Abstract
Protein aggregates are oligomeric complexes of misfolded proteins, and serve as the seeds of inclusion bodies termed aggresomes in the cells. Heat shock proteins (Hsps) prevent misfolding and aggregate formation. Here, we found that only avian Hsp25 dominantly accumulated in the aggresomes induced by proteasome inhibition. Molecular cloning of chicken Hsp25 (cHsp25) revealed that it belongs to the Hsp30 family, which is a subfamily of the alpha-crystallin/small Hsp gene family. Unexpectedly, overexpression of cHsp25 into HeLa cells promoted inclusion formation whereas overexpression of mouse Hsp27 and its chicken homologue did not. These results suggest that cHsp25 acts differently from other small Hsps on protein aggregates.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Avian Proteins / biosynthesis
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Blotting, Western
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Chickens
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Cloning, Molecular
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Crystallins / chemistry
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DNA, Complementary / metabolism
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Fibroblasts / metabolism
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HSP27 Heat-Shock Proteins
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HSP30 Heat-Shock Proteins
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HeLa Cells
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Heat-Shock Proteins / biosynthesis
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / physiology*
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Humans
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Inclusion Bodies
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins / physiology*
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Microscopy, Fluorescence
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Molecular Chaperones
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Molecular Sequence Data
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Neoplasm Proteins / chemistry
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Neoplasm Proteins / physiology*
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Phylogeny
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Protein Folding
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Protein Serine-Threonine Kinases / biosynthesis
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Quail
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Sequence Homology, Amino Acid
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Stress, Physiological*
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Ubiquitin / chemistry
Substances
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Avian Proteins
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Crystallins
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DNA, Complementary
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HSP27 Heat-Shock Proteins
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HSP30 Heat-Shock Proteins
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HSPB1 protein, human
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Heat-Shock Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Molecular Chaperones
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Neoplasm Proteins
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Ubiquitin
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MAP-kinase-activated kinase 2
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Protein Serine-Threonine Kinases