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Biomedical subjects

P D Ellis

Publications and source records attributed to P D Ellis.

At least 19 recordsLinked to original sources
PubMed1992

The relief of snoring by nasal surgery.

Patients with nasal obstruction may also complain of snoring. It is uncertain whether surgery which relieves the nasal obstruction will also relieve the snoring. We have reviewed 126 patients who complained of both nasal obstruction and snoring and who underwent nasal surgery. Snoring was completely relieved in 39 patients (31%), was less loud in a further 72 patients (57%), unchanged in 11 and louder in 4. It occurred on fewer nights post-operatively in 61, on the same number in 24 and more frequently in 2. Patients who had nasal polypectomy as part of their nasal surgery obtained the greatest snoring relief. This study suggests that when snoring and nasal obstruction coexist nasal surgery should be considered as the first line of surgical treatment.

Humans↗
PubMed1989

113Cd NMR of Cd2+-substituted carboxypeptidase. Support for a hexa-coordinate metal ion in the presence of inhibitors.

The liquid-state 113Cd NMR data of carboxypeptidase A in the presence and absence of inhibitors obtained by Gettins (Gettins, P. (1986) J. Biol. Chem. 261, 15513-15518) are analyzed in terms of whether the inhibitors displace water from Cd2+ upon binding to the protein. This question is addressed by applying the single crystal data and the methods introduced by Honkonen and Ellis (Honkonen, R. S., and Ellis, P. D. (1984) J. Am. Chem. Soc. 106, 5488-5497). Calculations based upon these data demonstrate that displacement of water by a carboxyl group should lead to significant shielding of a 113Cd resonance by approximately 100 ppm. Since the observed 113Cd chemical shifts for carboxypeptidase A are modest and deshielding (12-17 ppm), it is argued that the chemical shifts imply that water is not displaced from the Cd2+ center upon binding of inhibitors to carboxypeptidase A. Rather, the Cd2+ ion increases its coordination number from five to six upon binding of the inhibitor.

Cadmium↗
PubMed1989

19F nuclear magnetic resonance as a probe of the spatial relationship between the heme iron of cytochrome P-450 and its substrate.

The distance between the heme iron of ferrous cytochrome P-450-CAM and a fluorine label attached to the 9-methyl carbon of its substrate, (1R)-(+)-camphor, has been determined using 19F NMR. This investigation uses the Solomon-Bloembergen equation to measure the distance from a paramagnetic heme iron to a fluorine probe incorporated into a substrate that is not in fast exchange. The structural identity of the substrate analogue, 9-fluorocamphor, has been established using one- and two-dimensional NMR methods and mass spectrometry. The relaxation rate of 9-fluorocamphor bound to high-spin paramagnetic ferrous P-450-CAM has been studied at 188, 282, and 376 MHz, and the correlation time has been directly determined from the frequency dependence of the relaxation rate. When the substrate analogue was bound to the low-spin diamagnetic ferrous-CO derivative of the enzyme, the relaxation rate was found to be 100 times slower and was therefore neglected in the distance calculation. The relaxation data for the paramagnetic system and the correlation time have been used to calculate a distance of 3.8 A between the heme iron and the C-9 fluoride. A fit of the distance and the chemical shift data to the pseudocontact shift equation predicts an angle of approximately 52 degrees between the heme normal and the Fe-F vector. The solution state Fe-F distance is somewhat shorter and the angle between the heme normal and the Fe-F vector slightly larger for the substrate-bound ferrous enzyme reported herein than the analogous values for the substrate-bound ferric enzyme determined in the solid state by x-ray crystallography. These differences may reflect a structural change at the substrate-binding site upon reduction of the iron.

Camphor↗
PubMed1988

Cadmium-substituted skeletal troponin C metal binding investigations and sequence assignment of the cadmium-113 resonances.

The binding of cadmium to the calcium binding subunit of skeletal troponin (STnC) has been reinvestigated using direct binding methods and fluorescent derivatives. These data provide straightforward explanations of the observed titration behavior in the 113Cd NMR (Ellis, P.D., Strang, P., and Potter, J.D. (1984) J. Biol. Chem. 259, 10348-10356). Further, fluorescent derivatives of skeletal troponin C provide an excellent means of establishing a sequence assignment for the resonances observed in the 113Cd NMR. The results of these experiments demonstrate that sites I and II, the Ca2+ regulatory sites, can be assigned to resonances at -108.5 and -101.5 ppm, respectively. Sites III and IV, the structural sites, are assigned to resonances -112.8 and -106.8 ppm, respectively. These data are discussed in terms of recent structural findings and speculations.

Animals↗
PubMed1988

Synaptic protein tyrosine kinase: partial characterization and identification of endogenous substrates.

The subcellular distribution of protein tyrosine kinase in rat forebrain was determined using [Val5]-angiotensin II as exogenous substrate. Enzyme activity was present in each of the fractions analyzed and was enriched in synaptic membranes (SMs) and the synaptosomal soluble fraction (2.2- and 2.5-fold over the homogenate, respectively). SMs also phosphorylated polyglutamyltyrosine (pGT; molar ratio of 4:1), the Vmax for angiotensin and pGT phosphorylation being 26.3 +/- 1.6 and 142 +/- 4 pmol/min/mg, respectively. Extraction of SMs with several different detergents resulted in enhanced enzyme activity and the solubilization of 33-37% of the angiotensin and 43-70% of the pGT-phosphorylating activity. Isolated postsynaptic densities (PSDs) contained tyrosine kinase and phosphorylated angiotensin and pGT. The Vmax values for angiotensin and pGT phosphorylation by PSDs were 17 +/- 5 and 23 +/- 1 pmol/min/mg, respectively. Six putative endogenous substrates for SM tyrosine kinase, with molecular weights of 205K, 180K, 76K, 60K, 50K, and 45K, were identified. Each of these proteins, except p76, was phosphorylated in the detergent-insoluble residue obtained following the extraction of SMs with Triton X-100 as well as in PSDs, indicating that the postsynaptic apparatus is an active site of tyrosine phosphorylation. The phosphorylation of p76 was localized to the Triton X-100 extract and also occurred in the synaptosomal soluble fraction. The results indicate that tyrosine kinase and its substrates are located in both pre- and postsynaptic compartments and suggest a role for this enzyme in synaptic function.

Angiotensin II↗
PubMed1987

Nuclear magnetic resonance investigation of cadmium 113 substituted pea and lentil lectins.

The lentil (LcH) and pea (PSA) lectins, which are members of the class of D-glucose/D-mannose binding lectins, are Ca2+ X Mn2+ metalloproteins that require the metal ions for their saccharide binding and biological activities. We have prepared a variety of Cd2+ derivatives of PSA and LcH, with Cd2+ in either the transition metal (S1) or calcium (S2) sites, or in both. Thus, Cd2+ X Zn2+, Cd2+ X Mn2+, and Ca2+ X Cd2+ derivatives were prepared, in addition to the Cd2+ X Cd2+ derivatives which we have recently reported. This is the first report of stable mixed metal Cd2+ complexes of lectins. The physical and saccharide binding properties of the Cd2+ derivatives of both lectins were characterized by a variety of physiochemical techniques and found to be the same as those of the corresponding native proteins. 113Cd NMR spectra of mono- and disubstituted 113Cd2+ complexes of LcH and PSA were recorded and compared with 113Cd NMR data for concanavalin A (ConA) (Palmer, A.R., Bailey, D.B., Behnke, W.D., Cardin, A.D., Yang, P.P., and Ellis, P.D. (1980) Biochemistry 19, 5063-5070). The data for the PSA and LcH derivatives were found to be very similar, indicating close homology of their metal ion binding sites. 113Cd resonances at 44.6 ppm and -129.4 ppm for 113Cd2+ X 113Cd2+ X LcH, and at 46.6 and -130.4 for the corresponding PSA derivative, are chemical shifts very similar to those observed for 113Cd2+ X 113Cd2+ X ConA. Assignment of the resonances to the transition metal (S1) and calcium (S2) sites were unambiguous since the Ca2+ X 113Cd2+ and 113Cd2+ X Zn2+ derivatives of both lectins showed single resonances characteristic of the S1 and S2 sites, respectively. The results indicate that, unlike ConA, 113Cd2+ binds tightly to PSA and LcH. Binding of monosaccharide to both lectins induce small (2 ppm) upfield shifts in their S2 113Cd resonances, in contrast to the larger shift (8 ppm) observed in ConA. The 113Cd2+ X Mn2+ complexes of PSA and LcH fail to show a 113Cd resonance characteristic of these derivatives, which provides evidence for the close proximity of the metal ions in the two proteins. The present findings indicate that the coordinating ligand atoms to the metal ions at the S1 and S2 sites in LcH, PSA, and ConA are the same.

Cadmium↗
PubMed1985

Cadmium(II)-113 NMR studies of the mechanism of metal ion activation of yeast enolase.

Yeast enolase binds one mole of 113Cd2+ per subunit at a site that consists of all oxyligands in a distorted octahedral environment. This "conformational" metal ion's environment undergoes further distortion on addition of substrate/product or analogs. At pH's below the optimum value the shifted resonance tends to break up into several, suggesting the existence of several slowly exchanging intermediate forms. At acid pH's, on addition of one additional mole/subunit of 113Cd2+, which greatly increases catalysis, "conformational" resonance(s) further broadens, suggesting that the second, "catalytic" metal ion increases the rates of interconversion between "conformational" species. At more alkaline pH's, near the optimum pH, the "conformational" peak is sharpened, which suggests that very fast interconversion is occurring. The position of the "catalytic" metal ion resonance also suggests all oxyligands in a distorted octahedral geometry. The "catalytic" resonance is often broadened to the point where it cannot be seen, suggesting rapid changes in its geometry due to interconversion of substrate and product.

Binding Sites↗
PubMed1977

The applied anatomy of thyroglossal tract remnants.

Recurrences after surgery for thyroglossal cysts and fistulas were common until, in 1920, Sistrunk described his technique for removing the whole thyroglossal tract. Since that time there has been considerable argument concerning the exact path taken by the tract particularly in relation to the hyoid bone. In an attempt to elucidate this problem, studies have been made of embryos at varying stages of development, of serially step-sectioned adult larynges and of surgical specimens. These studies suggest that the thyroglossal tract occupies a constant and embryologically predictable position in relation to the hyoid bone and they support the rationale of Sistrunk's procedure.

Female↗
PubMed1976

Changes in nystagmus on raising body temperature in clinically suspected and proved multiple sclerosis.

Electronystagmography was used to record the appearance or alteration of nystagmus after raising the body temperature by a heat cradle. Nystagmus was increased or provoked in 13 out of 15 patients with clinically proved multiple sclerosis, in eight out of 12 suspected cases, but in no normal controls. No positive results were obtained in 12 patients with other neurological diseases, even when nystagmus was part of the clinical picutre. The technique is simple to use and may have a role in the diagnosis of multiple sclerosis.

Adult↗