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000136321 0247_ $$2doi$$a10.1515/BC.2011.169
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000136321 041__ $$aEnglish
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000136321 1001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b0$$eFirst author$$udzne
000136321 245__ $$aThe Nicastrin ectodomain adopts a highly thermostable structure.
000136321 260__ $$aBerlin [u.a.]$$bde Gruyter$$c2011
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000136321 520__ $$aNicastrin is a type I transmembrane glycoprotein, which is part of the high molecular weight γ-secretase complex. γ-Secretase is one of the key players associated with the generation of Alzheimer's disease pathology, since it liberates the neurotoxic amyloid β-peptide. Four proteins Nicastrin, anterior pharynx-defective-1 (Aph-1), presenilin enhancer-2 (Pen-2) and Presenilin are essential to form the active γ-secretase complex. Recently it has been shown, that Nicastrin has a key function in stabilizing the mature γ-secretase complex and may also be involved in substrate recognition. So far no structural data for the Nicastrin ectodomain or any other γ-secretase component are available. We therefore used Circular Dichroism (CD) spectroscopy to demonstrate that Nicastrin, similar to its homologues, the Streptomyces griseus aminopeptidase (SGAP) and the transferrin receptor (TfR), adopts a thermostable secondary structure. Furthermore, the Nicastrin ectodomain has an exceptionally high propensity to refold after thermal denaturation. These findings provide evidence to further support the hypothesis that Nicastrin may share evolutionary conserved properties with the aminopeptidase and the transferrin receptor family.
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000136321 650_7 $$2NLM Chemicals$$aMembrane Glycoproteins
000136321 650_7 $$2NLM Chemicals$$aReceptors, Transferrin
000136321 650_7 $$2NLM Chemicals$$anicastrin protein
000136321 650_7 $$0EC 3.4.-$$2NLM Chemicals$$aAmyloid Precursor Protein Secretases
000136321 650_7 $$0EC 3.4.11.-$$2NLM Chemicals$$aAminopeptidases
000136321 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000136321 650_2 $$2MeSH$$aAminopeptidases: chemistry
000136321 650_2 $$2MeSH$$aAmyloid Precursor Protein Secretases: chemistry
000136321 650_2 $$2MeSH$$aCell Line
000136321 650_2 $$2MeSH$$aCircular Dichroism
000136321 650_2 $$2MeSH$$aHumans
000136321 650_2 $$2MeSH$$aMembrane Glycoproteins: chemistry
000136321 650_2 $$2MeSH$$aProtein Refolding
000136321 650_2 $$2MeSH$$aProtein Stability
000136321 650_2 $$2MeSH$$aProtein Structure, Secondary
000136321 650_2 $$2MeSH$$aProtein Structure, Tertiary
000136321 650_2 $$2MeSH$$aReceptors, Transferrin: chemistry
000136321 650_2 $$2MeSH$$aStreptomyces griseus: enzymology
000136321 650_2 $$2MeSH$$aTemperature
000136321 7001_ $$0P:(DE-HGF)0$$aKamp, Frits$$b1
000136321 7001_ $$aGrammer, Gudula$$b2
000136321 7001_ $$0P:(DE-HGF)0$$aNuscher, Brigitte$$b3
000136321 7001_ $$0P:(DE-2719)2000023$$aSteiner, Harald$$b4$$udzne
000136321 7001_ $$0P:(DE-HGF)0$$aBeyer, Klaus$$b5
000136321 7001_ $$0P:(DE-2719)2202037$$aHaass, Christian$$b6$$eLast author$$udzne
000136321 77318 $$2Crossref$$3journal-article$$a10.1515/bc.2011.169$$b : Walter de Gruyter GmbH, 2011-11-01$$n11$$tBiological Chemistry$$v392$$x1437-4315$$y2011
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000136321 9201_ $$0I:(DE-2719)1110000-2$$kAG Fluhrer$$lSignal Peptide Peptidases as Models for γ-Secretase$$x0
000136321 9201_ $$0I:(DE-2719)1110000-1$$kAG Steiner$$lBiochemistry of γ-Secretase$$x1
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