During cutaneous tissue organization, numerous critical interactions occur between cells and the extracellular matrix (ECM). Cell-matrix interactions depend on the presence of ECM receptors. Many ECM receptors, known as
integrins, are heterodimeric
glycoproteins consisting of
one alpha and one beta chain.
Integrins containing beta 1 or beta 3 chains are ECM receptors, whereas those containing beta 2 chains are leukocyte cell-cell receptors. We have used porcine cutaneous
wounds as a paradigm for tissue organization and probed healing
wounds and adjacent normal skin with polyclonal
antibodies to
fibronectin and
fibronectin (alpha 5 beta 1) receptor. During re-epithelialization, the epidermis transits over a provisional matrix containing
fibronectin. Migrating epidermal cells expressed
fibronectin receptors in a bright linear peripheral pattern.
At 10 days, when reepithelialization was complete and the basement membrane was re-established, the
fibronectin matrix was markedly reduced and
fibronectin-receptor expression was limited to the basolateral aspect of basal cells, as observed in normal epidermis. Beneath the migrating epidermis in 5-d
wounds, granulation tissue had filled 80% of the
wound space. Day-5
wound fibroblasts did not express
fibronectin nor other beta 1
integrin receptors, were randomly oriented, and contained no actin bundles.
Fibronectin fibrils were assembled on the surfaces of day-5
wound fibroblasts but formed few linkages between cells. Day-7
wound fibroblasts expressed
fibronectin receptors, contained peripheral cytoplasmic actin bundles consistent with a contractile fibroblast phenotype, and were coaligned across the
wound in parallel array with interconnecting
fibronectin fibrils. The
wounds contracted between 7 and 10 days. Thus the migrating epidermis consistently expressed
fibronectin receptors.
Fibronectin receptors were expressed by fibroblasts just prior to
wound contraction.