L. Minchevanilsson et al., ACTIVATED HUMAN GAMMA-DELTA T-LYMPHOCYTES EXPRESS FUNCTIONAL LACTOFERRIN RECEPTORS, Scandinavian journal of immunology, 46(6), 1997, pp. 609-618
Lactoferrin (Lf) an iron-binding protein in milk, mucosal secretions a
nd neutrophil granules has bactericidal properties and is a source of
iron for breast-fed infants. In this paper the authors show that most
in vivo activated lymphocytes, i.e. freshly isolated lymphocytes from
first trimester human decidua, and most in vitro activated human blood
lymphocytes, express lactoferrin receptors (Lf-R), while unstimulated
blood lymphocytes do not. All major lymphocyte subsets, i.e. alpha be
ta T cells, gamma delta T cells, CD8(+) T cells, CD4(+) T cells, B cel
ls and NK cells, express Lf-R after activation. The proportion of Lf-R
expressing activated gamma delta T cells is significantly larger than
that of activated alpha beta T cells. Lf-R and transferrin receptors
(Tr-R/CD71) show the same kinetics of appearance on activated blood ly
mphocytes and are, to a large extent, expressed on the same cells. How
ever, 35% of decidual lymphocytes and 15% of activated blood lymphocyt
es express Lf-R only. Addition of Lf to cultures containing an optimal
concentration of Tr augments the proliferative response to polyclonal
T cell activators and alloantigens, suggesting that presently used st
andard culture conditions for in vitro activation are suboptimal in pa
rticular for gamma delta T cells. Lf-R on decidual lymphocytes contain
bound Lf, which probably is produced locally. The results suggest tha
t Lf is a growth-supporting factor, especially important in local immu
ne responses in the mucosa.