| RRC ID |
82840
|
| Author |
Yamada K, Mukaimine A, Nakamura A, Kusakari Y, Pradipta AR, Chang TC, Tanaka K.
|
| Title |
Chemistry-driven translocation of glycosylated proteins in mice.
|
| Journal |
Nat Commun
|
| Abstract |
Cell surface glycans form various "glycan patterns" consisting of different types of glycan molecules, thus enabling strong and selective cell-to-cell recognition. We previously conjugated different N-glycans to human serum albumin to construct glycoalbumins mimicking natural glycan patterns that could selectively recognize target cells or control excretion pathways in mice. Here, we develop an innovative glycoalbumin capable of undergoing transformation and remodeling of its glycan pattern in vivo, which induces its translocation from the initial target to a second one. Replacing α(2,3)-sialylated N-glycans on glycoalbumin with galactosylated glycans induces the translocation of the glycoalbumin from blood or tumors to the intestine in mice. Such "in vivo glycan pattern remodeling" strategy can be used as a drug delivery system to promote excretion of a drug or medical radionuclide from the tumor after treatment, thereby preventing prolonged exposure leading to adverse effects. Alternatively, this study provides a potential strategy for using a single glycoalbumin for the simultaneous treatment of multiple diseases in a patient.
|
| Volume |
15(1)
|
| Pages |
7409
|
| Published |
2024-10-2
|
| DOI |
10.1038/s41467-024-51342-5
|
| PII |
10.1038/s41467-024-51342-5
|
| PMID |
39358337
|
| PMC |
PMC11446924
|
| MeSH |
Animals
Cell Line, Tumor
Drug Delivery Systems
Female
Glycated Serum Albumin
Glycosylation
Humans
Mice
Polysaccharides* / chemistry
Polysaccharides* / metabolism
Protein Transport
Serum Albumin / chemistry
Serum Albumin / metabolism
Serum Albumin, Human / chemistry
Serum Albumin, Human / metabolism
|
| IF |
12.121
|
| Resource |
| Human and Animal Cells |
Hep G2(RCB1648) |
