Expression of collagen biosynthetic activities in lymphocytic cells.
Immunoglobulin-producing Merwin plasma cells, MPC-11, have been found to contain proplyl 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, on the other hand, 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 uas similar but not as pronounced. Thus, even when not accompanied by other collagen biosynthetic activities, prolyl hydroxylase is present in all cells of hematologic origin.
D000818:Animals; D002460:Cell Line; D003094:Collagen / Q000096:biosynthesis*; D003429:Cross Reactions; D005622:Friend murine leukemia virus; D006801:Humans; D007942:Leukemia, Experimental / Q000378:metabolism; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000378:metabolism*; D051379:Mice; D009101:Multiple Myeloma / Q000378:metabolism; D009374:Neoplasms, Experimental / Q000378:metabolism; D011393:Procollagen-Proline Dioxygenase / Q000276:immunology / Q000378:metabolism*
D003094:Collagen; D011393:Procollagen-Proline Dioxygenase