N-linked glycosylation plays an essential role in the stability and function of tissue-nonspecific alkaline phosphatase.

ABSTRACT: Tissue-nonspecific alkaline phosphatase (TNALP) is a membrane-anchored glycoprotein with five N-linked glycosylation sites (N140, N230, N271, N303, N430) that is crucial for bone mineralization. TNALP is released into the bloodstream, serving as a biomarker for bone and mineral disorders. This study explores the role of N-linked glycosylation in the secretion, enzymatic activity, stability, and structure of TNALP. To eliminate the N-linked glycosylation site specifically, a soluble TNALP expression construct was created with the following substitution mutations N140Q, N230Q, N271Q, N303Q and N430D, and expressed in mouse osteoblasts. The effect of glycosylation was also studied by computational modeling (molecular dynamics simulations and the GlycoSHIELD tool). We observed that substitutin

SUBMITTER: Atanasova D 

PROVIDER: S-EPMC12861225 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature