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Glycosylation Tunes...
Glycosylation Tunes Neuroserpin Physiological and Pathological Properties
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- Visentin, Cristina (författare)
- Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy.
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- Broggini, Luca (författare)
- Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy.
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- Sala, Benedetta Maria (författare)
- KTH,Proteinvetenskap,Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy.;Karolinska Inst, Dept Med Solna, Sci Life Lab, SE-17176 Stockholm, Sweden.;Karolinska Univ Hosp, Div Infect Dis, SE-17176 Stockholm, Sweden.
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- Russo, Rosaria (författare)
- Univ Milan, Dipartimento Fisiopatol Med Chirurg Trapianti, Via Fratelli Cervi 93, I-20090 Segrate, Italy.
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- Barbiroli, Alberto (författare)
- Univ Milan, Dipartimento Sci Alimenti Nutr & Ambiente, Via Celoria 2, I-20133 Milan, Italy.
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- Santambrogio, Carlo (författare)
- Univ Milano Bicocca, Dipartimento Biotecnol & Biosci, Piazza Ateneo Nuovo 1, I-20126 Milan, Italy.
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- Nonnis, Simona (författare)
- Univ Milan, Dept Med Vet, Via Univ 6, I-26900 Lodi, Italy.
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- Dubnovitsky, Anatoly (författare)
- Karolinska Institutet
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- Bolognesi, Martino (författare)
- Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy.
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- Miranda, Elena (författare)
- Sapienza Univ Roma, Dipartimento Biol & Biotecnol Charles Darwin, Piazzale Aldo Moro 5, I-00185 Rome, Italy.;Sapienza Univ Roma, Ist Pasteur Fdn Cenci Bolognetti, Piazzale Aldo Moro 5, I-00185 Rome, Italy.
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- Achour, Adnane (författare)
- Karolinska Institutet
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- Ricagno, Stefano (författare)
- Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy.
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Univ Milan, Dipartimento Biosci, Via Celoria 26, I-20133 Milan, Italy Proteinvetenskap (creator_code:org_t)
- 2020-05-03
- 2020
- Engelska.
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Ingår i: International Journal of Molecular Sciences. - : MDPI AG. - 1661-6596 .- 1422-0067. ; 21:9
- Relaterad länk:
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https://doi.org/10.3...
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https://www.mdpi.com...
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https://urn.kb.se/re...
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https://doi.org/10.3...
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http://kipublication...
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Abstract
Ämnesord
Stäng
- Neuroserpin (NS) is a member of the serine protease inhibitors superfamily. Specific point mutations are responsible for its accumulation in the endoplasmic reticulum of neurons that leads to a pathological condition named familial encephalopathy with neuroserpin inclusion bodies (FENIB). Wild-type NS presents two N-glycosylation chains and does not form polymers in vivo, while non-glycosylated NS causes aberrant polymer accumulation in cell models. To date, all in vitro studies have been conducted on bacterially expressed NS, de facto neglecting the role of glycosylation in the biochemical properties of NS. Here, we report the expression and purification of human glycosylated NS (gNS) using a novel eukaryotic expression system, LEXSY. Our results confirm the correct N-glycosylation of wild-type gNS. The fold and stability of gNS are not altered compared to bacterially expressed NS, as demonstrated by the circular dichroism and intrinsic tryptophan fluorescence assays. Intriguingly, gNS displays a remarkably reduced polymerisation propensity compared to non-glycosylated NS, in keeping with what was previously observed for wild-type NS in vivo and in cell models. Thus, our results support the relevance of gNS as a new in vitro tool to study the molecular bases of FENIB.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Medicinsk bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Medical Biotechnology (hsv//eng)
Nyckelord
- neuroserpin
- protein polymerisation
- glycosylation
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Till lärosätets databas
- Av författaren/redakt...
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Visentin, Cristi ...
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Broggini, Luca
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Sala, Benedetta ...
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Russo, Rosaria
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Barbiroli, Alber ...
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Santambrogio, Ca ...
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visa fler...
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Nonnis, Simona
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Dubnovitsky, Ana ...
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Bolognesi, Marti ...
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Miranda, Elena
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Achour, Adnane
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Ricagno, Stefano
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- TEKNIK OCH TEKNOLOGIER
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TEKNIK OCH TEKNO ...
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Kungliga Tekniska Högskolan
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Karolinska Institutet