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Soluble CD30 receptor from Hodgkin cells stimulates granulocytes to release angiogenic interleukin‐8

Hodgkin lymphoma is a malignancy where the malignant Hodgkin and Reed‐Sternberg (H‐RS) cells typically depend on the cross‐talk with normal bystander cells of the innate and adaptive immune system. CD30, a receptor of the tumor necrosis factor receptor superfamily is strongly overexpressed on H‐RS cells. However, the corresponding ligand (CD153) is membrane‐anchored and mainly expressed on bystander cells distant from the CD30 positive tumor cells. CD30 is released by metalloproteinase cleavage. Here, we tested whether the soluble ectodomain of CD30 (sCD30), instead of the receptor, is able to communicate with distant granulocytes. We showed that metalloproteinase‐dependent CD30 shedding from H‐RS cells is stimulated upon growth factor reduction and heat‐shock. Soluble CD30, released in the microenvironment, is initially multimerized. This form stimulated distant granulocytes by reverse signaling to release interleukin‐8 (IL‐8) which is involved in angiogenesis and metastasis. This finding suggests that malignant H‐RS cells might use receptor shedding not only to compete a cross‐talk but also manipulate distant cells in a trans‐signaling manner to generate survival factor.