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Biomedical subjects

W L West

Publications and source records attributed to W L West.

14 recordsLinked to original sources
PubMed1992

Ten milestone issues in AOTA history.

This paper identifies 10 professional questions that the author has labeled milestone issues in the history of the American Occupational Therapy Association. Subjects encompassed by these issues are medical control, certified occupational therapy assistants, licensure, proficiency testing, entry-level degrees, treatment media, maintenance of competency, whether occupational therapists serve patients or clients, professional autonomy, and the status of occupational therapy as a profession. Although this paper is primarily a factual record of events and discussions referenced in official publications, the reader will recognize the insertion of author commentary and opinion in several of the issues discussed.

History, 20th Century↗
PubMed1986

Calmodulin and alpha tocopherol as additional binding sites for doxorubicin.

The hydrophobic probes anthroylcholine (9AC), 8-anilino-1-napthalene sulfonate (ANSE), and 2-P-toluidinyl naphthalene 6-sulfonate (TNS) increased calcium-calmodulin (Ca2+-aM) fluorescence. This fluorescence was decreased by doxorubicin (DXR) in a dose-dependent fashion. The Ca2+ ion was an absolute requirement for the observed effects of DXR. DXR bound to the Ca2+-CaM complex (Kd = 4.2 X 10(-5) M, Bmax = 1.8) and to alpha tocopherol. The binding of untransformed (native) DXR to CaM was a reversible process. These data support a previous finding that DXR inhibits stimulation of calmodulin-deficient PDE (a CaM target enzyme) using either the Ca2+ CaM complex or alpha tocopherol by interacting with these agents, and suggest that other target enzymes for CaM may be similarly affected.

Antibiotics, Antineoplastic↗
PubMed1979

Specific inhibition of a calcium dependent activation of brain cyclic AMP phosphodiesterase activity by vinblastine.

Vinblastine selectively inhibits the activation of brain cyclic AMP phosphodiesterase activity by Ca++-protein activator (50% inhibition by 2 x 10(-5) M). This inhibitory effect was reversed by excessive amounts of the activator, whereas large quantities of Ca++ caused only a slight suppression of the vinblastine effect. This result of vinblastine suggests a new site of its action and also suggests the possible role of protein activator, phosphodiesterase proteins or cyclic nucleotides in the previously known effects of vinblastine in vivo and in vitro.

3',5'-Cyclic-AMP Phosphodiesterases↗