The fibrinogen C-terminal domain is seldom C-mannosylated but its C-mannosylation is important for the secretion of microfibril-associated glycoprotein 4.
C-mannosylation
Fibrinogen C-terminal domain
Glycosylation
Microfibril-associated glycoprotein 4
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
07
10
2019
revised:
13
05
2020
accepted:
16
05
2020
pubmed:
23
5
2020
medline:
15
12
2020
entrez:
23
5
2020
Statut:
ppublish
Résumé
C-mannosylation is the one of glycosylations. Microfibril-associated glycoprotein 4 (MFAP4), an important protein for tissue homeostasis and cell adhesion, contains a consensus sequence of C-mannosylation in its fibrinogen C-terminal domain. In this study, we sought to demonstrate that fibrinogen C-terminal domain is a new substrate domain for C-mannosylation. We established an MFAP4-overexpresssing HT1080 cell line and purified recombinant MFAP4 protein from the conditioned medium for LC-MS/MS analysis. Subcellular localization of MFAP4 was observed under confocal fluorescence microscope. We found that MFAP4 is C-mannosylated at Trp Our results demonstrate that the fibrinogen C-terminal domain is a novel C-mannosylation domain and that the C-mannosylation of MFAP4 is important for its secretion. These results suggest that C-mannosylation has a role for dominant effect for MFAP4 secretion.
Sections du résumé
BACKGROUND
C-mannosylation is the one of glycosylations. Microfibril-associated glycoprotein 4 (MFAP4), an important protein for tissue homeostasis and cell adhesion, contains a consensus sequence of C-mannosylation in its fibrinogen C-terminal domain. In this study, we sought to demonstrate that fibrinogen C-terminal domain is a new substrate domain for C-mannosylation.
METHODS
We established an MFAP4-overexpresssing HT1080 cell line and purified recombinant MFAP4 protein from the conditioned medium for LC-MS/MS analysis. Subcellular localization of MFAP4 was observed under confocal fluorescence microscope.
RESULTS
We found that MFAP4 is C-mannosylated at Trp
CONCLUSIONS
Our results demonstrate that the fibrinogen C-terminal domain is a novel C-mannosylation domain and that the C-mannosylation of MFAP4 is important for its secretion.
GENERAL SIGNIFICANCE
These results suggest that C-mannosylation has a role for dominant effect for MFAP4 secretion.
Identifiants
pubmed: 32442478
pii: S0304-4165(20)30149-5
doi: 10.1016/j.bbagen.2020.129637
pii:
doi:
Substances chimiques
Carrier Proteins
0
Extracellular Matrix Proteins
0
Glycoproteins
0
MFAP4 protein, human
0
Fibrinogen
9001-32-5
Mannose
PHA4727WTP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
129637Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors have no conflict of interest to declare.