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dc.contributor.authorVanz, Ana Letícia
dc.contributor.authorNimtz, Manfred
dc.contributor.authorRinas, Ursula
dc.date.accessioned2015-10-15T08:01:43Zen
dc.date.available2015-10-15T08:01:43Zen
dc.date.issued2014en
dc.identifier.citationDecrease of UPR- and ERAD-related proteins in Pichia pastoris during methanol-induced secretory insulin precursor production in controlled fed-batch cultures. 2014, 13 (1):23 Microb. Cell Fact.en
dc.identifier.issn1475-2859en
dc.identifier.pmid24521445en
dc.identifier.doi10.1186/1475-2859-13-23en
dc.identifier.urihttp://hdl.handle.net/10033/579716en
dc.description.abstractPichia pastoris is a popular yeast preferably employed for secretory protein production. Secretion is not always efficient and endoplasmic retention of proteins with aberrant folding properties, or when produced at exaggerated rates, can occur. In these cases production usually leads to an unfolded protein response (UPR) and the induction of the endoplasmic reticulum associated degradation (ERAD). P. pastoris is nowadays also an established host for secretory insulin precursor (IP) production, though little is known about the impact of IP production on the host cell physiology, in particular under industrially relevant production conditions. Here, we evaluate the cellular response to aox1 promoter-controlled, secretory IP production in controlled fed-batch processes using a proteome profiling approach.
dc.language.isoenen
dc.subject.meshBatch Cell Culture Techniquesen
dc.subject.meshEndoplasmic Reticulum-Associated Degradationen
dc.subject.meshGlycerolen
dc.subject.meshMethanolen
dc.subject.meshPichiaen
dc.subject.meshProinsulinen
dc.subject.meshProteomeen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshSecretory Pathwayen
dc.subject.meshUnfolded Protein Responseen
dc.titleDecrease of UPR- and ERAD-related proteins in Pichia pastoris during methanol-induced secretory insulin precursor production in controlled fed-batch cultures.en
dc.typeArticleen
dc.identifier.journalMicrobial cell factoriesen
refterms.dateFOA2018-06-12T16:50:21Z
html.description.abstractPichia pastoris is a popular yeast preferably employed for secretory protein production. Secretion is not always efficient and endoplasmic retention of proteins with aberrant folding properties, or when produced at exaggerated rates, can occur. In these cases production usually leads to an unfolded protein response (UPR) and the induction of the endoplasmic reticulum associated degradation (ERAD). P. pastoris is nowadays also an established host for secretory insulin precursor (IP) production, though little is known about the impact of IP production on the host cell physiology, in particular under industrially relevant production conditions. Here, we evaluate the cellular response to aox1 promoter-controlled, secretory IP production in controlled fed-batch processes using a proteome profiling approach.


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