Methods of modulating functions of polypeptide GalNAc-transferases and of screening test substances to find agents herefor, pharmaceutical compositions comprising such agents and the use of such agents for preparing medicaments
US7338932B2 · kind B2 · utility
Assignee
Inventors
Key dates
| Filing date | Nov 12, 2002 |
| Grant date | Mar 4, 2008 |
| Priority date | — |
| Expiry date | Oct 27, 2024 |
Classification
- Technology area (CPC G)Physics
- CPC primaryG01N2500/10
- WIPO fieldPharmaceuticals
- WIPO sectorChemistry
Abstract
Attachment of O-glycans to proteins is controlled by a large family of homologous polypeptide GalNAc-transferases. Polypeptide GalNAc-transferases contain a C-terminal sequence with similarity to lectins. This invention discloses that the putative lectin domains of GalNAc-transferase isoforms, GalNAc-T4, -T7, -T2, and -T3, are functional and recognize carbohydrates, glycopeptides, and peptides and discloses the lectin domains of GalNAc-T1-T16. These lectin domains have different binding specificities and modulate the functions of GalNAc-transferase isoforms differently. Novel methods for identification of inhibitors or modulators of binding activities mediated by lectin domains of polypeptide GalNAc-transferases are disclosed. Direct binding activity of GalNAc-transferase lectins has been demonstrated for the first time and methods to measure lectin mediated binding of isolated lectins or enzymes with lectin domains are disclosed. The present invention specifically discloses a novel selective inhibitor of polypeptide GalNAc-transferase lectin domains, which provides a major advancement in that this inhibitor and related inhibitors sharing common characteristics of activity bind lec…
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.