]
Total Authors: 3
Affiliation:
[1] Univ Sao Paulo, Inst Biomed Sci, Dept Immunol, BR-05508900 Sao Paulo - Brazil
Total Affiliations: 1
Document type: Review article
Source: Scandinavian Journal of Immunology; v. 73, n. 5, p. 436-448, MAY 2011.
Web of Science Citations: 8
Abstract

Chaperone production is an essential step for proper folding of certain proteins. Accumulation of misfolded/unfolded proteins within the endoplasmic reticulum (ER) lumen triggers a signalling pathway named unfolded protein response (UPR). Upon activation, the UPR pathway augments transcription of ER chaperones increasing protein folding, decreases protein translation to ameliorate the ER overload, increases protein degradation, and activates the apoptotic programme if all previous measures fail. In this review, we will cover the chaperones involved in folding of proteins related to the immune response, followed by an overview of the UPR pathway. Lastly, we will discuss data from this last decade that demonstrate how the improper activation of the UPR pathway has been uncovered as a mechanism responsible for failure to mount a proper immune response, both innate and adaptive. (AU)

FAPESP's process: 09/06529-8 - Regulation of homeostasis of ER in B lymphocytes in common variable immunodeficiency
Grantee:Susana Elaine Alves da Rosa
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 09/51326-8 - Regulation of Er homeostasis in b lymphocytes during common variable immunodeficiency
Grantee:Maristela Martins de Camargo
Support Opportunities: Regular Research Grants