Proteomics

Dataset Information

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Site-specific 5-hydroxy-tryptophan incorporation into apolipoprotein A-I impairs cholesterol efflux activity and high density lipoprotein biogenesis


ABSTRACT: We used genetic code expansion technology with an engineered Saccharomyces cerevisiae tryptophanyl tRNA- synthetase:suppressor tRNA pair in Escherichia coli, to directly insert the non- canonical amino acid 5-OH tryptophan (5-OHTrp) at position 72 in human apoA-I. Characterization of recombinant human apoA-I by mass spectrometry confirmed successful site-specific incorporation of Trp(5-OH) in apoA-I.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Blood Plasma

DISEASE(S): Atherosclerosis

SUBMITTER: Valentin Gogonea  

LAB HEAD: Stanley L. Hazen

PROVIDER: PXD017226 | Pride | 2020-03-02

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
A11_apoAI_WT.msf Msf
A11_apoAI_WT.raw Raw
A12_apoAI_WT.msf Msf
A12_apoAI_WT.raw Raw
A22_apoAI_WT.msf Msf
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Publications

Site-specific 5-hydroxytryptophan incorporation into apolipoprotein A-I impairs cholesterol efflux activity and high-density lipoprotein biogenesis.

Zamanian-Daryoush Maryam M   Gogonea Valentin V   DiDonato Anthony J AJ   Buffa Jennifer A JA   Choucair Ibrahim I   Levison Bruce S BS   Hughes Randall A RA   Ellington Andrew D AD   Huang Ying Y   Li Xinmin S XS   DiDonato Joseph A JA   Hazen Stanley L SL  

The Journal of biological chemistry 20200225 15


Apolipoprotein A-I (apoA-I) is the major protein constituent of high-density lipoprotein (HDL) and a target of myeloperoxidase-dependent oxidation in the artery wall. In atherosclerotic lesions, apoA-I exhibits marked oxidative modifications at multiple sites, including Trp<sup>72</sup> Site-specific mutagenesis studies have suggested, but have not conclusively shown, that oxidative modification of Trp<sup>72</sup> of apoA-I impairs many atheroprotective properties of this lipoprotein. Herein, w  ...[more]

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