Successful Isolation of Specific Organ Secreted Proteins In Vivo... "Utilized for Disease Diagnosis and Treatment"

Professor Seojaemyung from KAIST and Collaborative Research Team Develop Tissue-Specific Secreted Protein Labeling Technique

[Asia Economy Reporter Kim Bong-su] A technology has been developed that can isolate and identify proteins secreted by specific tissues within the body for use in disease diagnosis and treatment.

The Korea Advanced Institute of Science and Technology (KAIST) announced on the 13th that a research team led by Professor Jae-myung Seo of the Graduate School of Medical Science and Engineering, in collaboration with Professor Hyun-woo Lee of the Department of Chemistry at Seoul National University and Professor Jong-seo Kim of the Department of Life Sciences at Seoul National University, developed a tissue-specific secreted protein labeling technique in vivo.

The joint research team developed a method using proximity labeling enzymes to isolate proteins secreted by specific tissues in the plasma of mice. This in vivo labeling technique is expected to overcome the limitations of previous in vitro cell line experiments and be applied to the discovery of disease-related biomarkers and therapeutic targets.

This study was published online on the 1st in the international journal Nature Communications.

Secreted proteins are key factors that mediate signal transmission between cells and tissues, regulating physiological functions. They are also used as major targets for disease therapeutics, making secreted protein research biologically and medically significant. Until now, most secreted protein studies have analyzed conditioned media from cell line cultures, but in vitro cell culture is well known to have limitations in fully reflecting the physiological environment in vivo.

To overcome this, it is necessary to study proteins secreted by specific tissues into the bloodstream in vivo. However, since thousands of proteins are mixed in the blood, a technique to isolate proteins secreted by specific tissues is required.

To solve this problem, the research team used proximity labeling enzymes to biotin-label secreted proteins passing through the lumen of the endoplasmic reticulum. The labeled proteins could be easily detected or isolated using streptavidin. After delivering this enzyme to the liver of mice and administering biotin, only liver-derived secreted proteins were detected in the plasma of the mice. It was confirmed that liver-derived secreted proteins in vivo were distinctly different from those secreted by liver cell lines cultured in vitro.

To validate this technique in a disease model, it was applied to an insulin resistance mouse model, successfully detecting proteins reported to be associated with insulin resistance. It is expected that this technique can be applied to various tissues in vivo or combined with disease models to detect proteins related to disease progression.

The research team stated, "Proteins secreted by the liver in vivo were significantly different from those observed in cell lines, demonstrating the limitations of previous secreted protein studies using cell lines and highlighting the distinctiveness of this new technique that overcomes those limitations." They added, "This method can be utilized to discover biomarkers and therapeutic targets that more accurately reflect physiological states in vivo."

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