Structural and functional characterization of human kallistatin

Stephanie T.D. Pham, Kristian W. Nielsen, Jonas H. Graversen, Nanna Kristensen, Lasse B. Steffensen, Andrea R. Lundgaard, José L. Martín-Ventura, Peter Højrup, Yaseelan Palarasah · 2026

Read Structural and functional characterization of human kallistatin by Stephanie T.D. Pham, Kristian W. Nielsen, Jonas H. Graversen, Nanna Kristensen, Lasse B. Steffensen, Andrea R. Lundgaard, José L. Martín-Ventura, Peter Højrup, Yaseelan Palarasah (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13251767.txt.

Description

Stephanie T.D. Pham and colleagues characterize human kallistatin, a blood protein that restrains an enzyme involved in blood vessel control, in a 2026 study. Kallistatin belongs to the serpin family, whose members can link into inactive chains called polymers. Its sugar decorations, tissue locations, and tendency to polymerize were poorly mapped before this work.

The team built custom antibodies and a sensitive test that measures kallistatin in plasma and in fluid from cultured tissue, including vessel tissue from patients with aortic aneurysm. Mass spectrometry confirmed a predicted sugar attachment site on the protein. Experiments showed kallistatin does polymerize, and that stripping its sugars sharply increased polymer formation, meaning the sugars act as stabilizers. Polymerized kallistatin lost its ability to block its target enzyme, while sugar-stripped protein still worked. The authors say the tools and maps they built open the way to studying this protein in disease.

Catalog record

CREATORStephanie T.D. Pham, Kristian W. Nielsen, Jonas H. Graversen, Nanna Kristensen, Lasse B. Steffensen, Andrea R. Lundgaard, José L. Martín-Ventura, Peter Højrup, Yaseelan Palarasah
YEAR2026
COLLECTIONPAPERS
FORMATTXT
FILE SIZE54 KB
VERSION1.0
LICENSECC BY 4.0
RIGHTSCC BY
SOURCEEurope PMC

Source: https://europepmc.org/articles/PMC13251767

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