Recombinant Human
Lysyl Oxidase-like 2 Secreted from
Human Embryonic Kidney Cells Displays Complex and Acidic Glycans at
All Three N-Linked Glycosylation Sites
Version 2 2018-04-13, 20:09
Version 1 2018-04-13, 20:06
Posted on 2018-04-13 - 20:09
Human
lysyl oxidase-like 2 (hLOXL2), a glycoprotein implicated
in tumor progression and organ fibrosis, is a molecular target for
anticancer and antifibrosis treatment. This glycoprotein contains
three predicted N-linked glycosylation sites; one
is near the protein’s active site, and at least one more is
known to facilitate the protein’s secretion. Because the glycosylation
impacts the protein’s biology, we sought to characterize the
native, mammalian glycosylation profile and to determine how closely
this profile is recapitulated when the protein is expressed in insect
cells. All three glycosylation sites on the protein, expressed in
human embryonic kidney (HEK) cells, were characterized individually
using a mass spectrometry-based glycopeptide analysis workflow. These
data were compared to the glycosylation profile of the same protein
expressed in insect cells. We found that the producer cell type imparts
a substantial influence on the glycosylation of this important protein.
The more-relevant version, expressed in HEK cells, contains large,
acidic glycoforms; these glycans are not generated in insect cells.
The glycosylation differences likely have structural and functional
consequences, and these data should be considered when generating
protein for functional studies or for high-throughput screening campaigns.
CITE THIS COLLECTION
DataCite
3 Biotech
3D Printing in Medicine
3D Research
3D-Printed Materials and Systems
4OR
AAPG Bulletin
AAPS Open
AAPS PharmSciTech
Abhandlungen aus dem Mathematischen Seminar der Universität Hamburg
ABI Technik (German)
Academic Medicine
Academic Pediatrics
Academic Psychiatry
Academic Questions
Academy of Management Discoveries
Academy of Management Journal
Academy of Management Learning and Education
Academy of Management Perspectives
Academy of Management Proceedings
Academy of Management Review
Go, Eden P.; Moon, Hee-Jung; Mure, Minae; Desaire, Heather (2018). Recombinant Human
Lysyl Oxidase-like 2 Secreted from
Human Embryonic Kidney Cells Displays Complex and Acidic Glycans at
All Three N-Linked Glycosylation Sites. ACS Publications. Collection. https://doi.org/10.1021/acs.jproteome.7b00849
or
Select your citation style and then place your mouse over the citation text to select it.
SHARE
Usage metrics
AUTHORS (4)
EG
Eden P. Go
HM
Hee-Jung Moon
MM
Minae Mure
HD
Heather Desaire
KEYWORDS
producer cell typehigh-throughput screening campaignsproteinglycosylation sitesglycosylation profileinsect cellsmass spectrometry-based glycopeptide analysis workflowGlycosylation Sites Human lysyl oxidase-like 2HEKRecombinant Human Lysyl Oxidase-like 2 SecretedHuman Embryonic Kidney Cells Displays Complex