Galectin-3 endocytosis by carbohydrate independent and dependent pathways in different macrophage like cell types.
(2012) In Biochimica et Biophysica Acta - General Subjects 1820(7). p.804-818- Abstract
- BACKGROUND: Galectin-3 (the Mac-2 antigen) is abundantly expressed in both macrophage like cells and certain non-macrophage cells. We have studied endocytosis of galectin-3 as one important step relevant for its function, and compared it between variants of a macrophage like cell line, and non-macrophage cells.
METHODS: Endocytosis of galectin-3 was observed by fluorescence microscopy and measured by flow cytometry. The endocytosis mechanism was analysed using galectin-3 mutants, galectin-3 inhibitors and endocytic pathways inhibitors in the human leukaemia THP-1 cell line differentiated into naïve (M0), classical (M1) or alternatively activated (M2) macrophage like cells, and the non-macrophage cell lines HFL-1... (More) - BACKGROUND: Galectin-3 (the Mac-2 antigen) is abundantly expressed in both macrophage like cells and certain non-macrophage cells. We have studied endocytosis of galectin-3 as one important step relevant for its function, and compared it between variants of a macrophage like cell line, and non-macrophage cells.
METHODS: Endocytosis of galectin-3 was observed by fluorescence microscopy and measured by flow cytometry. The endocytosis mechanism was analysed using galectin-3 mutants, galectin-3 inhibitors and endocytic pathways inhibitors in the human leukaemia THP-1 cell line differentiated into naïve (M0), classical (M1) or alternatively activated (M2) macrophage like cells, and the non-macrophage cell lines HFL-1 fibroblasts and SKBR3 breast carcinoma.
RESULTS: Galectin-3 endocytosis in non-macrophage cells and M2 cells was blocked by lactose and a potent galectin-3 inhibitor TD139, and also by the R186S mutation in the galectin-3 carbohydrate recognition domain (CRD). In M1 cells galectin-3 endocytosis could be inhibited only by chlorpromazine and by interference with the non-CRD N-terminal part of galectin-3. In all the cell types galectin-3 entered early endosomes within 5-10min, to be subsequently targeted mainly to non-degradative vesicles, where it remained even after 24h.
CONCLUSIONS: Galectin-3 endocytosis in M1 cells is receptor mediated and carbohydrate independent, while in M2 cells it is CRD mediated, although the non-CRD galectin-3 domain is also involved. General significance The demonstration that galectin-3 endocytosis in M1 macrophages is carbohydrate independent and different from M2 macrophages and non-macrophage cells, suggests novel, immunologically significant interactions between phagocytic cells, galectin-3 and its ligands. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2431447
- author
- Lepur, Adriana LU ; Carlsson, Michael C. LU ; Novak, Ruđer ; Dumić, Jerka ; Nilsson, Ulf J. LU and Leffler, Hakon LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Endocytosis, Galectin-3, M1 macrophages, M2 macrophages, THP-1 cell line
- in
- Biochimica et Biophysica Acta - General Subjects
- volume
- 1820
- issue
- 7
- pages
- 15 pages
- publisher
- Elsevier
- external identifiers
-
- wos:000305366100003
- pmid:22450157
- scopus:84860675027
- pmid:22450157
- ISSN
- 0304-4165
- DOI
- 10.1016/j.bbagen.2012.02.018
- language
- English
- LU publication?
- yes
- id
- f63aac35-6350-4bf7-866a-e224429f2246 (old id 2431447)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/22450157?dopt=Abstract
- date added to LUP
- 2016-04-04 09:35:37
- date last changed
- 2023-05-15 08:24:15
@article{f63aac35-6350-4bf7-866a-e224429f2246,
abstract = {{BACKGROUND: Galectin-3 (the Mac-2 antigen) is abundantly expressed in both macrophage like cells and certain non-macrophage cells. We have studied endocytosis of galectin-3 as one important step relevant for its function, and compared it between variants of a macrophage like cell line, and non-macrophage cells. <br/><br>
<br/><br>
METHODS: Endocytosis of galectin-3 was observed by fluorescence microscopy and measured by flow cytometry. The endocytosis mechanism was analysed using galectin-3 mutants, galectin-3 inhibitors and endocytic pathways inhibitors in the human leukaemia THP-1 cell line differentiated into naïve (M0), classical (M1) or alternatively activated (M2) macrophage like cells, and the non-macrophage cell lines HFL-1 fibroblasts and SKBR3 breast carcinoma. <br/><br>
<br/><br>
RESULTS: Galectin-3 endocytosis in non-macrophage cells and M2 cells was blocked by lactose and a potent galectin-3 inhibitor TD139, and also by the R186S mutation in the galectin-3 carbohydrate recognition domain (CRD). In M1 cells galectin-3 endocytosis could be inhibited only by chlorpromazine and by interference with the non-CRD N-terminal part of galectin-3. In all the cell types galectin-3 entered early endosomes within 5-10min, to be subsequently targeted mainly to non-degradative vesicles, where it remained even after 24h. <br/><br>
<br/><br>
CONCLUSIONS: Galectin-3 endocytosis in M1 cells is receptor mediated and carbohydrate independent, while in M2 cells it is CRD mediated, although the non-CRD galectin-3 domain is also involved. General significance The demonstration that galectin-3 endocytosis in M1 macrophages is carbohydrate independent and different from M2 macrophages and non-macrophage cells, suggests novel, immunologically significant interactions between phagocytic cells, galectin-3 and its ligands.}},
author = {{Lepur, Adriana and Carlsson, Michael C. and Novak, Ruđer and Dumić, Jerka and Nilsson, Ulf J. and Leffler, Hakon}},
issn = {{0304-4165}},
keywords = {{Endocytosis; Galectin-3; M1 macrophages; M2 macrophages; THP-1 cell line}},
language = {{eng}},
number = {{7}},
pages = {{804--818}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta - General Subjects}},
title = {{Galectin-3 endocytosis by carbohydrate independent and dependent pathways in different macrophage like cell types.}},
url = {{http://dx.doi.org/10.1016/j.bbagen.2012.02.018}},
doi = {{10.1016/j.bbagen.2012.02.018}},
volume = {{1820}},
year = {{2012}},
}