Proteomics

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Proteomic Profiles of Human Arterioles Isolated from Fresh Adipose Tissue or Following Overnight Storage


ABSTRACT: Arterioles are key determinants of the total peripheral vascular resistance, which, in turn, is a key determinant of arterial blood pressure. However, the amount of protein available from one isolated human arteriole may be less than 5µg, making proteomic analysis challenging. In addition, obtaining human arterioles requires manual dissection of unfrozen clinical specimens. This limits its feasibility, especially for powerful multi-center clinical studies in which clinical specimens need to be shipped overnight to a research lab for arteriole isolation. We performed a study to address low input, test overnight tissue storage, and develop a reference human arteriolar proteomic profile. In tandem mass tag proteomics, use of a booster channel consisting of human induced pluripotent stem cells-derived endothelial and vascular smooth muscle cells (1:5 ratio) increased the number of proteins detected in a human arteriole segment with FDR < 0.01 from 1,051 to more than 3,000. The correlation coefficient of proteomic profile was similar between replicate arterioles isolated freshly, following cold storage, or before and after the cold storage (one-way ANOVA, p=0.60). We built a human arteriolar proteomic profile consisting of 3,832 proteins based on the analysis of 12 arteriole samples from three subjects. Of 1,945 BP-relevant proteins that we curated, 476 (12.5%) were detected in the arteriolar proteome, which was a significant overrepresentation (Chi-squared, p<0.05). These findings demonstrate that proteomic analysis is feasible with arterioles isolated from human adipose tissue following cold overnight storage and provide a reference human arteriolar proteome profile highly valuable for studies of arteriole-related traits.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Microvessel

SUBMITTER: Rajan Pandey  

LAB HEAD: Mingyu Liang

PROVIDER: PXD044454 | Pride | 2024-03-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2150-TMT.pdStudy Other
2150-test-ProZero-LFQ.pdStudy Other
2150_Porter_220722_Ts024_Zero-LFQ_1.pdResult Other
2150_Porter_220722_Ts024_test-AllFr_01.mzML Mzml
2150_Porter_220722_Ts024_test-AllFr_01.mzid.gz Mzid
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