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Biomedical subjects

L E Kelly

Publications and source records attributed to L E Kelly.

31 records · Page 2Linked to original sources
PubMed1989

The effectiveness of an interactive videodisc qualitative assessment training program.

This study was designed to investigate the effect of an interactive videodisc motor skill assessment training program on the development of preservice and inservice teachers' qualitative assessment proficiency on two motor skills: the overhand throw and catch. Twenty-seven preservice and 27 inservice physical education teachers were randomly assigned to one of three treatment conditions: interactive videodisc (IVD), teacher-directed (TD), or self-directed (SD). Motor skill qualitative assessment accuracy was evaluated on a pre- and post-test basis using a 50-item motor skill assessment accuracy test (10 performances rated on 5 components) for each skill. Analysis of covariance results indicated significant main effects for treatment for both skills. Post hoc tests revealed that for the overhand throw, the IVD and TD groups were superior to the SD group but not different from each other. For the catch, the IVD group was found to be superior to both the TD and SD groups. These findings are discussed in relation to the advantages of interactive videodisc in terms of efficiency and user independence and with comparable findings in other educational applications.

Adult↗
PubMed1987

Localization of the genes shaking-B, small optic lobes, sluggish-A, stoned and stress-sensitive-C to a well-defined region on the X-chromosome of Drosophila melanogaster.

Using deletion mapping and complementation tests, we have localized 5 behavioral mutations: shaking-B2, small optic lobesKS58, sluggish-AEE85, stonedts1, and stress-sensitive-C1 to 4 genetic complementation groups at the base of the X-chromosome. Shaking-B2 is an allele of the lethal complementation group R-9-29 near band 19E3; small optic lobesKS58 and sluggish-AEE85 belong to adjacent complementation groups, between lethals W2 and A112 near band 19F4; and stonedts1 and stress-sensitive-C1 are both alleles of the 8P1 lethal complementation group between lethals 114 and 13E3 near bands 20B-C.

Alleles↗
PubMed1987

Accuracy of anthropometric equations for estimating body composition of mentally retarded adults.

Body composition of 57 mentally retarded adults (25 women, 32 men) was assessed. Skinfold and girth measurements were collected to determine how accurately existing regression equations could predict percentage body fat for a retarded population when compared to hydrostatic weighing (criterion measure) at total lung capacity. No significant differences were found between five of the six regression equations evaluated for men and four of the six regression equations evaluated for women; however, three equations had the greatest predictability and were recommended for use in estimating the percentage body fat of retarded adults.

Adipose Tissue↗
PubMed1985

Sexual dimorphism and electrophoretic variation in the form I cyclic nucleotide phosphodiesterase from Drosophila melanogaster.

We have investigated the form I cyclic nucleotide phosphodiesterase (PDE) from Drosophila melanogaster and shown that whereas heads and male thoraces and abdomens contain high levels of Ca2+-stimulated enzyme, female thoraces and abdomens contain little Ca2+-stimulated activity. The electrophoretic patterns of form I PDE from these 3 sources have also been studied and reveal that heads, and male thoraces and abdomens, produce two bands of form I PDE both of which are stimulated by Ca2+. Extracts of female thoraces and abdomens, on the other hand, show only a single, faster running band of PDE activity which is only marginally stimulated by Ca2+, if at all. Surveying wild-type strains of Drosophila has revealed that one strain, Swedish, shows altered electrophoretic mobility of the PDE band from female thoraces and abdomens. The alteration is such that the Swedish PDE band runs more anodally than the Oregon-R and Canton-S PDE activities. Mixing experiments, using co-homogenization of heads with female thoraces and abdomens, yield a single faster running band on electrophoresis. This band contains only Ca2+-insensitive PDE. Attempts to reconstruct this loss of Ca2+-sensitive PDE without electrophoresis have failed. The Swedish electrophoretic variation of the PDE from female thoraces and abdomens has been found to be recessive with respect to the Canton-S phenotype, but the variation is observed to re-emerge and segregate with the third chromosome in the F2 generation. The results indicate that electrophoretic variation in the form I PDE is, by itself, insufficient to allow the location of the structural gene for this enzyme.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1983

The regulation of phosphorylation of a specific protein in synaptosomal fractions from Drosophila heads: the effects of light and two visual mutants.

Protein IV from synaptosomal fractions of Drosophila heads is phosphorylated in vitro by an endogenous cyclic adenosine monophosphate (cAMP)-dependent protein kinase. The in vivo phosphorylation of this protein is affected by light. Two visual mutants, tan and stoned, exhibit altered levels of in vivo phosphorylation of protein IV. The tan strain shows depressed in vivo levels of phosphorylation of protein IV, whereas stoned shows an increase in the in vivo level of phosphorylation of this same protein. Protein D is phosphorylated in vitro by an endogenous Ca2+/calmodulin-dependent protein kinase and has a molecular weight identical to that of protein IV. The stoned mutant strain shows an increase in the in vivo level of phosphorylation of protein D. The data presented here suggest that the phosphorylation of protein IV, and perhaps D, may play a role in the early processing of visual information in the fly.

Animals↗
PubMed1983

An altered electroretinogram transient associated with an unusual jump response in a mutant of Drosophila.

Mutations at the stoned locus of Drosophila melanogaster produce a reversible temperature-sensitive debilitation. At permissive temperatures they also exhibit an unusual jump response to a light-off stimulus. An increase in the amplitude of the off-transient of the electroretinogram (ERG) is associated with the abnormal jump. Both the jump response and the increased amplitude of the off-transient are shown to be dependent on the duration of the light pulse prior to the light-off stimulus. In stoned flies which are light adapted, the jump response, as measured by recording from the indirect flight muscles, is seen to habituate with increasing light-off frequency. This habituation corresponds to the decrease in the amplitude of the off-transient that also occurs with high-frequency stimulation. Another visual mutant tan, removes the off and on-transients of the ERG. The combining of the stoned mutation with tan in the tan, stoned double mutant results in the loss of the jump behavior as well as the partial restoration of the off-transient to an otherwise tan-like ERG. The relationship between the increase in the amplitude of the off-transient in stoned flies and the eliciting of the jump response is discussed.

Animals↗
PubMed1981

A calcium/calmodulin-dependent cyclic adenosine monophosphate phosphodiesterase from Drosophila heads.

A Ca2+-activated cycl AMP phosphodiesterase from Drosophila melanogaster heads was studied. The enzyme accounted for approx. 40% of the total, soluble cyclic AMP phosphodiesterase activity in heads. After gel filtration, Ca2+ stimulation of the enzyme was no longer apparent, but Ca2+ activation could be restored by the addition of boiled Drosophila extract to the column-fractionated phosphodiesterase. The protein responsible for restoring Ca2+ activation was purified and shown to have some characteristics of calmodulin. In addition, porcine calmodulin was able to activate the Drosophila phosphodiesterase. Thus, the phosphodiesterase-calmodulin system in Drosophila appears analogous to similar systems in mammals.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1974

The effects of increased temperature on electroretinograms of temperature-sensitive paralysis mutants of Drosophila melanogaster.

Mutations within the shibire locus of Drosophila melanogaster are non-complementing alleles which result in reversible paralysis at 29 degrees but retention of normal locomotor behavior at 22 degrees . Electroretinograms of six of the mutants have been recorded at various temperatures. Two changes occurred in the electroretinograms of flies carrying most of the alleles at high temperature: they lost the "on"- and "off"- transients of the normal electroretinogram, and the fast decay of the receptor potential was attenuated. For flies with four of the alleles, a base-line oscillation was also observed. Analysis of electroretinograms of mosaic shibire flies indicates that the loss of the transients can be attributed to both a pre-synaptic and a post-synaptic effect.

Alleles↗
PubMedDate not supplied

Identification of a gene family from Drosophila melanogaster encoding proteins with homology to invertebrate sarcoplasmic calcium-binding proteins (SCPS).

Using antibodies raised against the Drosophila Ca(2+)-binding protein DCABP-23, we have isolated two distinct cDNA clones that encode Ca(2+)-binding proteins of the invertebrate sarcoplasmic calcium-binding protein (SCP) family. Southern blot analysis of whole genomic DNA has shown that one of the clones, Dcabp-A.1, is present in more than one copy in the genome of the fly, and is located in the beta-heterochromatic region at cytological division 80 on chromosome III. The expression pattern of this transcript shows that it is present in the tubular but not the fibrillar muscles of the adult thorax. This expression pattern is consistent with this being a true SCP. In contrast, the expression pattern of the transcript corresponding to the second cDNA clone is exclusive to neural tissue. This transcript derives from a single copy gene, and is located at cytological position 89 D on chromosome III. Comparative analysis of the amino acid sequences from the proteins encoded by the two cDNAs with that of the original DCABP-23 protein indicates that the purified DCABP-23 contained mainly the DCABP-A.1 protein. The identification of members of the SCP family of proteins in Drosophila, will allow for a future genetic investigation of the function of these ubiquitous proteins.

Amino Acid Sequence↗