Proteomics

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Anastellin impacts on the processing of extracellular matrix and stimulates the release of cytokines from smooth muscle cells

ABSTRACT: Anastellin, a recombinant protein fragment from the first type III module of fibronectin, mimics a partially-unfolded intermediate with exposed cryptic protein-protein interaction sites implicated in assembly of fibronectin fibrils. Anastellin initiates in vitro fibrillation of fibronectin, yielding “superfibronectin”, a polymer with enhanced cell-adhesive properties. This ability is absent in an anastellin double mutant, L37AY40A. Here we demonstrate that both wild-type and L37AY40A anastellin affects fibronectin processing within the ECM of smooth muscle cells. FN fibrils are diminished in the ECM from cells treated with anastellin, but are partially rescued by supplementation with plasma fibronectin in cell media. Proteomics analysis reveals that anastellin also impacts on the processing of other ECM proteins, with increased collagen and decreased laminin detected in media from cells exposed to wild-type anastellin.

INSTRUMENT(S): Bruker Daltonics timsTOF series

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Smooth Muscle Cell Of The Coronary Artery

SUBMITTER: Per Hägglund  

LAB HEAD: Per Hägglund

PROVIDER: PXD033732 | Pride | 2023-02-01

REPOSITORIES: Pride

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Dataset's files

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Action DRS
20220311_AN_Mut_Ctrl.pg_matrix.tsv Tabular
AN_1_BA5_1_6983.d.zip Other
AN_2_BA6_1_6984.d.zip Other
AN_BA4_1_6982.d.zip Other
Ctrl_1_BA2_1_6979.d.zip Other
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Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells.

He Jianfei J   Steffen Jonas Hyld JH   Thulstrup Peter Waaben PW   Pedersen Jannik Nedergaard JN   Sauerland Max B MB   Otzen Daniel E DE   Hawkins Clare L CL   Gourdon Pontus P   Davies Michael J MJ   Hägglund Per P  

Scientific reports 20221221 1

Anastellin, a recombinant protein fragment from the first type III module of fibronectin, mimics a partially unfolded intermediate implicated in the assembly of fibronectin fibrils. Anastellin influences the structure of fibronectin and initiates in vitro fibrillation, yielding "superfibronectin", a polymer with enhanced cell-adhesive properties. This ability is absent in an anastellin double mutant, L37AY40A. Here we demonstrate that both wild-type and L37AY40A anastellin affect fibronectin pro  ...[more]

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