UNLABELLED: The integrin receptors are a family of transmembrane glycoproteins comprising non-covalent heterodimers. They interact with a wide variety of ligands including extracellular matrix glycoproteins, complement and other cells while their intracellular domains interact with the cytoskeleton. They participate in cell-matrix and cell-cell adhesion in many physiologically important processes including embryological development, hemostasis, thrombosis, wound healing, immune and nonimmune defense mechanisms, and oncogenic transformation. This investigation is focused on the histological distribution of the beta 1-integrins in the human thymus, using an indirect immunoperoxidase method. With the exception of VLA-4, none of the beta 1 integrins were expressed on thymocytes which were strongly positive in the cortex and perivascular compartment, somewhat weaker in the medulla. Thymic epithelial cells were positive for VLA-1, VLA-2, VLA-3 and VLA-6, but the distribution pattern of these molecules in epithelial cells at certain locations was quite different. VLA-1 was weakly expressed by both cortical and medullary epithelial cells. VLA-2 was strongly positive in cortical epithelial cells forming a dense framework at the peripheral cortex. VLA-3 and VLA-6 selectively stained a single flattened epithelial cell layer (perilobular epithelial cells) demarcating the peripheral cortex from the surrounding perivascular compartment. VLA-1,3,5,6 were also demonstrated in the endothelial cells and subendothelial layer of the thymic vasculature. IN CONCLUSION: the distribution of integrins in human thymus tissues is of special interest. Such distribution shows that the VLA integrins may have different functions in different areas. The data presented in this study may be important in evaluating the functional role of the VLA integrins in thymocyte maturation in different compartments of the thymus.
UNLABELLED: The integrin receptors are a family of transmembrane glycoproteins comprising non-covalent heterodimers. They interact with a wide variety of ligands including extracellular matrix glycoproteins, complement and other cells while their intracellular domains interact with the cytoskeleton. They participate in cell-matrix and cell-cell adhesion in many physiologically important processes including embryological development, hemostasis, thrombosis, wound healing, immune and nonimmune defense mechanisms, and oncogenic transformation. This investigation is focused on the histological distribution of the beta 1-integrins in the human thymus, using an indirect immunoperoxidase method. With the exception of VLA-4, none of the beta 1 integrins were expressed on thymocytes which were strongly positive in the cortex and perivascular compartment, somewhat weaker in the medulla. Thymic epithelial cells were positive for VLA-1, VLA-2, VLA-3 and VLA-6, but the distribution pattern of these molecules in epithelial cells at certain locations was quite different. VLA-1 was weakly expressed by both cortical and medullary epithelial cells. VLA-2 was strongly positive in cortical epithelial cells forming a dense framework at the peripheral cortex. VLA-3 and VLA-6 selectively stained a single flattened epithelial cell layer (perilobular epithelial cells) demarcating the peripheral cortex from the surrounding perivascular compartment. VLA-1,3,5,6 were also demonstrated in the endothelial cells and subendothelial layer of the thymic vasculature. IN CONCLUSION: the distribution of integrins in human thymus tissues is of special interest. Such distribution shows that the VLA integrins may have different functions in different areas. The data presented in this study may be important in evaluating the functional role of the VLA integrins in thymocyte maturation in different compartments of the thymus.