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Kaji Lab
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A lab that uses mass spectrometry to study proteins carrying glycans.

AboutAbout the lab
Reading how glycans attach to proteins using mass spectrometry
Project Professor Hiroyuki Kaji of the Glycan Big Data Center studies glycoproteomics, which uses mass spectrometry to analyze glycans attached to proteins.
Glycosylation is one of the post-translational modifications of proteins, and in a paper he states that many challenges remain to be solved in its analysis.
He has published papers on developing analysis software for studying how glycans are attached and on comparing glycans across tissues.
He is also a co-author of a paper from Japan's Human Glycome Atlas Project.
Key terms
- Glycoproteomics
- A research field that studies glycans attached to proteins, including which protein and which site they are attached to
- Mass spectrometry
- A method that precisely measures the mass of molecules to determine the type and structure of substances
- Post-translational modification
- A chemical change a protein undergoes after it is made. Glycan attachment is one of them
ResearchResearch themes
Project Professor Hiroyuki Kaji studies methods for analyzing glycan-bearing proteins by mass spectrometry, and software for that analysis. His papers also cover an analysis comparing how glycans are attached across tissues, and a summary of the challenges in identifying glycoproteins based on MS2.
*Illustrative imageGlycopeptide detection method and analysis software
The lab has developed a method called Glyco-RIDGE, which finds glycan-bearing peptides from their mass and chromatographic properties, and GRable, software that carries out this process semi-automatically.
*Illustrative imageDifferences in glycans across tissues
By comparing how glycans are attached to glycoproteins in mouse liver, kidney, spleen, pancreas, stomach, and testis, the lab examines how glycans differ between tissues.
*Illustrative imageChallenges in glycoprotein identification and how to complement them
The lab summarizes the technical challenges of glycoprotein identification based on MS2 in mass spectrometry, and presents efforts to complement them in Japan's Human Glycome Atlas Project.
MembersFaculty
- Project ProfessorHiroyuki Kaji
VoicesStudent voices
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “Secondary Ion Mass Spectrometer (SIMS) Tube - DPLA - 2a22bbd17e faf628d93a557 (page 4)” Honig, Richard E. (Richard Edward) / CC BY 4.0 (cropped)
- Glycopeptide detection method and analysis software: “Mass-spectrometer awi hg” Hannes Grobe / CC BY-SA 2.5 (cropped)
- Differences in glycans across tissues: “TMEM171 Structure Model” Bauma319 / CC BY-SA 4.0 (cropped)
- Challenges in glycoprotein identification and how to complement them: “Ion mobility-mass spectrometry workflow” Remilawal / CC BY-SA 4.0 (cropped)
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