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Updated: Aug 8, 2026

Long-term Intravital Immunofluorescence Imaging of Tissue Matrix Components with Epifluorescence and Two-photon Microscopy
Published on: April 22, 2014
Fibroblast matrix and surface components that mediate cell-to-cell interaction with lymphocytes
Insights
Lymphocytes (T and B cells) strongly adhere to human fibroblasts and their components in vitro. This interaction involves fibronectin and potentially other fibroblast surface molecules, suggesting complex adhesion mechanisms.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Lymphocyte-fibroblast interactions are crucial in various physiological and pathological processes.
- Understanding these interactions requires detailed analysis of adhesion molecules and mechanisms.
Purpose of the Study:
- To quantitatively assess the in vitro binding of T and B lymphocytes to human dermal fibroblasts.
- To identify specific fibroblast components and molecules involved in lymphocyte adhesion.
Main Methods:
- Quantitative ELISA assay on microtiter plates.
- Use of anti-Thy-1 and anti-IgM antibodies for T and B cell binding measurement.
- Testing binding to intact fibroblasts, plasma membranes, extracellular matrix extracts, and fibronectin-coated surfaces.
Main Results:
- Both T and B lymphocytes adhered strongly to intact fibroblasts, fibroblast membranes, and extracellular matrix extracts.
- Attachment occurred on fibronectin-coated surfaces, but not on collagens or fixed fibroblasts.
- Lymphocyte binding was partially inhibited by antibodies against fibroblast MHC class II antigens.
Conclusions:
- Lymphocyte adhesion to fibroblasts involves fibronectin and potentially other unidentified fibroblast surface molecules.
- The interaction is complex, with multiple adhesion pathways likely contributing to lymphocyte binding.
Abstract:
The interaction between lymphocytes and fibroblasts in vitro has been examined using a quantitative ELISA assay to measure the binding of T and B cells to monolayer cultures of human dermal fibroblasts. This was carried out on microtiter culture plates, using an anti-Thy-1 monoclonal antibody, to determine the attachment of murine T lymphocytes and an affinity-purified polyclonal anti-IgM antibody to measure B cell binding. Both types of lymphocyte were found to adhere strongly to intact human fibroblasts, and also had high levels of attachment to purified fibroblast plasma membranes and extracts of the fibroblast extracellular matrix. Attachment, particularly of B lymphocytes, also took place onto plastic surfaces coated with fibronectin, but not to collagens or to intact fibroblasts that had been fixed with a low concentration of paraformaldehyde. Lymphocyte binding to fibroblasts was partially prevented by a monoclonal antibody against fibroblast MHC class II antigens, but not against the class I membrane complex, or by polyclonal antiserum to the cell surface mannose 6-phosphate receptor. In addition, although both lymphocyte types were able to adhere to fibro-nectin, the presence of antibody against fibronectin or the synthetic peptide Arg-Gly-Asp-Ser, had no effect on their attachment to fibroblasts. Thus, lymphocyte adhesion may occur by fibronectin, but other types of interactions with fibroblasts also appear to take place.
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