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GRP78: A cell's response to stress.

Ibrahim M Ibrahim1, Doaa H Abdelmalek1, Abdo A Elfiky1

  • 1Biophysics Department, Faculty of Science, Cairo University, Giza, Egypt.

Life Sciences
|April 13, 2019
PubMed
Summary

Glucose-Regulated Protein 78 (GRP78) is a key chaperone protein. This review covers GRP78

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Area of Science:

  • Molecular Biology
  • Cellular Stress Response
  • Protein Folding

Background:

  • Glucose-Regulated Protein 78 (GRP78) is a critical chaperone heat shock protein.
  • GRP78 regulates the unfolded protein response (UPR) in the Endoplasmic Reticulum (ER) of normal cells.
  • It facilitates protein refolding or degradation via cellular mechanisms.

Purpose of the Study:

  • To review the structure and function of GRP78.
  • To elucidate the mechanisms GRP78 employs under normal and stress conditions.
  • To explore GRP78 targeting strategies for therapeutic applications.

Main Methods:

  • Literature review of GRP78 research.
  • Analysis of GRP78's role in cellular stress.
  • Investigation of GRP78's involvement in pathogenesis and cancer.

Main Results:

  • GRP78 overexpression on cell membranes under stress aids pathogen entry.
  • Elevated GRP78 levels in cancer cells correlate with increased disease aggressiveness.
  • GRP78's dual role in normal cellular function and disease states.

Conclusions:

  • GRP78's structure, function, and regulatory mechanisms are summarized.
  • Targeting GRP78 offers potential for inhibiting pathogen virulence and cancer progression.
Keywords:
GRP78HSP70Heat shock proteinsMembrane receptorsStressUnfolded protein response

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