VWA7 – A Putative Human Phosphatidylcholine-specific Phospholipase C

For over four decades, the existence of mammalian phosphatidylcholine-specific phospholipase C (pc-PLC) has been reported. However, the gene encoding this enzyme has not been unambiguously determined to date. This study presents human von Willebrand factor A domain-containing protein 7 (VWA7) as putative pc-PLC and provides some biochemical insights into its potential function. Structural comparison of the modelled N-terminal region of VWA7 with Bacillus cereus pc-PLC revealed high similarity and, remarkably, a conserved active site architecture. The localization and activity of different VWA7 versions were investigated in mammalian cells. Eventually, pc-PLC activity was confirmed for VWA7 variants produced in bacteria, with the most active variant reaching 733 mU/mg. These findings establish a basis for future investigations on the role of human pc-PLC as well as on the poorly studied human VWA7.

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Publication Details

Journal
Journal of Molecular Biology
Published
2025-05-29
DOI
https://doi.org/10.1016/j.jmb.2025.169239
Citations
1
Primary Topic
Pancreatic function and diabetes
Type
article
Field-Weighted Citation Impact
2.01

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article

VWA7 – A Putative Human Phosphatidylcholine-specific Phospholipase C

Michael Burger, A. Klipp, Jean‐Christophe Leroux, Christina Greitens
1 citations
Journal of Molecular Biology
Pancreatic function and diabetes
2.01
article

VWA7 – A Putative Human Phosphatidylcholine-specific Phospholipase C

Michael Burger, A. Klipp, Jean‐Christophe Leroux, Christina Greitens
article en
1 citations

Abstract

For over four decades, the existence of mammalian phosphatidylcholine-specific phospholipase C (pc-PLC) has been reported. However, the gene encoding this enzyme has not been unambiguously determined to date. This study presents human von Willebrand factor A domain-containing protein 7 (VWA7) as putative pc-PLC and provides some biochemical insights into its potential function. Structural comparison of the modelled N-terminal region of VWA7 with Bacillus cereus pc-PLC revealed high similarity and, remarkably, a conserved active site architecture. The localization and activity of different VWA7 versions were investigated in mammalian cells. Eventually, pc-PLC activity was confirmed for VWA7 variants produced in bacteria, with the most active variant reaching 733 mU/mg. These findings establish a basis for future investigations on the role of human pc-PLC as well as on the poorly studied human VWA7.

Journal of Molecular BiologyVol. 437(17)
ETH Zurich (CH)
Eidgenössische Technische Hochschule Zürich, Horizon 2020 Framework Programme, European Research Council, HORIZON EUROPE European Research Council
Zero hunger
Openalex Percentile: Top 15%
Pancreatic function and diabetes
2.01
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