Specific binding of placental acidic isoferritin to cells of the T‐cell line HD‐MAR

FEBS Letters

Konijn, A.M.¹  Meyron-Holtz, E.G.¹  Levy, R.¹  Ben-Bassat, H.¹  Matzner, Y.¹ 

[1] Department of Nutrition, The Hebrew University-Hadassah Medical School, Jerusalem, Israel

关键词: T-cell;    Ferritin;    Isoferritin;    Receptor;   

DOI  :  10.1016/0014-5793(90)81380-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Acidic placental isoferritin inhibited the blastogenic response of peripheral human lymphocytes to T-cell activating lectins. We measured specific binding of radioiodinated placental isoferritin to cells of the T-cell line HD-MAR and found specific high-affinity binding. Binding was faster and more ferritin was bound at 37°C than at 4°C. Displacement experiments indicated that most of the binding occurred at the cell surface. Acidic placental ferritin and isolated H-type ferritin subunits but not isolated L-type subunits, competed for the binding. Scatchard plot analysis showed characteristics of a single binding species with a dissociation constant (K _d) of 1.3–4.4 × 10⁻¹¹ M. The results suggest the presence of receptors for acidic isoferritin on T-lymphocytes and thus, a regulatory role for the acidic ferritin H-type subunit in T-cell function.

【 授权许可】

Unknown