Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

Carl Michael Carlsson; Per Bengtson; Helena Cucak; Hakon Leffler

doi:10.1074/jbc.M113.487793

Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

Carl Michael Carlsson, Per Bengtson, Helena Cucak, Hakon Leffler

Glycomics Program

21 Citationer (Scopus)

Abstract

Background: Transferrin has two N-glycans but their biological function remains unknown. Results: About 5% of human serotransferrin glycoforms bind galectin-3 and are targeted to a different endocytic pathway. Conclusion: Transferrin glycosylation may mediate a previously unrecognized level of physiological regulation. Significance: This is the first evidence that different molecular forms of transferrin, besides iron loading, may have different cellular function.

Originalsprog	Engelsk
Tidsskrift	The Journal of Biological Chemistry
ISSN	0021-9258
DOI	https://doi.org/10.1074/jbc.M113.487793
Status	Udgivet - 27 sep. 2013

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title = "Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms",

abstract = "Background: Transferrin has two N-glycans but their biological function remains unknown. Results: About 5% of human serotransferrin glycoforms bind galectin-3 and are targeted to a different endocytic pathway. Conclusion: Transferrin glycosylation may mediate a previously unrecognized level of physiological regulation. Significance: This is the first evidence that different molecular forms of transferrin, besides iron loading, may have different cellular function.",

author = "Carlsson, {Carl Michael} and Per Bengtson and Helena Cucak and Hakon Leffler",

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doi = "10.1074/jbc.M113.487793",

language = "English",

journal = "Journal of Biological Chemistry",

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T1 - Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

AU - Carlsson, Carl Michael

AU - Bengtson, Per

AU - Cucak, Helena

AU - Leffler, Hakon

PY - 2013/9/27

Y1 - 2013/9/27

N2 - Background: Transferrin has two N-glycans but their biological function remains unknown. Results: About 5% of human serotransferrin glycoforms bind galectin-3 and are targeted to a different endocytic pathway. Conclusion: Transferrin glycosylation may mediate a previously unrecognized level of physiological regulation. Significance: This is the first evidence that different molecular forms of transferrin, besides iron loading, may have different cellular function.

AB - Background: Transferrin has two N-glycans but their biological function remains unknown. Results: About 5% of human serotransferrin glycoforms bind galectin-3 and are targeted to a different endocytic pathway. Conclusion: Transferrin glycosylation may mediate a previously unrecognized level of physiological regulation. Significance: This is the first evidence that different molecular forms of transferrin, besides iron loading, may have different cellular function.

U2 - 10.1074/jbc.M113.487793

DO - 10.1074/jbc.M113.487793

M3 - Journal article

C2 - 23926108

SN - 0021-9258

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

ER -

Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

Abstract

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