|Title||Expression of collagen biosynthetic activities in lymphocytic cells.|
|Publication Type||Journal Article|
|Year of Publication||1978|
|Authors||Chen-Kiang S, Cardinale GJ, Udenfriend S|
|Journal||Proc Natl Acad Sci U S A|
|Date Published||1978 Mar|
|Keywords||Animals, Cell Line, Collagen, Cross Reactions, Friend murine leukemia virus, Humans, Leukemia, Experimental, Lymphocyte Activation, Lymphocytes, Mice, Multiple Myeloma, Neoplasms, Experimental, Procollagen-Proline Dioxygenase|
Immunoglobulin-producing Merwin plasma cells, MPC-11, have been found to contain proplyl hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase; EC 126.96.36.199) 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.
|Alternate Journal||Proc Natl Acad Sci U S A|
|PubMed Central ID||PMC411475|
Selina Chen-Kiang, Ph.D.