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Recombinant PNPLA3 ...
Recombinant PNPLA3 protein shows triglyceride hydrolase activity and its I148M mutation results in loss of function.
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- Pingitore, Piero, 1986 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Pirazzi, Carlo (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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- Mancina, Rosellina Margherita (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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- Motta, Benedetta Maria (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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Indiveri, Cesare (author)
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Pujia, Arturo (author)
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Montalcini, Tiziana (author)
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- Hedfalk, Kristina, 1969 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Romeo, Stefano, 1976 (author)
- Gothenburg University,Göteborgs universitet,Wallenberglaboratoriet,Wallenberg Laboratory
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(creator_code:org_t)
- Elsevier BV, 2014
- 2014
- English.
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In: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. - : Elsevier BV. - 1388-1981. ; 1841:4, s. 574-580
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Abstract
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- The patatin-like phospholipase domain containing 3 (PNPLA3, also called adiponutrin, ADPN) is a membrane-bound protein highly expressed in the liver. The genetic variant I148M (rs738409) was found to be associated with progression of chronic liver disease. We aimed to establish a protein purification protocol in a yeast system (Pichia pastoris) and to examine the human PNPLA3 enzymatic activity, substrate specificity and the I148M mutation effect. hPNPLA3 148I wild type and 148M mutant cDNA were cloned into P. pastoris expression vectors. Yeast cells were grown in 3L fermentors. PNPLA3 protein was purified from membrane fractions by Ni-affinity chromatography. Enzymatic activity was assessed using radiolabeled substrates. Both 148I wild type and 148M mutant proteins are localized to the membrane. The wild type protein shows a predominant lipase activity with mild lysophosphatidic acid acyl transferase activity (LPAAT) and the I148M mutation results in a loss of function of both these activities. Our data show that PNPLA3 has a predominant lipase activity and I148M mutation results in a loss of function.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Pingitore, Piero ...
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Pirazzi, Carlo
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Mancina, Roselli ...
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Motta, Benedetta ...
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Indiveri, Cesare
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Pujia, Arturo
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Montalcini, Tizi ...
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Hedfalk, Kristin ...
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Romeo, Stefano, ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
- Articles in the publication
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Biochimica et Bi ...
- By the university
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University of Gothenburg