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 |
Volume | 75 |
Issue | 3 |
Pagination | 1379-83 |
Date Published | 1978 Mar |
ISSN | 0027-8424 |
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 |
Abstract | 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. |
DOI | 10.1073/pnas.75.3.1379 |
Alternate Journal | Proc Natl Acad Sci U S A |
PubMed ID | 206896 |
PubMed Central ID | PMC411475 |
Related Faculty:
Selina Chen-Kiang, Ph.D.