Small heat-shock proteins and their potential role in human disease.

Abstract

The elevated expression of stress proteins is considered to be a universal response to adverse conditions, representing a potential mechanism of cellular defense against disease and a potential target for novel therapeutics, including gene therapy and chaperone-modulating reagents. Recently, a single mutation in the small heat-shock protein human alphaB-crystallin was linked to desmin-related myopathy, which is characterized by abnormal intracellular aggregates of intermediate filaments in human muscle. New findings demonstrate that the high level of expression of stress proteins can contribute to an autoimmune response and can protect proteins that contribute to disease processes.

• Authors: J I Clark, P J Muchowski
• Journal: Current opinion in structural biology (Curr Opin Struct Biol) Vol. 10 Issue 1 Pg. 52-9 (Feb 2000) ISSN: 0959-440X [Print] England
• PMID: 10679464 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S., Review)

Chemical References

• Bacterial Proteins
• Crystallins
• Heat-Shock Proteins
• Nerve Tissue Proteins

Topics

• Amino Acid Sequence
• Animals
• Autoimmune Diseases (immunology)
• Bacterial Proteins (chemistry, physiology)
• Crystallins (chemistry, physiology)
• Drug Design
• Gene Expression Regulation
• Heat-Shock Proteins (chemistry, physiology)
• Humans
• Molecular Sequence Data
• Nerve Tissue Proteins (chemistry, physiology)
• Neurodegenerative Diseases (metabolism)
• Phosphorylation
• Protein Folding
• Protein Processing, Post-Translational
• Protein Structure, Tertiary
• Rats
• Sequence Alignment
• Sequence Homology, Amino Acid
• Stress, Physiological (genetics, metabolism)