Biomedical subjects
C Whitaker
Publications and source records attributed to C Whitaker.
Preparation and characterization of a purified influenza virus neuraminidase vaccine.
Influenza virus neuraminidase (NA) has been shown to induce protective but infection-permissive immunity in experimental animals. Challenge infection following such immunization is attended by decreased viral replication and disease manifestations but is sufficient to provide antigenic stimulation and definitive immunity to the virus. The present report describes the preparation and characterization of a purified NA vaccine (NAV) used in Phase 1 (immunogenicity and toxicity) trials in humans. In essence, virion NA was isolated from detergent-disrupted virus by affinity chromatography on oxamic acid-agarose, treated with formalin and tested for its enzymatic activity and for its immunogenicity in Balb/c mice and New Zealand rabbits. The preparation was essentially free of viral hemagglutinin but contained residual NP and M1 proteins. Both dispersed and aggregated NA tetrameric heads were seen in electron micrographs. Enzymatic activity was preserved, and minimal immunogenic doses in mice and rabbits, respectively, were 3.7 and 0.027 micrograms per kg.
Management perspectives. As a nursing care coordinator, I have responsibilities to my director of nursing, my staff, and the patients on my unit.
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Successful change: renaissance without revolution.
Change does not have to be painful. In fact, with careful planning it can even be liberating, empowering, and fun. Creating a vision, establishing trust, and encouraging participation are all critical steps in the process of change. Additionally, understanding the organizational culture, effective communication and assessing readiness are necessary in managing the change process and setting the stage for success. A case presentation describing the development and implementation of a staff on-call program is presented to illustrate the important steps in planning for a successful change process.
M protein (M1) of influenza virus: antigenic analysis and intracellular localization with monoclonal antibodies.
A panel of 16 monoclonal antibodies recognizing M protein (M1) of influenza virus was generated. Competition analyses resulted in localization of 14 monoclonal antibodies to three antigenic sites. Three monoclonal antibodies localized to site 1B recognized a peptide synthesized to M1 (residues 220 to 236) with enzyme-linked immunosorbent assay titers equivalent to or greater than that seen with purified M1; therefore, site 1B is located near the C terminus of M1. Sites 2 and 3 localize to the N-terminal half of M1. Antigenic variation of M proteins was seen when the monoclonal antibodies were tested against 14 strains of type A influenza viruses. Several monoclonal antibodies showed specific recognition of A/PR/8/34 and A/USSR/90/77 M proteins and little or no reactivity for all other strains tested. Immunofluorescence analysis with the monoclonal antibodies showed migration of M protein to the nucleus during the replicative cycle and demonstrated association of M protein with actin filaments in the cytoplasm. Use of a vaccinia virus recombinant containing the M-protein gene demonstrated migration of M protein to the nucleus in the absence of synthesis of gene products from other influenza virus RNA segments.
Methods for microcarrier culture of bovine pulmonary artery endothelial cells avoiding the use of enzymes.
Enzymes situated along the luminal surface of pulmonary endothelial cells interact with circulating solutes, notably with vasoactive substances, to regulate the hormonal composition of systemic arterial blood. However, it is becoming clear that the range and complexity of reactions occurring at or near the surface of endothelial cells are greater than previously recognized. In addition, evidence indicates that the quality of cell cultures used to define specific endothelial functions must be carefully controlled, together with development of improved understanding of the effects of long-term culture on pulmonary endothelial cells. We have developed new techniques for the culture of pulmonary endothelial cells which avoid exposure to proteolytic enzymes at both the isolation step and during subculture. A combination of mechanical harvest and culture on microcarrier beads has provided a system for the long-term, large-scale culture of pulmonary endothelial cells, features which to a large extent determine the scope of biochemical studies which can be undertaken.
How do kinins affect vascular tone?
Because kinins affect vascular tone, it is assumed that kinins act directly on smooth muscle. However, a direct interaction is difficult to conceive. Vessels containing smooth muscle are lined by a continuous endothelium with tight junctions. In addition, kinins act on endothelial cells to cause the release of prostaglandin-related substances; possibly through receptors. Furthermore, endothelial cells have a great capacity for hydrolyzing kinins to inactive products. Hence, even invoking active transport, less than 1% of kinins might be expected to reach the first layer of smooth muscle cells. However, kinins may not act directly on smooth muscle as endothelial cells and smooth muscle cells form specialized cell contacts. Myoendothelial junctions occur, and we have shown, in pulmonary arterioles, that smooth muscle cells send large numbers of projections into the cytoplasm of the endothelial cells. In addition, smooth muscle cells attach directly to the abluminal surface of endothelial cells, as do pericytes. Thus, there is a morphologic basis by which kinins can affect tone of smooth muscle without acting directly on smooth muscle cells.
Isolation and culture of endothelial cells from the lungs of small animals.
Techniques are descirbed for the isolation and culture of endothelial cells from the lungs of small animals. The cells are collected by retrograde perfusion of blood-free lungs with buffered saline containing collagenase. The cells are characterized by light microscopy, electron microscopy of thin sections and surface replicas, and by the presence of angiotensin-converting enzyme (ACE). ACE was assayed using 3H-benzoyl-Phe-Ala-Pro as substrate and was localized by indirect immunofluorescence using guinea pig endothelial cells incubated with rabbit antibodies to guinea pig lung ACE followed by goat anti-rabbit globulins conjugated to fluorescein. Thus, endothelial cultures can be established using small animals commonly employed in studies of pulmonary processing of vasoactive substances.
Localization of angiotensin converting enzyme (kininase II). II. Immunocytochemistry and immunofluorescence.
The cellular and subcellular sites of angiotensin converting enzyme (kininase II) in lung tissue and endothelial cells in culture were examined by immunocytochemical and immunofluorescence techniques. Converting enzyme is capable of inactivating bradykinin and of converting angiotensin I to its potent lower homolog, angiotensin II. Immunocytochemistry at the electron microscope level used goat anti- (pig lung and angiotensin converting enzyme) coupled to 11-MP (11-microperoxidase) via glutaraldehyde or to 8-MP (8-microperoxidase) via a bifunctional active ester, bis-succinyl succinate. The latter conjugate, which does not contain complex polymers, has been characterized in detail in terms of immunoreactivity and peroxidase activity.
Subcellular localization of pulmonary antiotensin-converting enzyme (kininase II).
Goat antibodies to pig lung angiotensin-converting enzyme (kininase II) were conjugated to microperoxidase. Rat lung tissue, previously incubated with non-immune goat serum, was incubated with the antibody-microperoxidase conjugate and then with H2O2 and 3,3-diaminobenzidine. Electron microscopy revealed reaction product on the plasma membrane and caveolae of endothelial cells, especially those of capillaries and venules. These results support the hypothesis that angiotensin I and bradykinin are metabolized by enzymes on the luminal surface of pulmonary endothelial cells.
Problems of the beginning family therapist.
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Asymptomatic goiter as an expression of a rare disease.
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Serial impasses in marriage.
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Serous cystadenofibroma arising in an ectopic ovary.
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