FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2024407722> ?p ?o ?g. }

• W2024407722 endingPage "6192" @default.
• W2024407722 startingPage "6186" @default.
• W2024407722 abstract "We analyzed the effect of the vacuolar H+-ATPase inhibitor bafilomycin A1 (bafA1) on the processing of β-amyloid precursor protein (βAPP). In kidney 293 cells stably transfected with the wild-type βAPP cDNA, bafA1 caused a stabilization of mature βAPP and its 10-kDa COOH-terminal fragment. Moreover, it caused a 2-3-fold increase in secretion of soluble APP and amyloid-β protein (Aβ). Interestingly, bafA1 treatment of cells transfected with a mutant βAPP isoform that occurs in a Swedish kindred with familial Alzheimer's disease resulted in a decrease of Aβ production and no increase of soluble APP secretion. Identical results were obtained when the effect of bafA1 was analyzed on fibroblasts derived from affected versus unaffected members of the Swedish family. These data demonstrate a differential effect of bafA1 on the production of Aβ derived from wild-type or Swedish mutant βAPP. Radiosequencing of Aβ derived from bafA1-treated cells expressing wild-type βAPP revealed a marked increase of Aβ peptides starting at amino acids phenylalanine 4 and valine −3 and a relative decrease of Aβ molecules beginning at the typical NH2 terminus of aspartate 1. Cells transfected with the Swedish mutation and treated with bafA1 did not produce these alternative Aβ peptides, so that bafA1 treatment resulted in a decrease of Aβ starting at aspartate 1. Our data indicate that multiple proteases are able to cleave Aβ at or near its NH2 terminus. Inhibition of the protease cleaving at aspartate 1 by bafA1 and perhaps other similar agents can result in an increase of alternatively cleaved peptides. We analyzed the effect of the vacuolar H+-ATPase inhibitor bafilomycin A1 (bafA1) on the processing of β-amyloid precursor protein (βAPP). In kidney 293 cells stably transfected with the wild-type βAPP cDNA, bafA1 caused a stabilization of mature βAPP and its 10-kDa COOH-terminal fragment. Moreover, it caused a 2-3-fold increase in secretion of soluble APP and amyloid-β protein (Aβ). Interestingly, bafA1 treatment of cells transfected with a mutant βAPP isoform that occurs in a Swedish kindred with familial Alzheimer's disease resulted in a decrease of Aβ production and no increase of soluble APP secretion. Identical results were obtained when the effect of bafA1 was analyzed on fibroblasts derived from affected versus unaffected members of the Swedish family. These data demonstrate a differential effect of bafA1 on the production of Aβ derived from wild-type or Swedish mutant βAPP. Radiosequencing of Aβ derived from bafA1-treated cells expressing wild-type βAPP revealed a marked increase of Aβ peptides starting at amino acids phenylalanine 4 and valine −3 and a relative decrease of Aβ molecules beginning at the typical NH2 terminus of aspartate 1. Cells transfected with the Swedish mutation and treated with bafA1 did not produce these alternative Aβ peptides, so that bafA1 treatment resulted in a decrease of Aβ starting at aspartate 1. Our data indicate that multiple proteases are able to cleave Aβ at or near its NH2 terminus. Inhibition of the protease cleaving at aspartate 1 by bafA1 and perhaps other similar agents can result in an increase of alternatively cleaved peptides." @default.
• W2024407722 created "2016-06-24" @default.
• W2024407722 creator A5004033835 @default.
• W2024407722 creator A5017314590 @default.
• W2024407722 creator A5043404109 @default.
• W2024407722 creator A5065084452 @default.
• W2024407722 creator A5087935119 @default.
• W2024407722 date "1995-03-01" @default.
• W2024407722 modified "2023-09-27" @default.
• W2024407722 title "The Vacuolar H+-ATPase Inhibitor Bafilomycin A1 Differentially Affects Proteolytic Processing of Mutant and Wild-type β-Amyloid Precursor Protein" @default.
• W2024407722 cites W1502820594 @default.
• W2024407722 cites W1521304851 @default.
• W2024407722 cites W1524969330 @default.
• W2024407722 cites W1531666134 @default.
• W2024407722 cites W1534308634 @default.
• W2024407722 cites W1539232350 @default.
• W2024407722 cites W1550693054 @default.
• W2024407722 cites W1553073688 @default.
• W2024407722 cites W1554535382 @default.
• W2024407722 cites W1570050776 @default.
• W2024407722 cites W1574959285 @default.
• W2024407722 cites W1599007193 @default.
• W2024407722 cites W1923107093 @default.
• W2024407722 cites W1968912921 @default.
• W2024407722 cites W1969810313 @default.
• W2024407722 cites W1971256323 @default.
• W2024407722 cites W1979543098 @default.
• W2024407722 cites W1980906872 @default.
• W2024407722 cites W1984996311 @default.
• W2024407722 cites W1986695958 @default.
• W2024407722 cites W2011424449 @default.
• W2024407722 cites W2030641075 @default.
• W2024407722 cites W2033382511 @default.
• W2024407722 cites W2035501441 @default.
• W2024407722 cites W2035853121 @default.
• W2024407722 cites W2038012168 @default.
• W2024407722 cites W2038086035 @default.
• W2024407722 cites W2049471629 @default.
• W2024407722 cites W2050111346 @default.
• W2024407722 cites W2053060747 @default.
• W2024407722 cites W2058110454 @default.
• W2024407722 cites W2058723245 @default.
• W2024407722 cites W2059804089 @default.
• W2024407722 cites W2065235688 @default.
• W2024407722 cites W2067811915 @default.
• W2024407722 cites W2081678091 @default.
• W2024407722 cites W2081881251 @default.
• W2024407722 cites W2084015178 @default.
• W2024407722 cites W2084338110 @default.
• W2024407722 cites W2086278983 @default.
• W2024407722 cites W2090150925 @default.
• W2024407722 cites W2120236371 @default.
• W2024407722 cites W2139818289 @default.
• W2024407722 cites W2153317225 @default.
• W2024407722 cites W2159846320 @default.
• W2024407722 cites W2166681711 @default.
• W2024407722 cites W2405724104 @default.
• W2024407722 doi "https://doi.org/10.1074/jbc.270.11.6186" @default.
• W2024407722 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7890753" @default.
• W2024407722 hasPublicationYear "1995" @default.
• W2024407722 type Work @default.
• W2024407722 sameAs 2024407722 @default.
• W2024407722 citedByCount "89" @default.
• W2024407722 countsByYear W20244077222012 @default.
• W2024407722 countsByYear W20244077222013 @default.
• W2024407722 countsByYear W20244077222014 @default.
• W2024407722 countsByYear W20244077222015 @default.
• W2024407722 countsByYear W20244077222016 @default.
• W2024407722 countsByYear W20244077222017 @default.
• W2024407722 countsByYear W20244077222019 @default.
• W2024407722 countsByYear W20244077222020 @default.
• W2024407722 countsByYear W20244077222021 @default.
• W2024407722 countsByYear W20244077222023 @default.
• W2024407722 crossrefType "journal-article" @default.
• W2024407722 hasAuthorship W2024407722A5004033835 @default.
• W2024407722 hasAuthorship W2024407722A5017314590 @default.
• W2024407722 hasAuthorship W2024407722A5043404109 @default.
• W2024407722 hasAuthorship W2024407722A5065084452 @default.
• W2024407722 hasAuthorship W2024407722A5087935119 @default.
• W2024407722 hasBestOaLocation W20244077221 @default.
• W2024407722 hasConcept C104317684 @default.
• W2024407722 hasConcept C142724271 @default.
• W2024407722 hasConcept C143065580 @default.
• W2024407722 hasConcept C153911025 @default.
• W2024407722 hasConcept C181199279 @default.
• W2024407722 hasConcept C182220744 @default.
• W2024407722 hasConcept C185592680 @default.
• W2024407722 hasConcept C190283241 @default.
• W2024407722 hasConcept C203522944 @default.
• W2024407722 hasConcept C207583985 @default.
• W2024407722 hasConcept C2776714187 @default.
• W2024407722 hasConcept C2777722557 @default.
• W2024407722 hasConcept C2779134260 @default.
• W2024407722 hasConcept C2779926675 @default.
• W2024407722 hasConcept C31705614 @default.
• W2024407722 hasConcept C49039625 @default.
• W2024407722 hasConcept C502032728 @default.
• W2024407722 hasConcept C54009773 @default.

• next