Document Detail

Immunocytochemical detection of the 70-kd heat shock protein in alcoholic liver disease.
MedLine Citation:
PMID:  1693268     Owner:  NLM     Status:  MEDLINE    
Exposure of cells to physical (eg, heat) or chemical (eg, alcohol) stress results in increased synthesis of a set of highly conserved polypeptides termed heat shock proteins (HSPs), among which the 70-kd protein (HSP 70) is one of the most consistently inducible and highly conserved. This HSP has adenosine triphosphate-binding properties and is known to associate strongly with cytoskeletal structures that are usually disrupted on injury by heat or alcohol. Some HSPs apparently function as accessories to a nonlysosomal, adenosine triphosphate-dependent proteolytic system that binds and digests away stress-generated abnormal or denatured proteins after their conjugation with ubiquitin, a small HSP. Ubiquitin has been demonstrated immunocytochemically in Mallory bodies, which represent mainly degenerated intermediate filaments accumulated in hepatocytes of alcoholic-diseased liver. We immunostained histologic sections from patients with alcoholic liver disease using a polyclonal antibody raised against HSP 70. Strong diffuse cytoplasmic immunoreactivity was observed in many hepatocytes, including cells without Mallory bodies or fatty degeneration. Positive immunoreactivity for HSP 70 points to a possible involvement of this HSP in the pathogenesis of alcoholic liver disease. It also suggests that immunocytochemical detection of HSP 70 may serve as a more sensitive indicator of hepatocellular injury.
R Omar; M Pappolla; B Saran
Related Documents :
14638828 - Are hsps suitable for indicating stressed states in fish?
18923828 - Comparative proteome analysis of robust saccharomyces cerevisiae insights into industri...
16841168 - Induced and constitutive heat shock protein expression in the olfactory system--a revie...
26088 - Heat shock of drosophila melanogaster induces the synthesis of new messenger rnas and p...
25231958 - Differential expression and interaction specificity of heterotrimeric g-protein family ...
25450978 - Fe-s proteins that regulate gene expression.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Archives of pathology & laboratory medicine     Volume:  114     ISSN:  0003-9985     ISO Abbreviation:  Arch. Pathol. Lab. Med.     Publication Date:  1990 Jun 
Date Detail:
Created Date:  1990-07-03     Completed Date:  1990-07-03     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  7607091     Medline TA:  Arch Pathol Lab Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  589-92     Citation Subset:  AIM; IM    
Department of Pathology, West Virginia University School of Medicine, Morgantown 26506.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Heat-Shock Proteins / analysis*
Immunoenzyme Techniques
Inclusion Bodies / analysis
Liver / pathology
Liver Diseases, Alcoholic / metabolism*,  pathology
Middle Aged
Staining and Labeling
Reg. No./Substance:
0/Heat-Shock Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Acridine orange--RNA histofluorescence of sarcomas and small round cell tumors of childhood.
Next Document:  Primary retroperitoneal angiosarcoma with eosinophilic globules. A combined light-microscopic, immun...