FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2082573867> ?p ?o ?g. }

• W2082573867 endingPage "19507" @default.
• W2082573867 startingPage "19500" @default.
• W2082573867 abstract "Matriptase-2 is a hepatic membrane serine protease that regulates iron homeostasis. Defects in matriptase-2 cause iron deficiency anemia. In cells, matriptase-2 is synthesized as a zymogen. To date, how matriptase-2 expression and activation are regulated remains poorly understood. Here we expressed human matriptase-2 in HEK293 and hepatic BEL-7402, SMMC-7721, and QGY-7703 cells. By labeling cell surface proteins and Western analysis, we examined matriptase-2 cell surface expression, zymogen activation, and ectodomain shedding. Our results show that matriptase-2 was activated on the cell surface but not intracellularly. Activated matriptase-2 underwent ectodomain shedding, producing soluble fragments in the conditioned medium. By testing inactive mutants, R576A and S762A, we found that matriptase-2 activation and shedding were mediated by its own catalytic activity and that the one-chain form of matriptase-2 had little activity in ectodomain shedding. We made additional matriptase-2 mutants, N136Q, N184Q, N216Q, N338Q, N433Q, N453Q, and N518Q, in which each of the predicted N-glycosylation sites was mutated. All of these mutants were expressed on the cell surface. However, mutants N216Q, N453Q, and N518Q, but not the other mutants, had impaired zymogen activation and ectodomain shedding. Our results indicate that N-glycans at specific sites are critical for matriptase-2 activation. Together, these data provide new insights into the cell surface expression, zymogen activation, and ectodomain shedding of matriptase-2. Matriptase-2 is a hepatic membrane serine protease that regulates iron homeostasis. Defects in matriptase-2 cause iron deficiency anemia. In cells, matriptase-2 is synthesized as a zymogen. To date, how matriptase-2 expression and activation are regulated remains poorly understood. Here we expressed human matriptase-2 in HEK293 and hepatic BEL-7402, SMMC-7721, and QGY-7703 cells. By labeling cell surface proteins and Western analysis, we examined matriptase-2 cell surface expression, zymogen activation, and ectodomain shedding. Our results show that matriptase-2 was activated on the cell surface but not intracellularly. Activated matriptase-2 underwent ectodomain shedding, producing soluble fragments in the conditioned medium. By testing inactive mutants, R576A and S762A, we found that matriptase-2 activation and shedding were mediated by its own catalytic activity and that the one-chain form of matriptase-2 had little activity in ectodomain shedding. We made additional matriptase-2 mutants, N136Q, N184Q, N216Q, N338Q, N433Q, N453Q, and N518Q, in which each of the predicted N-glycosylation sites was mutated. All of these mutants were expressed on the cell surface. However, mutants N216Q, N453Q, and N518Q, but not the other mutants, had impaired zymogen activation and ectodomain shedding. Our results indicate that N-glycans at specific sites are critical for matriptase-2 activation. Together, these data provide new insights into the cell surface expression, zymogen activation, and ectodomain shedding of matriptase-2." @default.
• W2082573867 created "2016-06-24" @default.
• W2082573867 creator A5006668200 @default.
• W2082573867 creator A5041956749 @default.
• W2082573867 creator A5050313380 @default.
• W2082573867 creator A5060259605 @default.
• W2082573867 creator A5060284901 @default.
• W2082573867 creator A5061354837 @default.
• W2082573867 creator A5084792129 @default.
• W2082573867 date "2014-07-01" @default.
• W2082573867 modified "2023-10-14" @default.
• W2082573867 title "N-Glycosylation Is Required for Matriptase-2 Autoactivation and Ectodomain Shedding" @default.
• W2082573867 cites W1550867738 @default.
• W2082573867 cites W1578028616 @default.
• W2082573867 cites W1832976650 @default.
• W2082573867 cites W1885241490 @default.
• W2082573867 cites W1964050759 @default.
• W2082573867 cites W1966509874 @default.
• W2082573867 cites W1977845897 @default.
• W2082573867 cites W1979134200 @default.
• W2082573867 cites W1980663890 @default.
• W2082573867 cites W1982180165 @default.
• W2082573867 cites W1984773555 @default.
• W2082573867 cites W1987961752 @default.
• W2082573867 cites W1992858904 @default.
• W2082573867 cites W1994352714 @default.
• W2082573867 cites W2012956876 @default.
• W2082573867 cites W2013180631 @default.
• W2082573867 cites W2016021454 @default.
• W2082573867 cites W2020150065 @default.
• W2082573867 cites W2020745334 @default.
• W2082573867 cites W2028943315 @default.
• W2082573867 cites W2036200292 @default.
• W2082573867 cites W2037632814 @default.
• W2082573867 cites W2046410714 @default.
• W2082573867 cites W2048448975 @default.
• W2082573867 cites W2048657871 @default.
• W2082573867 cites W2068339549 @default.
• W2082573867 cites W2069849774 @default.
• W2082573867 cites W2070165530 @default.
• W2082573867 cites W2070751916 @default.
• W2082573867 cites W2072551243 @default.
• W2082573867 cites W2074125004 @default.
• W2082573867 cites W2076234811 @default.
• W2082573867 cites W2079035228 @default.
• W2082573867 cites W2083714563 @default.
• W2082573867 cites W2085132515 @default.
• W2082573867 cites W2093104438 @default.
• W2082573867 cites W2094945284 @default.
• W2082573867 cites W2101543922 @default.
• W2082573867 cites W2108843246 @default.
• W2082573867 cites W2109406699 @default.
• W2082573867 cites W2114556481 @default.
• W2082573867 cites W2114716461 @default.
• W2082573867 cites W2119445810 @default.
• W2082573867 cites W2132916747 @default.
• W2082573867 cites W2144801974 @default.
• W2082573867 cites W2164451457 @default.
• W2082573867 cites W2168209462 @default.
• W2082573867 doi "https://doi.org/10.1074/jbc.m114.555110" @default.
• W2082573867 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4094060" @default.
• W2082573867 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24867957" @default.
• W2082573867 hasPublicationYear "2014" @default.
• W2082573867 type Work @default.
• W2082573867 sameAs 2082573867 @default.
• W2082573867 citedByCount "36" @default.
• W2082573867 countsByYear W20825738672014 @default.
• W2082573867 countsByYear W20825738672015 @default.
• W2082573867 countsByYear W20825738672016 @default.
• W2082573867 countsByYear W20825738672017 @default.
• W2082573867 countsByYear W20825738672018 @default.
• W2082573867 countsByYear W20825738672019 @default.
• W2082573867 countsByYear W20825738672020 @default.
• W2082573867 countsByYear W20825738672021 @default.
• W2082573867 countsByYear W20825738672022 @default.
• W2082573867 countsByYear W20825738672023 @default.
• W2082573867 crossrefType "journal-article" @default.
• W2082573867 hasAuthorship W2082573867A5006668200 @default.
• W2082573867 hasAuthorship W2082573867A5041956749 @default.
• W2082573867 hasAuthorship W2082573867A5050313380 @default.
• W2082573867 hasAuthorship W2082573867A5060259605 @default.
• W2082573867 hasAuthorship W2082573867A5060284901 @default.
• W2082573867 hasAuthorship W2082573867A5061354837 @default.
• W2082573867 hasAuthorship W2082573867A5084792129 @default.
• W2082573867 hasBestOaLocation W20825738671 @default.
• W2082573867 hasConcept C1009742 @default.
• W2082573867 hasConcept C170493617 @default.
• W2082573867 hasConcept C181199279 @default.
• W2082573867 hasConcept C185592680 @default.
• W2082573867 hasConcept C2776714187 @default.
• W2082573867 hasConcept C2777313579 @default.
• W2082573867 hasConcept C2777807008 @default.
• W2082573867 hasConcept C2778775115 @default.
• W2082573867 hasConcept C55493867 @default.
• W2082573867 hasConcept C86803240 @default.
• W2082573867 hasConcept C95444343 @default.
• W2082573867 hasConceptScore W2082573867C1009742 @default.
• W2082573867 hasConceptScore W2082573867C170493617 @default.

• next