Galectin-3 acts as a matricellular protein (2004)
- Authors:
- USP affiliated authors: SANTOS, MARINILCE FAGUNDES DOS - ICB ; CHAMMAS, ROGER - FM ; BRENTANI, MARIA MITZI - FM
- Unidades: ICB; FM
- Assunto: HISTOLOGIA
- Language: Inglês
- Abstract: Expression of galectin-3, a ?-galactoside binding lectin, is associated with sarcoma tumor progression and metastasis. Intracellular galectin-3 may play a role in cell survival, conferring resistance to anoikis. However, galectin-3 is also secreted and may play a role in cell:matrix interactions in a carbohydrate dependent way. Here we present evidence that galectin-3 acts as a matricellular protein, modulating integrin function. Upon transfection with EJ-ras, murine fibroblasts shifted from a stationary to a more migratory phenotype associated with an increase in both ?6?1 integrin and galectin-3 expression. Galectin-3 was found in the leading edge of migrating cells, colocalizing with polyllactosamine containing glycoconjugates. Transformed cells displayed galectin-3 on the cell surface, as determined by flow cytometric analysis. The haptotatic response of transformed cells to laminin, which was mediated by ?6?1 integrins, was inhibitable by lactose, suggesting a role for galectins in cell migration. We further evaluated the migratory response of cells derived from galectin-3 null mice. Embryonic mesenchymal cells from both wildtype and galectin-3 null mice were analyzed regarding both integrin expression and the migratory response to laminin. Despite having similar amounts of ?6?1 integrins on the cell surface, galectin-3 null cells were less migratory than control cells. We have also established cell lines from methylcholantrene-inducedsarcomas from both wild type and galectin-3 null mice. In this system, galectin-3 null cells were also less migratory than control cells in laminin. ) Finally, when galectin-3 was transiently expressed in galectin-3 null sarcoma cells, it inhibited cell adhesion to laminin and stimulated the migratory response to laminin. Mechanistically, extracellular galectin-3 disrupted the focal adhesion plaque, as defined by the loss of phosphorylated FAK in the ventral surface of migrating cells. Although it is clear that the ?6?1 integrin is the actual mediator of fibroblast migration towards laminin, galectin-3 acts as a positive modulator of this process. Supported by FAPESP (97/13100-9 and 99/13013-4) and TWAS
- Imprenta:
- Source:
- Título do periódico: Abstracts
- Conference titles: Congress of the Brazilian Society for Cell Biology
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ABNT
MELO, F. H. M. et al. Galectin-3 acts as a matricellular protein. 2004, Anais.. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo, 2004. . Acesso em: 19 abr. 2024. -
APA
Melo, F. H. M., Junqueira, M. S., Brentani, M. M., Santos, M. F. dos, Hsu, D. K., Liu, F. T., & Chammas, R. (2004). Galectin-3 acts as a matricellular protein. In Abstracts. Campinas: Instituto de Ciências Biomédicas, Universidade de São Paulo. -
NLM
Melo FHM, Junqueira MS, Brentani MM, Santos MF dos, Hsu DK, Liu FT, Chammas R. Galectin-3 acts as a matricellular protein. Abstracts. 2004 ;[citado 2024 abr. 19 ] -
Vancouver
Melo FHM, Junqueira MS, Brentani MM, Santos MF dos, Hsu DK, Liu FT, Chammas R. Galectin-3 acts as a matricellular protein. Abstracts. 2004 ;[citado 2024 abr. 19 ] - Involvement of galectin-3 in dysfunctional migration of fibroblasts on laminin-1
- Galectin-3 modulates dysfunctional migration of fibroblasts on laminin-1 surfaces
- Extracellular galectin-3 modulates dysfunctional migration of fibroblasts on laminin-1 surfaces
- Extracellular galectin-3 disrupts focal adhesion plaques and induces dysfunctional migration of fibroblasts of laminin-1
- Galectin-3 modulates the migratory response of fibroblasts to laminin: a possible function of galectin-3 in sarcoma tumor progression
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