The reed-sternberg cell/lymphocyte rosette. I. Properties of rosettes formed between hodgkin's cell lines and allogeneic lymphocytes

ABSTRACT The properties of rosettes formed between the Hodgkin's cell lines, L428 and L591, and allogeneic peripheral blood mononuclear cell populations have been investigated.

Immunocytochemical analysis showed that the majority of adherent cells were T-cells of both the CD4 and CD8 subsets. Only relatively few B-cells and monocytes were seen to adhere. However,

when peripheral blood mononuclear cell populations were fractionated, it was found that monocytes were as good as T-cells at forming rosettes with both L428 and L591, though B-cells were

shown to be poor at forming such associations. Treatment of both L428 and L591 with neuraminidase resulted in a significant reduction (P less than 0.01) in the mean number of adherent

lymphocytes and in the numbers of Hodgkin's tumour cells which formed rosettes. Smaller, less significant effects were observed for Cytochalasin B and trypsin. EDTA (10(-2) M) at pH 7.2

had no significant effect on rosetting for L428 or L591. Adherence of allogeneic lymphocytes to L428 or L591 was pH dependent but did not appear to correlate with cell surface charge.

Treatment of L428 cells with Fab fragments prepared from the IgG fraction of a hyperimmune rabbit anti-L428 antiserum, significantly (P less than 0.05) inhibited the adherence of allogeneic

lymphocytes, but only when used at high concentration. The binding requirements of the Hodgkin's cell lines with allogeneic peripheral blood lymphocytes, as described in this study,

appear to be quite different from those described for freshly isolated Hodgkin's tumour cells with autologous intratumoral lymphocytes. This suggests that the two phenomena may be

unrelated. There would appear to be an absolute requirement for cell surface sialic acid for allogeneic lymphocyte attachment to the HD cell lines. This might suggest that the

receptor-ligand system involved contains sialic acid as an integral part of the cell surface receptor structure involved in recognition of the appropriate ligand. Access through your

institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive 24 print

issues and online access $259.00 per year only $10.79 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to

local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT

BEING VIEWED BY OTHERS G PROTEIN COUPLED RECEPTOR TRANSCRIPTS IN HUMAN IMMUNE CELLS AND PLATELETS Article Open access 27 September 2024 IDENTIFICATION, SORTING AND PROFILING OF FUNCTIONAL

KILLER CELLS VIA THE CAPTURE OF FLUORESCENT TARGET-CELL LYSATE Article 31 August 2023 SERUM COMPONENTS INFLUENCE ANTIBODY REACTIVITY TO GLYCAN AND DNA ANTIGENS Article Open access 22 August

2023 AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * University Department of Pathology, Southampton General Hospital, UK DJ Flavell Authors * DJ Flavell View author publications You can also

search for this author inPubMed Google Scholar * DH Wright View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and

permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Flavell, D., Wright, D. The Reed-Sternberg cell/lymphocyte rosette. I. Properties of rosettes formed between Hodgkin's cell lines and

allogeneic lymphocytes. _Br J Cancer_ 59, 165–173 (1989). https://doi.org/10.1038/bjc.1989.35 Download citation * Issue Date: 01 February 1989 * DOI: https://doi.org/10.1038/bjc.1989.35

SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to

clipboard Provided by the Springer Nature SharedIt content-sharing initiative