Intrabodies against the Polysialyltransferases ST8SiaII and ST8SiaIV inhibit Polysialylation of NCAM in rhabdomyosarcoma tumor cells.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractPolysialic acid (polySia) is a carbohydrate modification of the neural cell adhesion molecule (NCAM), which is implicated in neural differentiation and plays an important role in tumor development and metastasis. Polysialylation of NCAM is mediated by two Golgi-resident polysialyltransferases (polyST) ST8SiaII and ST8SiaIV. Intracellular antibodies (intrabodies; IB) expressed inside the ER and retaining proteins passing the ER such as cell surface receptors or secretory proteins provide an efficient means of protein knockdown. To inhibit the function of ST8SiaII and ST8SiaIV specific ER IBs were generated starting from two corresponding hybridoma clones. Both IBs αST8SiaII-IB and αST8SiaIV-IB were constructed in the scFv format and their functions characterized in vitro and in vivo.
CitationIntrabodies against the Polysialyltransferases ST8SiaII and ST8SiaIV inhibit Polysialylation of NCAM in rhabdomyosarcoma tumor cells. 2017, 17 (1):42 BMC Biotechnol.
AffiliationHelmholtz Centr for infection research
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
- Enzyme-dependent variations in the polysialylation of the neural cell adhesion molecule (NCAM) in vivo.
- Authors: Galuska SP, Geyer R, Gerardy-Schahn R, Mühlenhoff M, Geyer H
- Issue date: 2008 Jan 4
- Impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid synthesis during postnatal mouse brain development.
- Authors: Oltmann-Norden I, Galuska SP, Hildebrandt H, Geyer R, Gerardy-Schahn R, Geyer H, Mühlenhoff M
- Issue date: 2008 Jan 18
- Molecular defects that cause loss of polysialic acid in the complementation group 2A10.
- Authors: Windfuhr M, Manegold A, Muhlenhoff M, Eckhardt M, Gerardy-Schahn R
- Issue date: 2000 Oct 20
- The polysialyltransferases interact with sequences in two domains of the neural cell adhesion molecule to allow its polysialylation.
- Authors: Thompson MG, Foley DA, Colley KJ
- Issue date: 2013 Mar 8
- Polysialic acid profiles of mice expressing variant allelic combinations of the polysialyltransferases ST8SiaII and ST8SiaIV.
- Authors: Galuska SP, Oltmann-Norden I, Geyer H, Weinhold B, Kuchelmeister K, Hildebrandt H, Gerardy-Schahn R, Geyer R, Mühlenhoff M
- Issue date: 2006 Oct 20