Biomedical subjects
Publications and source records attributed to E F Johnson.
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A program of cooperative education between LeMoyne-Owen College and the University of Tennessee Center for the Health Sciences (UTCHS) was designed to attract students from the undergraduate institution to the various health professional schools at UTCHS. The program was initiated by a black faculty member at UTCHS. It involved a faculty exchange between the two institutions and the implementation of several changes in the pre-health science curriculum at the undergraduate institution. Other components of the program included: the gift of equipment and supplies to LeMoyne-Owen College by UTCHS; counseling of LeMoyne-Owen students by UTCHS faculty members; the generation of private funds by the faculty and staff at UTCHS for the support of LeMoyne-Owen students participating in the cooperative education program; and broad exposure of LeMoyne-Owen students to the laboratories and clinical facilities at UTCHS.
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Black, poor, aged, and female patients are more susceptible to having to face problems of loneliness and stress, feelings offailure, sagging egos, and other psychological and emotional difficulties. Relief of these feelings is often found through artificial supports such as over-the-counter drugs. Because of the easy accessibility of such drugs as sleeping pills, weight control pills, and vitamins, an individual could have a bottle of almost any drug medication advertised in the media without physician supervision. Ignorance of the cumulative impact of mixing medications often leads to habit-forming results and significant side effects.A major step toward prevention of drug abuse is to know that someone cares and will reach out to patients before the problem drives them to seek relief from over-the-counter medications and drugs. A second major step is education about the hazards of mixing medicines without physician supervision.
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Two forms of cytochrome P-450 with different substrate specificities were isolated from liver microsomes of rabbits treated with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). A specific antibody was produced toward the major form of the cytochrome. The antibody inhibits microsomal acetanilide hydroxylation (80%). It does not cross-react with the minor fraction of the cytochrome or inhibit the hydroxylation of 3,4-benzpyrene or coumarin, the N-demethylation of aminopyrine or the O-deethylation of 7-ethoxycoumarin catalyzed by rabbit liver microsomes. The major form has an estimated Mr = 54,000 and displays an n-octylamine difference spectrum with an absorption maximum at 426 nm and a minimum at 391 nm. When reconstituted, this cytochrome catalyzes acetanilide hydroxylation at a higher rate than microsomes or the minor fraction. The n-octylamine difference spectrum of the minor fraction displays an absorption maximum at 431 nm and a minimum at 410 nm. When reconstituted, this fraction catalyzes the hydroxylation of 3,4-benzpyrene and the O-deethylation of 7-ethoxycoumarin. The two cytochromes appear to be distinct entities and function in different catalytic pathways.
In this update we provide a list of the 71 P450 genes and the four P450 pseudogenes that have been characterized as of September 30, 1988. The chromosomal locations of many of these genes are also summarized. A modest revision of the initially proposed nomenclature of the P450 superfamily (Nebert et al., DNA 6, 1-11, 1987) is described specifically for the human and mouse chromosomal loci. The motivation for this revision is to conform to the rules of nomenclature for human and mouse genes. Recommendations for the naming of chromosomal loci include the root symbol "CYP" for human ("Cyp" for mouse), denoting "cytochrome P450." We recommend that this root also be used for other organisms. For a chromosomal locus, the root symbol is followed by an Arabic numeral designating the P450 family, a letter indicating the subfamily, and an Arabic numeral representing the individual gene within the family or subfamily. Numbers of the individual genes usually will be assigned in the order the genes are identified. This system is consistent with our earlier proposed nomenclature for P450 families and gene products from all eukaryotes and prokaryotes.
We provide here a list of 154 P450 genes and seven putative pseudogenes that have been characterized as of October 20, 1990. These genes have been described in a total of 23 eukaryotes (including nine mammalian and one plant species) and six prokaryotes. Of 27 gene families so far described, 10 exist in all mammals. These 10 families comprise 18 subfamilies, of which 16 and 14 have been mapped in the human and mouse genomes, respectively; to date, each subfamily appears to represent a cluster of tightly linked genes. We propose here a modest revision of the initially proposed (Nebert et al., DNA 6, 1-11, 1987) and updated (Nebert et al., DNA 8, 1-13, 1989) nomenclature system based on evolution of the superfamily. For the gene we recommend that the italicized root symbol CYP for human (Cyp for mouse), representing cytochrome P450, be followed by an Arabic number denoting the family, a letter designating the subfamily (when two or more exist), and an Arabic numeral representing the individual gene within the subfamily. A hyphen should precede the final number in mouse genes. We suggest that the human nomenclature system be used for other species. This system is consistent with our earlier proposed nomenclature for P450 of all eukaryotes and prokaryotes, except that we are discouraging the future use of cumbersome Roman numerals.
We studied the distribution of the peripheral nerves innervating the distal forepaw by recording receptive fields from fascicles of the ulnar, radial, and median nerves and compared this result with the peripheral nerve representation in primary somatosensory (SI) cortex of cat. Our findings suggest that SI cortex receives input, in large part, from multiple peripheral nerves even when those nerves do not show a strong overlapping pattern in the periphery. This overlap pattern observed in SI cortex may be responsible, in part, for the immediate reorganization which is known to follow peripheral nerve deafferentation.
Large, independent variations occur among New Zealand White rabbits in the 21- and and 6 beta-hydroxylation of progesterone as catalysed by liver microsomes. These reactions are catalysed respectively by two electrophoretically distinct types of rabbit-liver microsomal cytochrome P-450, 1 and 3b, as judged by their catalytic efficiency and the capacity of specific monoclonal antibodies to extensively inhibit the respective microsomal hydroxylases. The relatively large variations in progesterone 6 beta-hydroxylase activity do not appear to be associated with differences in microsomal content of cytochrome P-450 3b, whereas differences in the microsomal concentration of cytochrome P-450 1 may underlie variations in 21-hydroxylase activity. Preparations of cytochrome P-450 3b contain at least two catalytically distinct subforms, one of which catalyses both 6 beta- and 16 alpha-hydroxylation of progesterone with a low Km while the other subform catalyses predominantly 16 alpha-hydroxylation with a significantly greater Km. The two catalytic subforms of cytochrome P-450 3b can be independently modulated in vitro by positive and negative effectors that can arise in vivo from the metabolism of progesterone. The 6 beta-hydroxylase subform of cytochrome P-450 3b is not expressed in a genetically defined strain of rabbits, IIIVO/J, indicating a heritable basis for the differential expression of the two subforms of cytochrome P-450 3b. These results indicate that the extent of cytochrome P-450 multiplicity may be greater than is evident from the isolation of electrophoretically distinct forms of cytochrome P-450, and that small differences in structure may underlie large differences in catalytic properties. It is not known whether the differences among outbred New Zealand White rabbits in the expression of either cytochrome P-450 1 or the subforms of cytochrome P-450 3b reflect regulatory phenomena or genetic polymorphism.
Cytochromes P450 (CYPs) play an important role in the oxidative metabolism of xenobiotics. Three-dimensional structures of CYPs are needed to study structure-function relationships in their molecules and interaction with partner proteins. Experimental determination of eucaryotic CYPs 3D structures is difficult because of hydrophobic membrane anchors and surface hydrophobic regions that prevent their crystallization. Replacement of surface hydrophobic amino acids by hydrophilic residues without any changes in protein structure and function can help to solve this problem. Such modification can be proposed using the analysis of 3D model of protein. In this work computer aided 3D structure of microsomal P450 2B4 (CYP2B4) was modeled for the further prediction of surface mutations for hydrophilization of the protein surface. The model of 3D structure of CYP2B4 was constructed by homology with CYP2C5 Model optimization was made by energy minimization and molecular dynamics simulation of protein molecule in water environment. The model was verified by using special statistic software and by comparison with the experimental data on the substrate recognition site, redox-partner binding sites and chemical modification of the protein surface.
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