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Biomedical subjects

J B Miller

Publications and source records attributed to J B Miller.

At least 91 records · Page 5Linked to original sources
PubMed1992

Comparison of single-dose antibiotic prophylaxis in uncomplicated transurethral resection of the prostate.

We evaluated the necessity for antibiotic prophylaxis in uncomplicated transurethral resection of the prostate. A total of 107 patients was entered into a double-blind, prospective, placebo-controlled, randomized trial. Only 7 patients were excluded because they had positive preoperative urine cultures. All patients received a single dose of either 1 gm. cefonicid or saline placebo intramuscularly before surgery. No further antibiotics were administered. Urine cultures were obtained intraoperatively, daily while hospitalized, and at 2 and 4 weeks postoperatively. A growth of 10(4) organisms constituted a positive urine culture. Postoperative infection rates were statistically significant with 12% (6 of 51) in the cefonicid group and 37% (18 of 49) in the placebo group (p = 0.003). During the initial 2 days postoperatively there were no infections in the cefonicid treated patients as opposed to 8 in the placebo group (p = 0.003). Our study demonstrated the need for antibiotic prophylaxis to prevent infection after uncomplicated transurethral resection of the prostate. This can be accomplished by using a single dose, broad-spectrum cephalosporin (cefonicid). This procedure simplifies the implementation and decreases the cost of prophylaxis for transurethral resection of the prostate.

Aged↗
PubMed1992

Rice: a high or low glycemic index food?

We determined the glycemic (GI) and insulin-index (II) values for 12 rice products, using eight healthy subjects. The products were brown and white versions of three commercial varieties of rice [two varieties with normal amylose content (20%) and the other with 28% amylose], a waxy rice (0-2% amylose), a converted rice, a quick-cooking brown rice, puffed rice cakes, rice pasta, and rice bran. The GI of the rices ranged from 64 +/- 9 to 93 +/- 11, where glucose = 100. The high amylose rice gave a lower GI and II (P < 0.01) than did the normal-amylose and waxy-rice varieties. The converted rice and most other rice products gave a high GI. Insulin indices correlated positively with GI (r = 0.75, P < 0.05), although they were lower than expected. These results indicate that many varieties of rice, whether white, brown, or parboiled, should be classified as high GI foods. Only high-amylose varieties are potentially useful in low-GI diets.

Blood Glucose↗
PubMed1992

Expression of MRF4, a myogenic helix-loop-helix protein, produces multiple changes in the myogenic program of BC3H-1 cells.

Expression of MRF4, a myogenic regulatory factor of the basic helix-loop-helix type, produced multiple changes in the myogenic program of the BC3H-1 cell line. BC3H-1 cells that stably expressed exogenous MRF4 were prepared and termed BR cell lines. Upon differentiation, the BR cells were found to have three muscle-specific properties (endogenous MyoD expression, myoblast fusion, and fast myosin light-chain 1 expression) that the parent BC3H-1 cells did not have. Of the four known myogenic regulatory factors (MyoD, myogenin, Myf-5, and MRF4), only MRF4 was capable of activating expression of the endogenous BC3H-1 myoD gene. In addition, the pattern of Myf-5 expression in BR cells was the opposite of that in BC3H-1 cells. Myf-5 expression was low in BR myoblasts and showed a small increase upon myotube formation, whereas Myf-5 expression was high in BC3H-1 myoblasts and decreased upon differentiation. Though the MRF4-transfected BR cells fused to form large myotubes and expressed fast myosin light-chain 1, the pattern of myosin heavy-chain isoform expression was the same in the BR and the nonfusing parent BC3H-1 cells, suggesting that factors in addition to the MyoD family members regulate myosin heavy-chain isoform expression patterns in BC3H-1 cells. In contrast to the changes produced by MRF4 expression, overexpression of Myf-5 did not alter BC3H-1 myogenesis. The results suggest that differential expression of the myogenic regulatory factors of the MyoD family may be one mechanism for generating cells with diverse myogenic phenotypes.

Animals↗
PubMed1992

Skeletal muscle phenotypes initiated by ectopic MyoD in transgenic mouse heart.

Forced expression of the myogenic regulatory gene MyoD in many types of cultured cells initiates their conversion into skeletal muscle. It is not known, however, if MyoD expression serves to activate all or part of the skeletal muscle program in vivo during animal development, nor is it known how limiting the influences of cellular environment may be on the regulatory effects of MyoD. To begin to address these issues, we have produced transgenic mice which express MyoD in developing heart, where neither MyoD nor its three close relatives--myogenin, Myf-5, and MRF4/herculin/Myf-6--are normally expressed. The resulting gross phenotype in offspring from multiple, independent transgenic founders includes abnormal heart morphology and ultimately leads to death. At the molecular level, affected hearts exhibit activation of skeletal muscle-specific regulatory as well as structural genes. We conclude that MyoD is able to initiate the program that leads to skeletal muscle differentiation during mouse development, even in the presence of the ongoing cardiac differentiation program. Thus, targeted misexpression of this tissue-specific regulator during mammalian embryogenesis can activate, either directly or indirectly, a diverse set of genes normally restricted to a different cell lineage and a different cellular environment.

Animals↗
PubMed1991

Rapid automated quantitation of isoleucine, leucine, tyrosine and phenylalanine from dried blood filter paper specimens.

Isothermal and isocratic HPLC chromatography for rapid quantitation of isoleucine and leucine (merged peak), tyrosine and phenylalanine from a single dried blood filter paper specimen (1/8" dot blot) is described. The net chromatography time of the relevant peaks is less than 3 min. The results can be used to screen for PKU, MSUD, and tyrosinemia in one single assay. The advantage for early determination of PKU by simultaneous quantitation of both phenylalanine and tyrosine with the determination of their ratio is discussed. Using a dual column system this procedure might be suitable for large-scale newborn screening.

Amino Acid Metabolism, Inborn Errors↗
PubMed1991

Relations between young adults and their parents.

Young adults' relationships with mothers and fathers are compared in a survey of undergraduates. Both men and women report spending more time with mothers than fathers. They indicate receiving more positive treatment from mothers and experiencing more positive emotion and closeness with them than fathers. Correlations between perceptions of treatment and experience of emotion are moderately strong, as are those between treatment/emotion and intentions to model parents. Young adults express greater certainty in using mothers than fathers as models in child-rearing, which is associated with experiencing more positive treatment and emotion with them. Since they report no more negative treatment from fathers than from mothers, their closer connections with mothers are probably due to a more positive dynamic with mothers rather than a negative dynamic with fathers. These results are consistent with previous findings that individuation and well-being in adolescence are facilitated by close, positive relationships with parents rather than distancing ones.

Adult↗
PubMed1991

Myoblasts, myosins, MyoDs, and the diversification of muscle fibers.

Distinct types of muscle fibers form and become innervated by appropriate motor neurons during development. Though the activity pattern of the innervating motor neuron affects fiber type in the adult, it is now clear that innervation is not required for the initial formation of fast and slow muscle fibers during embryonic and fetal development. In addition, multiple types of intrinsically different myoblasts are found at different stages of development and motor neurons may preferentially innervate specific types of muscle fibers at relatively early stages of myogenesis. Thus, at least some of the information required for the formation of specific motor units must be carried by muscle cells. Cellular and molecular analyses of the multiple types of myoblasts, myosin heavy chain isoforms, and myogenesis regulating proteins of the MyoD family are leading to a new understanding of the events that choreograph the formation of fast and slow motor units.

Animals↗
PubMed1991

Luteal enzymes of the luteinizing hormone and beta-adrenergic signal transduction pathways in hypophysectomized rabbits do not require pituitary hormone support.

Experiments were conducted to determine whether continuous pituitary hormone support is required for expression of the LH and beta-adrenergic cAMP signal transduction pathways in rabbit CL during pseudopregnancy. Parameters of the LH and catecholamine cAMP signal transduction pathways in CL of estrogen-treated hypophysectomized rabbits were compared to those of pituitary-intact rabbits. Results showed that each of the parameters of the LH and beta-adrenergic cAMP signal transduction pathways was retained in CL taken from estrogen-treated pseudopregnant rabbits that had been hypophysectomized for as long as 13 days at levels not significantly different from those of estrogen-treated pituitary-intact rabbits. These included luteal basal, and LH-, epinephrine-, and fluoride-stimulated adenylyl cyclase activities; total luteal cAMP levels; the number and affinity of cAMP-dependent protein kinase regulatory subunit cAMP binding sites; binding activity of the type I and type II regulatory subunits; and the amount of catalytic subunit protein of cAMP-dependent protein kinase. We conclude that expression of the proteins of the cAMP signal pathway for LH and beta-adrenergic hormones in CL of estrogen-treated rabbits does not require pituitary hormone support.

Animals↗
PubMed1991

Improving access to health care through total quality management.

Editor's Note: The intense interest in adapting principles of industrial quality control to health care is frequently identified in terms of total quality management (TQM). Introduction and implementation of these programs hospital-wide is a characteristic focus of that interest. This commentary by Drs. Miller and Milakovich discusses an even broader implication for these TQM approaches. They suggest their application to health care systems, not only to enhance quality, but to improve access as well, through the revenues generated by increased efficiency.

Efficiency↗
PubMed1990

Calcium-independent phospholipid/diolein-dependent phosphorylation of a soluble ovarian Mr 80,000 substrate protein: biochemical characteristics.

Soluble ovarian extracts were incubated with protein kinase effectors in the presence of [gamma 32P]ATP and proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Autoradiograms revealed phosphorylation of an ovarian Mr = 80,000 substrate in the presence of EGTA ([ethylenebis(oxyethylenenitrilo)]tetraacetic acid), phosphatidylserine and 1,2-diolein. In contrast to a classical response pattern to C-kinase effectors, the ovarian Mr = 80,000 phosphorylation was inhibited by 2 x 10(-7) M or greater free Ca2+. The ovarian Mr = 80,000 substrate was distinguished from the myristoylated acidic Mr = 80,000 C-kinase substrate of brain tissue on the basis of heat stability and phosphorylative response to effectors. Phosphorylation of the exogenous substrate myelin basic protein by DEAE-resolved ovarian kinase showed the variant effector dependence, maximal in the presence of EGTA, phosphatidylserine and 1,2-diolein. Finally, the effect of Ca2+ on ovarian Mr = 80,000 [32P]phosphate content could not be accounted for by post-phosphorylation activities, or by DEAE-resolvable or hydroxylapatite-resolvable inhibitory activities.

Animals↗
PubMed1990

Myogenic programs of mouse muscle cell lines: expression of myosin heavy chain isoforms, MyoD1, and myogenin.

Different mouse muscle cell lines were found to express distinct patterns of myosin heavy chain (MHC) isoforms, MyoD1, and myogenin, but there appeared to be no correlation between the pattern of MHC expression and the patterns of MyoD1 and myogenin expression. Myogenic cell lines were generated from unconverted C3H10T1/2 cells by 5-azacytidine treatment (Aza cell lines) and by stable transfection with MyoD1 (TD cell lines) or myogenin (TG cell lines). Myogenic differentiation of the newly generated cell lines was compared to that of the C2C12 and BC3H-1 cell lines. Immunoblot analysis showed that differentiated cells of each line expressed the embryonic and slow skeletal/beta-cardiac MHC isoforms though slow MHC was expressed at a much lower, barely detectable level in BC3H-1 cells. Differentiated cells of each line except BC3H-1 also expressed an additional MHC(s) that was probably the perinatal MHC isoform. Myogenin mRNA was expressed by every cell line, and, with the exception of BC3H-1 (cf., Davis, R. L., H. Weintraub, and A. B. Lassar. 1987. Cell. 51:987-1000), MyoD1 mRNA was expressed by every cell line. To determine if MyoD1 expression would alter the differentiation of BC3H-1 cells, cell lines (termed BD) were generated by transfecting BC3H-1 cells with MyoD1 under control of the beta-actin promoter. The MyoD1 protein expressed in BD cells was correctly localized in the nucleus, and, unlike the parental BC3H-1 cell line that formed differentiated MHC-expressing cells, which were predominantly mononucleated, BD cell lines formed long, multinucleated myotubes (cf., Brennan, T. J., D. G. Edmondson, and E. N. Olson. 1990. J. Cell. Biol. 110:929-938). Despite the differences in morphology and MyoD1 expression, BD myotubes and the parent BC3H-1 cells expressed the same pattern of sarcomeric MHCs.

Animals↗
PubMed1989

Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression.

A cDNA expression strategy was used to localize amino acid sequences which were specific for fast, as opposed to slow, isoforms of the chicken skeletal muscle myosin heavy chain (MHC) and which were conserved in vertebrate evolution. Five monoclonal antibodies (mAbs), termed F18, F27, F30, F47, and F59, were prepared that reacted with all of the known chicken fast MHC isoforms but did not react with any of the known chicken slow nor with smooth muscle MHC isoforms. The epitopes recognized by mAbs F18, F30, F47, and F59 were on the globular head fragment of the MHC, whereas the epitope recognized by mAb F27 was on the helical tail or rod fragment. Reactivity of all five mAbs also was confined to fast MHCs in the rat, with the exception of mAb F59, which also reacted with the beta-cardiac MHC, the single slow MHC isoform common to both the rat heart and skeletal muscle. None of the five epitopes was expressed on amphioxus, nematode, or Dictyostelium MHC. The F27 and F59 epitopes were found on shark, electric ray, goldfish, newt, frog, turtle, chicken, quail, rabbit, and rat MHCs. The epitopes recognized by these mAbs were conserved, therefore, to varying degrees through vertebrate evolution and differed in sequence from homologous regions of a number of invertebrate MHCs and myosin-like proteins. The sequence of those epitopes on the head were mapped using a two-part cDNA expression strategy. First, Bal31 exonuclease digestion was used to rapidly generate fragments of a chicken embryonic fast MHC cDNA that were progressively deleted from the 3' end. These cDNA fragments were expressed as beta-galactosidase/MHC fusion proteins using the pUR290 vector; the fusion proteins were tested by immunoblotting for reactivity with the mAbs; and the approximate locations of the epitopes were determined from the sizes of the cDNA fragments that encoded a particular epitope. The epitopes were then precisely mapped by expression of overlapping cDNA fragments of known sequence that covered the approximate location of the epitopes. With this method, the epitope recognized by mAb F59 was mapped to amino acids 211-231 of the chicken embryonic fast MHC and the three distinct epitopes recognized by mAbs F18, F30, and F47 were mapped to amino acids approximately 65-92. Each of these epitope sequences is at or near the ATPase active site.

Amino Acid Sequence↗
PubMed1989

Multiple cellular processes regulate expression of slow myosin heavy chain isoforms during avian myogenesis in vitro.

We analyzed the expression of two slow myosin heavy chain isoforms (slow MHC1 and slow MHC2) in myotubes formed from embryonic and fetal chicken myoblasts in vitro and found that the myotubes formed from myoblasts of these two developmental periods had different patterns of expression of slow MHCs. In cultures of myogenic cells from the Embryonic Day 5 (E5) hindlimb, immunoblot analysis showed that two slow MHCs with the immunological and electrophoretic properties like those of slow MHC1 and slow MHC2 were expressed on Day 3 of culture and that both slow MHCs continued to be expressed through 10 days of culture. In cultures of myogenic cells from the fetal (E12) thigh, in contrast, slow MHC1 was not expressed on Day 3 of culture, but was expressed after Day 7; slow MHC2 was never expressed by myotubes formed from fetal myoblasts. Immunocytochemistry was used to further analyze slow MHC1 and slow MHC2 expression in individual myotubes formed from embryonic and fetal myoblasts in both clonal cultures and high density, cytosine arabinoside-treated cultures. These analyses showed that (i) E5 embryonic myoblasts were of two principal types, those that formed myotubes that expressed isoforms like slow MHC1 and MHC2 throughout the life of the myotube, and those that formed myotubes that did not express slow MHCs at any time; and (ii) E12 fetal myoblasts formed myotubes that at first expressed only fast MHC but expressed both fast MHC and slow MHC1--but not slow MHC2--as culture duration was lengthened. Thus, the expression patterns of slow MHC1 and slow MHC2-like isoforms appeared to be regulated by different cellular processes in myotubes formed from embryonic and fetal myoblasts.

Animals↗