Specific Activity: >300 pmol/min/μg (human ortholog; mouse activity inferred similarly) .
Assay Protocol:
Galnt1 initiates O-glycosylation, a modification linked to cellular adhesion, signaling, and cancer progression.
Substrate Specificity: Targets peptides such as MUC1, MUC5AC, and MUC7 .
Hierarchy: Acts as an "early transferase" for nonglycosylated or monoglycosylated substrates .
A study in hepatocellular carcinoma (HCC) revealed:
| Observation | Mechanism | Outcome |
|---|---|---|
| GALNT1 Overexpression | Enhanced EGFR activation via reduced O-glycosylation | Increased cell migration/invasion |
| GALNT1 Knockdown | Delayed EGFR degradation; increased co-localization with lysosomes (LAMP1) | Suppressed migration/invasion |
| EGFR Signaling | Downregulation of p-Y1068 (activated EGFR) and accelerated degradation | Reduced tumor aggressiveness |
GALNT1 knockdown in HCC cells (e.g., HA22T, PLC5) reduced EGF-induced migration by >50% .
EGFR degradation rate increased 2–3-fold in GALNT1-deficient cells .
Recombinant Mouse Polypeptide N-acetylgalactosaminyltransferase 1 (Galnt1) catalyzes the initial step in O-linked oligosaccharide biosynthesis: the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It exhibits broad substrate specificity, acting on various peptides including EA2, Muc5AC, Muc1a, Muc1b, and Muc7.