Panic disorder: the great mimic.
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Anxiety Disorders↗
Biomedical subjects
M Quillen
Publications and source records attributed to M Quillen.
Cell surface tubulin in leukemic cells: molecular structure, surface binding, turnover, cell cycle expression, and origin.
We report here new characteristics of cell surface tubulin from a human leukemia cell line. These cells (CEM cells) possess tubulin that is readily iodinated on the surface of living cells, turns over at a rate identical to that of other surface proteins, and is present throughout the cell cycle. When removed with trypsin, it rapidly returns to the surface. Peptide mapping of iodinated surface tubulin indicates that it possesses a similar, but not identical, primary structure to total CEM and rat brain tubulin. Living CEM cells are able to bind specifically a subfraction of CEM tubulin from metabolically labeled high speed supernatants of lysed CEM cells. Surface tubulin is more basic than the total tubulin pool. The binding, which is saturable, is inhibited by unlabeled CEM high speed supernatants but not by excess thrice-cycled rat or bovine brain tubulin. Surface tubulin is also shown to bind to living nontransformed normal rat kidney cells but not to normal, circulating, mononuclear white cells. Activated lymphocytes produce a tubulin that binds to CEM cells. Since CEM tubulin was detected in the media of 6-h cultures of CEM cells, we must conclude that at least some of the surface tubulin comes from the media. We further conclude that these leukemic cells produce an unusual tubulin that may bind specifically to any membrane. The presence of iodinatable surface tubulin, however, appears to require both the production of a unique tubulin and the presence of a "receptor-like" surface binding component.
Animals↗
Tubulin as a major cell surface protein in human lymphoid cells of leukemic origin.
Surface-exposed proteins of vinblastine-sensitive human lymphoid cell line of leukemic origin (CCRF-CEM) were examined by the lactoperoxidase-catalyzed iodination and two-dimensional polyacrylamide gel electrophoresis methods. Spots which comigrate with bovine brain tubulin and rabbit muscle actin were prominently labeled in the whole membrane but not in the high-speed supernatant fraction of the disrupted cells. Mild trypsinization of labeled cells removed the iodinated tubulin and actin without significantly affecting the protein staining pattern. Iodination of normal human lymphocytes resulted in no labeling of the tubulin or actin. The presence of surface-exposed tubulin in this leukemic cell line suggests a possible mechanism for their enhanced sensitivity to the cytotoxic action of vinblastine.
Cell Line↗