Further evidence of different lactoferrin and transferrin binding sites on human HT29-D4 cells. Effects of lysozyme, fucose and cathepsin G. Comparison with transferrin.
Biochim Biophys Acta
; 1224(3): 441-4, 1994 Dec 30.
Article
em En
| MEDLINE
| ID: mdl-7803501
ABSTRACT
We have defined by using competition experiments the nature of specific lactoferrin binding sites, probably responsible for the previously observed stimulatory growth effect of the iron binding protein on HT29-D4 cells. Lysozyme, albumin and fucose do not affect lactoferrin binding showing that the binding of the protein is mediated neither by electrostatic forces nor by fucose. Iron-free and iron-loaded protein produce similar effects, demonstrating that the metal is not involved in the protein recognition. Similar results are observed for transferrin. A specific binding inhibition of lactoferrin by cathepsin G, a leukocyte proteinase, is observed, suggesting the existence of a common receptor for lactoferrin and cathepsin G on HT29-D4 cells. These results and the fact that tumor tissues are more often infiltrated by inflammatory cells such as polymorphonuclear leukocytes could evoke an unexpected role for leukocytes, possibly mediated in part by these two proteins, on the proliferative cancer effect.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transferrina
/
Muramidase
/
Catepsinas
/
Fucose
/
Lactoferrina
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
França