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:3.4.21.64 (
proteinase K
)
4,071
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Prion disease or transmissible spongiform encephalopathies are characterized by the presence of the abnormal form of the prion protein (PrP
Sc
). The pathological and transmissible properties of PrP
Sc
are enciphered in its secondary and tertiary structures. Since it's well established that different strains of prions are linked to different conformations of PrP
Sc
, biochemical characterization of prions seems a preliminary but reliable approach to detect, analyze, and compare prion strains. Experimental biochemical procedures might be helpful in distinguishing PrP
Sc
physicochemical properties and include resistance to
proteinase K
(PK) digestion, insolubility in nonionic detergents, PK-resistance under denaturing conditions and sedimentation properties in sucrose gradients. This biochemical approach has been extensively applied in human prion disorders and subsequently expanded for PrP
Sc
characterization in animals. In particular, in sporadic Creutzfedlt-Jakob disease (sCJD) PrP
Sc
is characterized by two main glycotypes conventionally named Type 1 and Type 2, based on the apparent gel migration at 21 and
19kDa
of the PrP
Sc
PK-resistant fragment. An additional PrP
Sc
type was identified in sCJD characterized by an unglycosylated dominant glycoform pattern and in 2010 a variably protease-sensitive prionopathy (VPSPr) was reported showing a PrP
Sc
with an electrophoretic ladder like pattern. Additionally, the presence of PrP
Sc
truncated fragments completes the electrophoretic characterization of different prion strains. By two-dimensional (2D) electrophoretic analysis additional PrP
Sc
pattern was identified, since this procedure provides information about the isoelectric point and the different peptides length related to PK cleavage, as well as to glycosylation extent or GPI anchor presence. We here provide and extensive review on PrP
Sc
biochemical analysis in human and animal prion disorders. Further, we show that PrP
Sc
glycotypes observed in CJD share similarities with PrP
Sc
in bovine spongiform encephalopathy forms (BSE).
...
PMID:Biochemical Characterization of Prions. 2883 71
