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Molecular chaperones in the kidney

Steven C Borkan1, Steven R Gullans

  • 1Evans Biomedical Research Center, Boston Medical Center, Renal Section, 650 Albany Street, Boston, Massachusetts 02118-2518, USA. sborkan@bu.edu

Annual Review of Physiology
|February 5, 2002
PubMed

Insights

Kidneys use molecular chaperones to manage stress from hypoxia and fluid shifts. These proteins stabilize cellular functions, aid protein repair, and protect kidney cells from damage, enhancing survival.

Area of Science:

  • Nephrology
  • Molecular Biology
  • Cellular Stress Response

Background:

  • The kidney operates in a harsh environment characterized by hypoxia, osmotic fluxes, and extensive fluid/solute reabsorption.
  • Cellular adaptation to these conditions necessitates specialized molecular machinery to maintain protein homeostasis.

Purpose of the Study:

  • To elucidate the multifaceted roles of molecular chaperones in renal cell adaptation and survival.
  • To explore both intracellular and cell surface chaperone functions in the kidney.

Main Methods:

  • Review and synthesis of existing literature on molecular chaperones in renal physiology.
  • Analysis of the known functions of various chaperone families in cellular stress response.

Main Results:

  • Intracellular molecular chaperones are crucial for protein folding, targeting, and preventing aggregation under normal and stressed conditions.
  • Inducible chaperones provide repair and degradation pathways for damaged proteins and inhibit apoptosis.
  • Cell surface chaperones modulate immune responses and exhibit cytokine-like activities.

Conclusions:

  • Molecular chaperones represent a critical defense system for renal cells, enabling adaptation to physiological and pathological stresses.
  • The diverse functions of chaperones, both intracellular and extracellular, contribute significantly to renal cell survival and function.

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