Expression of collagen biosynthetic activities in lymphocytic cells.

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Abstract
Immunoglobulin-producing [mouse myeloma] Merwin plasma cells, MPC-11, contained prolyl hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase EC 1.14.11.2) activity and its crossreacting protein, as well as hydroxyproline and a collagenous protein that could not be classified as type I, II or III collagen. Friend leukemic cells contained only prolyl hydroxylase. Thymus-derived (T) lymphocytes and bone-marrow-derived (B) lymphocytes freshly isolated from BALB/c mice expressed low but significant prolyl hydroxylase activity. Upon stimulation with phytohemagglutinin, the enzyme activity in T cells increased 22- to 29-fold. Crossreacting protein was also increased and appeared more stable than the prolyl hydroxylase. The effect of lipopolysaccharide stimulation on B cells was similar but not as pronounced. Even when not accompanied by other collagen biosyntehtic activities, prolyl hydroxylase is present in all cells of hematologic origin.