Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:4.1.2.13 (
aldolase
)
3,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Alpha-synuclein
, a major constituent of Lewy bodies (LBs) in Parkinson's disease (PD), has been implicated to play a critical role in synaptic events, such as neuronal plasticity during development, learning, and degeneration under pathological conditions, although the physiological function of
alpha-synuclein
has not yet been established. We here present biochemical evidence that recombinant
alpha-synuclein
has a chaperone-like function against thermal and chemical stress in vitro. In our experiments,
alpha-synuclein
protected glutathione S-transferase (GST) and
aldolase
from heat-induced precipitation, and alpha-lactalbumin and bovine serum albumin from dithiothreitol (DTT)-induced precipitation like other molecular chaperones. Moreover, preheating of
alpha-synuclein
, which is believed to reorganize the molecular surface of
alpha-synuclein
, increased the chaperone-like activity. Interestingly, in organic solvents, which promotes the formation of secondary structure,
alpha-synuclein
aggregated more easily than in its native condition, which eventually might abrogate the chaperone-like function of the protein. In addition,
alpha-synuclein
was also rapidly and significantly precipitated by heat in the presence of Zn2+ in vitro, whereas it was not affected by the presence of Ca2+ or Mg2+. Circular dichroism spectra confirmed that
alpha-synuclein
underwent conformational change in the presence of Zn2+. Taken together, our data suggest that
alpha-synuclein
could act as a molecular chaperone, and that the conformational change of the
alpha-synuclein
could explain the aggregation kinetics of
alpha-synuclein
, which may be related to the abolishment of the chaperonic-like activity.
...
PMID:Structural changes in alpha-synuclein affect its chaperone-like activity in vitro. 1120 70
Beta-synuclein exhibits high sequence homology and structural similarity with
alpha-synuclein
, a protein implicated in the pathogenesis of Parkinson's disease. We investigated the chaperone function of beta-synuclein and its anti-fibrillar activity in comparison with
alpha-synuclein
. beta-Synuclein suppressed the heat-induced aggregation of
aldolase
, alcohol dehydrogenase, and citrate synthase, and its anti-aggregative activity was remarkably higher than that of
alpha-synuclein
. Heat-induced inactivation of citrate synthase was significantly protected by beta-synuclein. Moreover, beta-synuclein inhibited the amyloid formation of both Abeta(1-40) and
alpha-synuclein
. It is, therefore, suggested that beta-synuclein can prevent abnormal protein aggregations more effectively than
alpha-synuclein
by acting as a molecular chaperone.
...
PMID:Beta-synuclein exhibits chaperone activity more efficiently than alpha-synuclein. 1547 47
