6 research outputs found
Mouse Organ-Specific Proteins and Functions
Organ-specific proteins (OSPs) possess great medical potential both in clinics and in biomedical research. Applications of them—such as alanine transaminase, aspartate transaminase, and troponins—in clinics have raised certain concerns of their organ specificity. The dynamics and diversity of protein expression in heterogeneous human populations are well known, yet their effects on OSPs are less addressed. Here, we used mice as a model and implemented a breadth study to examine the panorgan proteome for potential variations in organ specificity in different genetic backgrounds. Using reasonable resources, we generated panorgan proteomes of four in-bred mouse strains. The results revealed a large diversity that was more profound among OSPs than among proteomes overall. We defined a robustness score to quantify such variation and derived three sets of OSPs with different stringencies. In the meantime, we found that the enriched biological functions of OSPs are also organ-specific and are sensitive and useful to assess the quality of OSPs. We hope our breadth study can open doors to explore the molecular diversity and dynamics of organ specificity at the protein level. 
Mouse Organ-Specific Proteins and Functions
Organ-specific proteins (OSPs) possess great medical potential both in clinics and in biomedical research. Applications of them—such as alanine transaminase, aspartate transaminase, and troponins—in clinics have raised certain concerns of their organ specificity. The dynamics and diversity of protein expression in heterogeneous human populations are well known, yet their effects on OSPs are less addressed. Here, we used mice as a model and implemented a breadth study to examine the panorgan proteome for potential variations in organ specificity in different genetic backgrounds. Using reasonable resources, we generated panorgan proteomes of four in-bred mouse strains. The results revealed a large diversity that was more profound among OSPs than among proteomes overall. We defined a robustness score to quantify such variation and derived three sets of OSPs with different stringencies. In the meantime, we found that the enriched biological functions of OSPs are also organ-specific and are sensitive and useful to assess the quality of OSPs. We hope our breadth study can open doors to explore the molecular diversity and dynamics of organ specificity at the protein level
Glycocapture-Assisted Global Quantitative Proteomics (gagQP) Reveals Multiorgan Responses in Serum Toxicoproteome
Blood
is an ideal window for viewing our health and disease status.
Because blood circulates throughout the entire body and carries secreted,
shed, and excreted signature proteins from every organ and tissue
type, it is thus possible to use the blood proteome to achieve a comprehensive
assessment of multiple-organ physiology and pathology. To date, the
blood proteome has been frequently examined for diseases of individual
organs; studies on compound insults impacting multiple organs are,
however, elusive. We believe that a characterization of peripheral
blood for organ-specific proteins affords a powerful strategy to allow
early detection, staging, and monitoring of diseases and their treatments
at a whole-body level. In this paper we test this hypothesis by examining
a mouse model of acetaminophen (APAP)-induced hepatic and extra-hepatic
toxicity. We used a glycocapture-assisted global quantitative proteomics
(gagQP) approach to study serum proteins and validated our results
using Western blot. We discovered in mouse sera both hepatic and extra-hepatic
organ-specific proteins. From our validation, it was determined that
selected organ-specific proteins had changed their blood concentration
during the course of toxicity development and recovery. Interestingly,
the peak responding time of proteins specific to different organs
varied in a time-course study. The collected molecular information
shed light on a complex, dynamic, yet interweaving, multiorgan-enrolled
APAP toxicity. The developed technique as well as the identified protein
markers is translational to human studies. We hope our work can broaden
the utility of blood proteomics in diagnosis and research of the whole-body
response to pathogenic cues