HomeHealth articleshuman ureter proteomeWhat Is a Human Ureter Proteome?

A Proteomic Glimpse Into Human Ureter Proteome

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A detailed study of urinary proteins helps better diagnose several disorders. Read to know more about the human ureter proteome.

Written by

Dr. Saima Yunus

Published At December 23, 2022
Reviewed AtDecember 23, 2022

What Is a Proteome?

The proteome is the entire set of proteins expressed in the form of a genome, tissue, cell, or organism under certain conditions at a given time. The study of the proteome is known as “ proteomics.”

What Is a Human Ureter Proteome?

Several diseases can be diagnosed by detecting alterations in the composition of urine, including various proteins and polypeptides. Urine is regarded as an essential biofluid in proteomics. It is used in proteomics because of its stability and noninvasive nature. Most of the proteins found in the urine usually originate from the urogenital tract. However, the exact source of these proteins in the urinary tract is difficult to determine. The specific part of the urogenital tract, like the kidneys, ureter, or urinary bladder, is still not specified.

The human urinary proteome is screened for disease biomarkers. It is preferred over other biofluids like plasma and serum because of its relative simplicity and stability, particularly for the identification of protein or peptide biomarkers. Urine is produced by the kidneys and carried by the ureters, 25 to 30 cm tubes in length, and stored in the urinary bladder. In this process, 90 percent of the urine is reabsorbed. The remaining 10 percent of urine consists of wasted molecules and some protein molecules found in the urogenital tract and plasma.

What Are Proteins Found in the Human Ureter?

A comprehensive study or analysis of the ureter proteome has been performed. This study concluded that out of 2217 nonredundant ureter proteins, 751 proteins, or 33.8 percent, were detected as urinary or polypeptide proteins. When ureter proteins not shown in this study were compared to urinary bladder and prostate human proteins, it was reported that 21 proteins are specifically present in the ureter tissue. This finding will further help in the identification of biomarkers associated with ureter diseases like ureter carcinoma. Human ureter proteomics further helps to provide important information to scientists working in the field of urine biomarker discovery and urology in general.

The urinary proteins may originate from the following:

  • Secretions of soluble proteins in the renal tubules.

  • Sloughed cells of the urogenital tract.

  • Glomerular‐filtrate plasma proteins.

  • Membranous or cytosolic exosomal proteins.

  • Glycosylphosphatidylinositol‐anchored protein like uromodulin.

In a normal healthy individual, the urinary proteome that originates in the urogenital tract accounts for 70 percent. The remaining 30 percent are plasma proteins that originate in the glomerulus (a part of the kidney responsible for filtration and composed of a network of capillaries).

What Is the Potential Use of the Urinary Proteome?

The potential uses of the urinary proteome have been described in the following urogenital diseases:

What Is Analyzed in the Ureter Proteome?

It was proposed that some of the proteins may be released in urine as it passes through the ureter as exosomes or as a shredded epithelium. To confirm this, the ureter proteome was compared with an exosomal urinary database, comprehensive mass spectrometric urinary database, and kidney database. Further, the retained proteins of the ureter were compared to prostate and urinary bladder databases from the human protein atlas (HPA).

A normal healthy sample of around four to five centimeters in length was dissected from a ureter of a diseased kidney. Protein extracts were identified by putting the dissected ureter tissues in a protein prefractionation buffer containing thiourea, urea, Dithiothreitol (DTT), glycerol, and buffer with ampholytes of pH three to ten. Further, Complete ultra proteases were added to the buffer, and for protein extraction, the Precellys 24 tissue homogenizer was employed at four degrees Celsius. Then the two milligrams of protein extract recovered were subjected to fractionation. The complete analysis reported 2217 non-redundant proteins present in the ureter protein. Moreover, ureter protein data were compared with urine, urinary exosome, and kidney databases. The result documented that 24.3 percent of the ureter proteins were found in the urine database reports in the past. The data also reported that 21 percent of ureter proteins were excreted as urinary exosomes. Confirming these proteins in urine helps in an accurate and supportive diagnosis of ureter diseases.

Conclusion:

To conclude, it was reported that over one‐third, or 33.8 percent of ureter proteomes, were found in urine as protein or polypeptides. The exact genesis of urinary proteins is still at its earliest stages. The complete picture of urine biomarkers can be illustrated when plasma proteins are also identified along with the signature proteins of the urogenital tract tissues.

Frequently Asked Questions

1.

What Does Proteomics Mean?

Proteomics is a branch of the study of the structure and function of various proteins. This study includes the way the proteins work and interact with other proteins inside the cells. Proteomics helps in determining the location, time, and rate of protein expression and protein interactions.

2.

How Is a Proteomic Analysis Performed?

The standard proteomic analysis includes the extraction of proteins, enzymatic digestion, separation, analysis of the peptides with tandem mass spectrometry, and database searching or quantification of software-based protein. Mass spectrometry is an effective method in proteome analysis.

3.

How Many Proteins Does a Proteome Contain?

Studies have shown that a proteome contains approximately 25,000 proteins or even more. Humans have approximately 25,000 genes. About 20,000 of these human genes are protein-coding genes. Hence, approximately 20,000 proteins are being produced in the human body.

4.

How Is Proteomics Measured?

Proteomics is the evaluation of the structure and function of the proteins. Proteomics is measured through gel-based methods, namely differential gel electrophoresis, followed by identification using mass spectrometry, which catalogs thousands of proteins in an average cell sample.

5.

What Are the Enzymes Used in Proteomics?

An enzyme called trypsin is commonly used in proteomics. Protease enzymes with complementary cleavage specificity have been used in special circumstances. The bottom-up proteomic approach includes the use of chemically modified trypsin, which cleaves peptide bonds selectively and converts them into lysine and arginine residues.

6.

What Is Structural Proteomics?

Structural proteomics is an application that helps identify the proteins in a protein complex or organelle, determines their location, and characterizes protein-protein interactions. It uses protein chemistry and modern mass spectrometric techniques to characterize the protein structures and assemblies.

7.

How Is a Proteome Affected?

The proteome is highly dynamic and is affected both by the genome and various external factors, such as the tissue type, the state of development, the metabolic state, and various interactions. The proteome actively changes in response to the developmental stage of the organism and its internal and external conditions.

8.

Where Is the Proteome Situated?

The proteome refers to the entire set of proteins that are expressed by a genome, tissue, cell, or organism at a certain period of time. It denotes the set of expressed proteins in a given type of cell at a given period of time under specific conditions. It also describes the assortment of proteins produced in a particular cell or tissue type.

9.

Why Is Proteome Larger?

The proteome appears bigger than the genome in eukaryotes because there are more proteins than genes. This is because of the alternative splicing of genes and post-translational modifications like phosphorylation or glycosylation. The proteome is larger than the number of genes due to alternative splicing followed by transcription.

10.

What Is the Role of Proteome?

The proteome refers to the entire set of proteins produced in an organism and encoded by the genome. It functions as the cell’s storehouse of proteins and comprises all the proteins present in a cell. The study of proteomics has various applications in the field of medicine, oncology, agriculture, and food microbiology.

11.

What Are the Techniques Applied in Proteomics?

The techniques such as matrix-assisted laser desorption or ionization and electrospray ionization. Both these techniques represent soft-ionization techniques in which low internal energies are used to create ions. Matrix-assisted laser desorption or ionization is the most powerful technique in proteomics.

12.

What Are the Approaches to Proteomics?

There are three main approaches to proteomic analysis to identify a biomarker of the disease. It includes the extraction and separation of proteins, identification of proteins, and verification of proteins. Proteomic approaches help understand the disease and its related mechanisms. 

13.

What Are the Limitations Associated With Proteomics?

The limitations associated with proteomics include a lack of standardization in processing a sample, complexity in analysis, risk of false positivity, and dynamic range of samples, which limits the estimation of proteins in low abundance, and failure in validating biomarkers in large numbers of proteins.
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Dr. Samer Sameer Juma Ali Altawil
Dr. Samer Sameer Juma Ali Altawil

Urology

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