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1.
Genomics ; 71(1): 89-100, 2001 Jan 01.
Article in English | MEDLINE | ID: mdl-11161801

ABSTRACT

Here we report the cloning and characterization of HIVEP3, the newest member in the human immunodeficiency virus type 1 enhancer-binding protein family that encodes large zinc finger proteins and regulates transcription via the kappaB enhancer motif. The largest open reading frame of HIVEP3 contains 2406 aa. and is approximately 80% identical to the mouse counterpart. The HIVEP3 gene is located in the chromosomal region 1p34 and is at least 300 kb with 10 exons. RNA studies show that multiple HIVEP3 transcripts are differentially expressed and regulated. Additionally, transcription termination occurs in the ultimate exon, exon 10, or in exon 6. Therefore, HIVEP3 may produce protein isoforms that contain or exclude the carboxyl DNA binding domain and the leucine zipper by alternative RNA splicing and differential polyadenylation. Sequence homologous to HIVEP3 exon 6 is not found in mouse nor are the paralogous genes HIVEP1 and HIVEP2. Zoo-blot analysis suggests that sequences homologous to the human exon 6 are present only in primates and cow. Therefore, a foreign DNA harboring a termination exon likely was inserted into the HIVEP3 locus relatively recently in evolution, resulting in the acquisition of novel gene regulatory mechanisms as well as the generation of structural and functional diversity.


Subject(s)
Carrier Proteins/chemistry , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/genetics , Amino Acid Sequence , Animals , Blotting, Northern , Blotting, Southern , Brain/metabolism , Carrier Proteins/genetics , Chromosomes, Human, Pair 1 , Cloning, Molecular , Cosmids , DNA, Complementary/metabolism , DNA-Binding Proteins/biosynthesis , Exons , Expressed Sequence Tags , Gene Library , Humans , Introns , Mice , Models, Genetic , Molecular Sequence Data , Oligonucleotide Probes/metabolism , Open Reading Frames , Phylogeny , Poly A/metabolism , Protein Isoforms , Protein Structure, Tertiary , Reverse Transcriptase Polymerase Chain Reaction , Sequence Homology, Amino Acid , Tissue Distribution , Transcription Factors , Transcription, Genetic , Zinc Fingers
2.
Public Health Nurs ; 8(2): 74-80, 1991 Jun.
Article in English | MEDLINE | ID: mdl-1924111

ABSTRACT

The sociology of knowledge provided the conceptual and methodologic basis for this study of the relationship between the philosophic concept of holism and the professionalization of public health nursing. Set in the context of the history of ideas, the discussion examines the various meanings of holism and the circumstances surrounding their adoption, modification, and use in public health nursing. The nursing literature from the late 1800s to the 1980s was analyzed to explicate the pragmatic consequences of holism for public health nursing, and to examine holism's moral value and its part in establishing and extending public health nursing's professional domain.


Subject(s)
Holistic Health , Professional Autonomy , Public Health Nursing/history , History, 19th Century , History, 20th Century , Humans , Public Health Nursing/education , Public Health Nursing/standards
4.
J Anim Sci ; 68(11): 3642-8, 1990 Nov.
Article in English | MEDLINE | ID: mdl-2262415

ABSTRACT

Sera obtained from pigs before and after subtherapeutic levels of ASP250 supplementation (pre and post serum pools) have been subjected to comparative fractionation by using gel filtration and affinity chromatography on immobilized Cibacron Blue F3G-A. Comparable serum fractions obtained from pre- and post-ASP250 blood sera were assayed in muscle cell culture bioassays designed to measure their effect on proliferation. Pre- and post-ASP250 sera were subjected to gel filtration and divided into the following fractions: fraction 1, Kav less than .17; fraction 2, Kav = .17 to .41; fraction 3, Kav = .41 to .59. Post-ASP250 fractions 2 and 3 increased proliferation rate in cultured muscle cells to a greater extent than comparable pre-ASP250 fractions (P less than .001). Chromatography of fraction 3 on immobilized Cibacron Blue F3G-A showed that both pre- and post-ASP250 fraction 3 contained a putative inhibitor of myogenic cell proliferation as well as mitogenic factors. However, negative growth factor activity was greater in pre-ASP250 fraction 3 than in post-ASP250 fraction 3 (P less than .05). Additionally, positive growth factor activity was lower in pre-ASP250 fraction 3 than in post-ASP250 fraction 3 (P less than .05). These data suggest that levels and(or) activities of both positive and negative muscle growth factors in serum may be altered by the addition of antimicrobials to the diets of growing pigs.


Subject(s)
Anti-Bacterial Agents/pharmacology , Muscles/cytology , Swine/growth & development , Animals , Anti-Bacterial Agents/blood , Cell Division/drug effects , Chlortetracycline/blood , Chlortetracycline/pharmacology , Clone Cells , Dose-Response Relationship, Drug , Electrophoresis, Polyacrylamide Gel , Male , Muscles/drug effects , Penicillins/blood , Penicillins/pharmacology , Sulfamethazine/blood , Sulfamethazine/pharmacology
5.
J Anim Sci ; 68(10): 3190-7, 1990 Oct.
Article in English | MEDLINE | ID: mdl-2254195

ABSTRACT

The effect of antimicrobial supplementation of pigs on the capacity of their sera to influence proliferation and protein turnover in cultured muscle cells was evaluated. Mitogenic activity of sera increased when pigs were fed ASP250 (P less than .005) or carbadox (P less than .001), whereas the mitogenic activity of serum from pigs receiving the basal diet remained unchanged (P = .5). Additionally, sera from ASP250-fed pigs significantly decreased (P less than .001) total cellular protein degradation compared with sera obtained from the same pigs prior to supplementation. Neither ASP250 nor carbadox stimulated proliferation of myogenic cells when added to the culture media. Inclusion of ASP250 in swine diets altered the composition of their sera in a way that stimulated muscle cell proliferation and reduced the rate of protein degradation in cultured myogenic cells. Likewise, the inclusion of carbadox in swine diets increased the ability of their sera to stimulate cultured muscle cell proliferation.


Subject(s)
Anti-Infective Agents/pharmacology , Blood Physiological Phenomena , Muscle Proteins/metabolism , Muscles/cytology , Swine/blood , Animals , Carbadox/pharmacology , Cell Division , Cell Line , Chlortetracycline/pharmacology , Dose-Response Relationship, Drug , Drug Combinations , Male , Penicillin G/pharmacology , Sulfamethazine/pharmacology
6.
J Nutr ; 110(1): 66-73, 1980 Jan.
Article in English | MEDLINE | ID: mdl-6766501

ABSTRACT

The effects of dietary vitamin E-depletion and repletion on the cyclooxygenase activity was studied in the semitendinosus muscle of rabbits. The prostaglandin (PG) cyclooxygenase system in rabbit semitendinosus muscle was characterized and found to depend on reduced glutathione and 1-epinephrine as cofactors. Skeletal muscle cyclooxygenase generates PGE2 and PGF2 alpha at a ratio approximately equal to one. Weanling New Zealand white rabbits were fed a vitamin E-deficient diet for 4 to 5 weeks. Controls received 50 mg dl-alpha-tocopherol acetate twice weekly. Vitamin E deficiency caused a significant reduction in cyclooxygenase activity but did not change the PGE2/PGF2 alpha ratio. Oral supplementation of tocopherol acetate promptly returned the cyclooxygenase activity back to the control values within 48 hours. The decreased cyclooxygenase activity explains in part the increased level of arachidonic acid in skeletal muscle phospholipid previously reported in this laboratory. The possible involvement of decreased prostaglandin endoperoxides with platelet aggregation in vitamin E deficiency is discussed.


Subject(s)
Muscles/enzymology , Prostaglandin-Endoperoxide Synthases/metabolism , Prostaglandins/biosynthesis , Vitamin E Deficiency/metabolism , Vitamin E/pharmacology , Animals , Kinetics , Male , Microsomes/metabolism , Muscles/drug effects , Oxygenases/metabolism , Prostaglandins E/biosynthesis , Prostaglandins F/biosynthesis , Rabbits , Vitamin E Deficiency/enzymology
7.
J Nutr ; 110(1): 74-81, 1980 Jan.
Article in English | MEDLINE | ID: mdl-7354387

ABSTRACT

The key enzyme controlling prostaglandin (PG) catabolism, 15-hydroxyprostaglandin dehydrogenase (PGDH), was characterized in rabbit tissues. The apparent Michaelis constant (Km) using PGE2 as substrate was found to be 5.3, 4.0, 4.0 and 7.1 microM for semitendinosus and soleus muscles, heart and kidney, respectively. The effect of dietary vitamin E depletion and repletion on the PGDH activity in these tissues was studied. Vitamin E deficiency caused an elevation of PGDH activity in rabbit skeletal muscles but not in the heart and kidney. Oral supplementation of tocopherol acetate to the deficient animals did not affect the skeletal muscle PGDH activity. A long period of refeeding (30 days) was required to suppress the elevated PGDH level to the control values. The data indicates a higher turnover of the PGs in the vitamin E-deficient rabbit skeletal muscles. The significance of such a change in connection to prostaglandin metabolism is discussed.


Subject(s)
Hydroxyprostaglandin Dehydrogenases/metabolism , Kidney/enzymology , Muscles/enzymology , Myocardium/enzymology , Vitamin E Deficiency/enzymology , Vitamin E/pharmacology , Animals , Kinetics , Male , Organ Specificity , Prostaglandins E , Rabbits , Species Specificity
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