title: Mast cells express functional CD30 ligand and are the predominant CD30L-positive cells in Hodgkin's disease.
abstract: Hodgkin's disease (HD) tumours are characterized by the presence of few tumour cells, the Hodgkin and Reed-Sternberg (HRS) cells, surrounded by a large amount of non-neoplastic cells. The role of this cell infiltrate for the development of HD is not known. CD30, belonging to the tumour necrosis factor receptor superfamily, is highly expressed on HRS cells and believed to be involved in tumourigenesis and tumour progression. Tumour samples from 42 patients were immunohistochemically double-stained for tryptase, a mast cell-specific proteinase and CD30 ligand (CD30L). Tryptase-positive mast cells were present in all tumours. Of these cells, 50% expressed CD30L and 66% of the CD30L-positive cells were mast cells. CD30L mRNA in in vitro developed normal mast cells and malignant human and murine mast cell lines was detected using reverse transcription polymerase chain reaction. CD30L protein expressed on human mast cells was detected using flow cytometry. In a co-culture assay, the human mast cell line HMC-1 stimulated thymidine uptake in HRS cell lines, and the stimulation could be blocked using CD30L-specific monoclonal antibodies. In conclusion, mast cells are present in HD tumours and are the predominant CD30L-expressing cells. CD30L-CD30 interaction is a pathway by which mast cells may stimulate DNA synthesis in HRS cells.
authors.affiliation: Department of Genetics and Pathology, Uppsala University, University Hospital, Uppsala, Sweden.
authors.forename: D
authors.initials: D
authors.lastname: Molin
authors.forename: M
authors.initials: M
authors.lastname: Fischer
authors.forename: Z
authors.initials: Z
authors.lastname: Xiang
authors.forename: U
authors.initials: U
authors.lastname: Larsson
authors.forename: I
authors.initials: I
authors.lastname: Harvima
authors.forename: P
authors.initials: P
authors.lastname: Venge
authors.forename: K
authors.initials: K
authors.lastname: Nilsson
authors.forename: C
authors.initials: C
authors.lastname: Sundström
authors.forename: G
authors.initials: G
authors.lastname: Enblad
authors.forename: G
authors.initials: G
authors.lastname: Nilsson
mesh_terms: D000328:Adult; D000818:Animals; D015415:Biomarkers / Q000032:analysis; D053285:CD30 Ligand; D002455:Cell Division; D002460:Cell Line; D018920:Coculture Techniques; D005260:Female; D005434:Flow Cytometry; D006689:Hodgkin Disease / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D017730:Ki-1 Antigen / Q000378:metabolism; D008297:Male; D008407:Mast Cells / Q000201:enzymology / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000032:analysis* / Q000235:genetics; D051379:Mice; D012333:RNA, Messenger / Q000032:analysis; D016539:Reed-Sternberg Cells / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012697:Serine Endopeptidases / Q000032:analysis; D013936:Thymidine / Q000378:metabolism; D053802:Tryptases; D014407:Tumor Cells, Cultured
chemical_list: D015415:Biomarkers; D053285:CD30 Ligand; D017730:Ki-1 Antigen; D008562:Membrane Glycoproteins; D012333:RNA, Messenger; C505774:TNFSF8 protein, human; C505775:Tnfsf8 protein, mouse; C509190:Tpsb2 protein, mouse; D012697:Serine Endopeptidases; C509222:Tpsab1 protein, mouse; D053802:Tryptases; D013936:Thymidine