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Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans
06:01

Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans

Published on: July 3, 2020

Investigating receptors for extracellular heat shock proteins

Ayesha Murshid1, Jimmy Theriault, Jianlin Gong

  • 1Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 8, 2011
PubMed

Insights

Extracellular heat shock proteins (HSP) bind to cell surface receptors, including c-type lectin receptors (CLR) and scavenger receptors (SR). This study identifies specific interactions and discusses methods for further investigation.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Extracellular heat shock proteins (HSP) are crucial for cell signaling and immune responses.
  • Cell surface receptors mediate many of these HSP effects across various cell types.

Purpose of the Study:

  • To identify and characterize the cell surface receptors that bind extracellular heat shock proteins (HSP).
  • To explore the nature of the interactions between HSP70 and its identified receptors.

Main Methods:

  • Utilized Chinese Hamster Ovary (CHO-K1) cells, which lack endogenous HSP binding capacity, for receptor cloning.
  • Investigated HSP70 binding to candidate receptors, including c-type lectin receptors (CLR) and scavenger receptors (SR).

Main Results:

  • Discovered that HSP70 binds to at least two distinct receptor classes: CLRs and SRs.
  • Confirmed HSP70 binding to LOX-1 (a CLR and SR), utilizing its c-type lectin binding domain (CTLD).
  • Identified binding to SR family members SREC-I and FEEL-1/CLEVER-1/STABILIN-1, which possess EGF-like repeats.

Conclusions:

  • HSP70 interacts with multiple receptor types, including CLRs and SRs, with specific domains mediating these interactions.
  • The study provides a foundation for understanding HSP-receptor dynamics and their functional implications.
  • Outlines methodologies for receptor identification, individual receptor analysis, and in vivo functional studies of HSP receptors.

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