O‐glycosylation of the non‐canonical T‐cadherin from rabbit skeletal muscle by single mannose residues. Issue 22 (7th October 2013)
- Record Type:
- Journal Article
- Title:
- O‐glycosylation of the non‐canonical T‐cadherin from rabbit skeletal muscle by single mannose residues. Issue 22 (7th October 2013)
- Main Title:
- O‐glycosylation of the non‐canonical T‐cadherin from rabbit skeletal muscle by single mannose residues
- Authors:
- Winterhalter, Patrick R.
Lommel, Mark
Ruppert, Thomas
Strahl, Sabine - Abstract:
- Abstract : O ‐mannosylation is a vital protein modification. In humans, defective O ‐mannosylation of α‐dystroglycan results in severe congenital muscular dystrophies. However, other proteins bearing this modification in vivo are still largely unknown. Here, we describe a highly reliable method combining glycosidase treatment with LC–MS analyses to identify mammalian O ‐mannosylated proteins from tissue sources. Our workflow identified T‐cadherin (H‐cadherin, CDH13) as a novel O ‐mannosylated protein. In contrast to known O ‐mannosylated proteins, single mannose residues (Man‐α‐Ser/Thr) are attached to this cell adhesion molecule. Conserved O ‐glycosylation sites in T‐, E‐ and N‐cadherins from different species, point to a general role of O ‐mannosyl glycans for cadherin function. Abstract : New workflow to detect O ‐mannosyl glycans from native tissue sources. Use of specific enzymes to discriminate sugar isomers with mass spectrometry. Identification of T‐cadherin (CDH13) as novel mammalian O ‐mannosylated protein. T‐cadherin is the first protein characterized with single O ‐linked mannose residues. O ‐mannosylation of diverse cadherin family members is suggested.
- Is Part Of:
- FEBS letters. Volume 587:Issue 22(2013)
- Journal:
- FEBS letters
- Issue:
- Volume 587:Issue 22(2013)
- Issue Display:
- Volume 587, Issue 22 (2013)
- Year:
- 2013
- Volume:
- 587
- Issue:
- 22
- Issue Sort Value:
- 2013-0587-0022-0000
- Page Start:
- 3715
- Page End:
- 3721
- Publication Date:
- 2013-10-07
- Subjects:
- T-cad -- T-cadherin -- CID -- collision-induced dissociation -- ConA -- concanavalin A -- α-DG -- α-dystroglycan -- EC -- extracellular cadherin -- ER -- endoplasmic reticulum -- GPI -- glycosylphosphatidylinositol -- LC–MS -- liquid chromatography–mass spectrometry -- POMT -- protein O-mannosyltransferase -- XIC -- extracted ion chromatogram -- T-cadherin -- H-cadherin -- CDH13 -- O-mannosylation -- Glycosylation -- Mass spectrometry
Biochemistry -- Periodicals
Biophysics -- Periodicals
Molecular biology -- Periodicals
Biochimie -- Périodiques
Biochemistry
Biophysics
Molecular biology
Periodicals
572.05 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00145793 ↗
http://febs.onlinelibrary.wiley.com/hub/journal/10.1002/(ISSN)1873-3468/ ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.febslet.2013.09.041 ↗
- Languages:
- English
- ISSNs:
- 0014-5793
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3901.600000
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