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Immunolocalization of integrin receptors in normal lymphoid tissues
MM Zutter
Department of Pathology, Washington University School of Medicine, St.
Louis, MO 63110.
The integrin superfamily of cell adhesion receptors consists of
heterodimeric glycoproteins composed of unique alpha and beta subunits.
These receptors mediate cell-substrate and cell-cell adhesive properties
for a variety of cell types. This investigation has focused on the
histologic distribution of the beta 1 subfamily of integrins within
lymphoid tissues including tonsil, lymph node, spleen, thymus, and
appendix. The dendritic cells of both follicular center and thymic origin
express the alpha 1, alpha 2, alpha 3, alpha 5, and alpha 6, as well as the
beta 1 integrin subunits. Most lymphoid cells in normal tissues do not
express the alpha 1, alpha 2, alpha 3, alpha 5, and alpha 6 subunits, or
the alpha v beta 3 integrin. The beta 1 subunit is expressed by all
lymphocytes but with variable intensity. Increased levels of the alpha 5
and beta 1 subunits are observed in the follicular light zone, suggesting a
role for these integrins in B-cell activation. Although the alpha 4 subunit
is expressed by all lymphoid cells, an increased expression of alpha 4 and
decreased expression of beta 1 by the mantle zone B-cell compartment is
noted in comparison with the decreased expression of alpha 4 and increased
expression of beta 1 by follicular center B-cells. These studies suggest
that alpha 4 may be paired with a beta subunit other than beta 1 on the
mantle zone lymphoid population. Thus, integrin expression by cells of
lymphoid tissues varies with location and function and differs
significantly from integrin expression observed on circulating and cultured
peripheral blood lymphocytes.
Volume 77,
Issue 10,
pp. 2231-2236,
05/15/1991
Copyright © 1991 by The American Society of Hematology
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