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000136944 0247_ $$2doi$$a10.1002/jbmr.1895
000136944 0247_ $$2pmid$$apmid:23426979
000136944 0247_ $$2ISSN$$a0884-0431
000136944 0247_ $$2ISSN$$a1523-4681
000136944 037__ $$aDZNE-2020-03266
000136944 041__ $$aEnglish
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000136944 1001_ $$0P:(DE-HGF)0$$aBronckers, Antonius L J J$$b0$$eCorresponding author
000136944 245__ $$aThe intramembrane protease SPPL2A is critical for tooth enamel formation.
000136944 260__ $$aHoboken, NJ [u.a.]$$bWiley$$c2013
000136944 264_1 $$2Crossref$$3online$$bWiley$$c2013-06-18
000136944 264_1 $$2Crossref$$3print$$bWiley$$c2013-07-01
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000136944 520__ $$aIntramembrane proteases are critically involved in signal transduction and membrane protein turnover. Signal-peptide-peptidase-like 2a (SPPL2A), a presenilin-homologue residing in lysosomes/late endosomes, cleaves type II-oriented transmembrane proteins. We recently identified SPPL2A as the enzyme controlling turnover and functions of the invariant chain (CD74) of the major histocompatibility complex II (MHCII) and demonstrated critical importance of this process for B cell development. Surprisingly, we found that SPPL2A is critical for formation of dental enamel. In Sppl2a knockout mice, enamel of the erupted incisors was chalky white and rapidly eroded after eruption. SPPL2A was found to be expressed in enamel epithelium during secretory and maturation stage amelogenesis. Mineral content of enamel in Sppl2a⁻/⁻ incisors was inhomogeneous and reduced by ∼20% compared to wild-type mice with the most pronounced reduction at the mesial side. Frequently, disruption of the enamel layer and localized detachment of the most superficial enamel layer was observed in the knockout incisors leading to an uneven enamel surface. In Sppl2a null mice, morphology and function of secretory stage ameloblasts were not noticeably different from that of wild-type mice. However, maturation stage ameloblasts showed reduced height and a characteristic undulation of the ameloblast layer with localized adherence of the cells to the outer enamel. This was reflected in a delayed and incomplete resorption of the proteinaceous enamel matrix. Thus, we conclude that intramembrane proteolysis by SPPL2A is essential for maintaining cellular homeostasis of ameloblasts. Because modulation of SPPL2A activity appears to be an attractive therapeutic target to deplete B cells and treat autoimmunity, interference with tooth enamel formation should be investigated as a possible adverse effect of pharmacological SPPL2A inhibitors in humans.
000136944 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000136944 542__ $$2Crossref$$i2015-09-01$$uhttp://doi.wiley.com/10.1002/tdm_license_1.1
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000136944 650_7 $$2NLM Chemicals$$aAntigens, Differentiation, B-Lymphocyte
000136944 650_7 $$2NLM Chemicals$$aHistocompatibility Antigens Class II
000136944 650_7 $$2NLM Chemicals$$aMembrane Proteins
000136944 650_7 $$2NLM Chemicals$$ainvariant chain
000136944 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aAspartic Acid Endopeptidases
000136944 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aSPPL2a protein, mouse
000136944 650_2 $$2MeSH$$aAmeloblasts: enzymology
000136944 650_2 $$2MeSH$$aAnimals
000136944 650_2 $$2MeSH$$aAntigens, Differentiation, B-Lymphocyte: genetics
000136944 650_2 $$2MeSH$$aAntigens, Differentiation, B-Lymphocyte: metabolism
000136944 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: genetics
000136944 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000136944 650_2 $$2MeSH$$aDental Enamel: enzymology
000136944 650_2 $$2MeSH$$aDental Enamel: growth & development
000136944 650_2 $$2MeSH$$aHistocompatibility Antigens Class II: genetics
000136944 650_2 $$2MeSH$$aHistocompatibility Antigens Class II: metabolism
000136944 650_2 $$2MeSH$$aIncisor: enzymology
000136944 650_2 $$2MeSH$$aIncisor: growth & development
000136944 650_2 $$2MeSH$$aMembrane Proteins: genetics
000136944 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000136944 650_2 $$2MeSH$$aMice
000136944 650_2 $$2MeSH$$aMice, Knockout
000136944 650_2 $$2MeSH$$aProteolysis
000136944 7001_ $$0P:(DE-HGF)0$$aGueneli, Nur$$b1
000136944 7001_ $$0P:(DE-HGF)0$$aLüllmann-Rauch, Renate$$b2
000136944 7001_ $$0P:(DE-HGF)0$$aSchneppenheim, Janna$$b3
000136944 7001_ $$0P:(DE-HGF)0$$aMoraru, Andreea P$$b4
000136944 7001_ $$0P:(DE-HGF)0$$aHimmerkus, Nina$$b5
000136944 7001_ $$0P:(DE-HGF)0$$aBervoets, Theodore J$$b6
000136944 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b7$$udzne
000136944 7001_ $$0P:(DE-HGF)0$$aEverts, Vincent$$b8
000136944 7001_ $$0P:(DE-HGF)0$$aSaftig, Paul$$b9
000136944 7001_ $$0P:(DE-HGF)0$$aSchröder, Bernd$$b10
000136944 77318 $$2Crossref$$3journal-article$$a10.1002/jbmr.1895$$b : Wiley, 2013-06-18$$n7$$p1622-1630$$tJournal of Bone and Mineral Research$$v28$$x0884-0431$$y2013
000136944 773__ $$0PERI:(DE-600)2008867-X$$a10.1002/jbmr.1895$$gVol. 28, no. 7, p. 1622 - 1630$$n7$$p1622-1630$$q28:7<1622 - 1630$$tJournal of bone and mineral research$$v28$$x0884-0431$$y2013
000136944 8564_ $$uhttps://pub.dzne.de/record/136944/files/DZNE-2020-03266_Restricted.pdf
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000136944 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2000007$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b7$$kDZNE
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000136944 9141_ $$y2013
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000136944 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ BONE MINER RES : 2017
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