Multifunctional α-enolase: its role in diseases

@article{Pancholi2001MultifunctionalI,
  title={Multifunctional $\alpha$-enolase: its role in diseases},
  author={Vijaykumar Pancholi},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2001},
  volume={58},
  pages={902-920}
}
  • V. Pancholi
  • Published 1 June 2001
  • Biology
  • Cellular and Molecular Life Sciences CMLS
Abstract.Enolase, a key glycolytic enzyme, belongs to a novel class of surface proteins which do not possess classical machinery for surface transport, yet through an unknown mechanism are transported on the cell surface. Enolase is a multifunctional protein, and its ability to serve as a plasminogen receptor on the surface of a variety of hematopoetic, epithelial and endothelial cells suggests that it may play an important role in the intravascular and pericellular fibrinolytic system. Its… Expand

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References

SHOWING 1-10 OF 120 REFERENCES
The role of an enolase-related molecule in plasminogen binding to cells.
TLDR
The role of enolase as a cell-surface plasminogen-binding site with profibrinolytic functions is established as well as the role of immunopurified alpha-enolase in the interaction of these isoforms with plAsminogen. Expand
α-Enolase, a Novel Strong Plasmin(ogen) Binding Protein on the Surface of Pathogenic Streptococci*
TLDR
These findings, showing both the protected protease activity of SEN-bound plasmin and SEN-specific immune responses, provide evidence for an important role of SEN in the disease process and post-streptococcal autoimmune diseases. Expand
Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display.
TLDR
Data indicate that this sequence contains the epitope recognized by mAB 9C12 and is, therefore, exposed on the cell surface, further suggesting that alpha-enolase and alpha-ERM share common amino acid sequences. Expand
Autoantibodies to the centrosome (centriole) react with determinants present in the glycolytic enzyme enolase.
TLDR
This work has studied autoantibodies from patients that react with the centrosome (centriole) region of the cell and found by immunoblotting techniques that these antibodies react with a 48-kDa protein. Expand
Identification of a glucan-associated enolase as a main cell wall protein of Candida albicans and an indirect target of lipopeptide antimycotics.
Growth-subinhibitory nonlytic doses of cilofungin (lipopeptide antibiotic affecting (1,3)-beta-D-glucan synthesis) inhibited the incorporation of 46- to 48-kDa glucan-associated (46K) protein intoExpand
Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.
TLDR
It is shown for the first time that pure betabeta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), favouring the hypothesis that these three enzymes form a functional glycoleytic segment. Expand
New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase.
  • M. Sirover
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1999
TLDR
The mechanisms through which mammalian cells may utilize GAPDH amino acid sequences to provide new functions and to determine its intracellular localization are considered and the interrelationship between new GAPDh activities and its role in cell pathologies is addressed. Expand
The cell biology of the plasminogen system
TLDR
Shared binding sites for lipoprotein(a) and plasmin(ogen) on cell surfaces and in the sub endothelial matrix may contribute to the pathogenetic risks associated with elevated levels of lipop protein(a). Expand
Minireview. Emerging new functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells.
Recent evidence indicates new, intriguing roles for the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), in fundamental mammalian cell processes. These include its role in DNAExpand
Clinical biochemistry of neuron specific enolase.
The soluble brain protein 14-3-2 first described by Moore and McGregor in 1965 is now known to be a cell specific isoenzyme of the glycolytic enzyme enolase (EC 4.2.1.11), designated neuron specificExpand
...
1
2
3
4
5
...