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Fortieth Annual Meeting February 17-21, 1996 Baltimore

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Fortieth Annual Meeting February 17-21, 1996 Baltimore MOLECULAR RECOGNITION AND BINDING II A301 Tu-Pos219 Tu-Pos220 SPERMIDINE RELEASE FROM XENOPUS OOCYTES: A SIMPLE BARRIER MODEL IS SUFFICIENT TO EXPLAIN ELECTRODIFFUSION THROUGH A MEMBRANE CHANNEL. ((Sha, Q., 'CROSSOVER' EFFECT AND CORRECT SHIFT OF INWARD Lopatin, A.N. and C.G. Nichols)) Department of Cell Biology and Physiology, RECTIFICATION INDUCED BY MULTIVALENT POLYAMINES. ((A.N. Washington University School of Medicine, St. Louis, MO 63110 Lopatin, E.N. Makhina and C.G. Nichols)) Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110 The release of 3H-spermidine from Xenopus oocytes was examined under A different ionic conditions, and under voltage-clamp. In normal solution (2 mM -_>= Inward rectification induced by multivalent [K+]), the efflux rate is less than 1 % per hour, and is stimulated - 2-fold by -150 150 polyamines (spermine", spermidine3+, inclusion of Ca2e (1 mM) in the incubation medium. Spermidine efflux is V. (mv)putrescine2+) is relieved by external [K+], stimulated - 10-fold in high [K+] (100 mM K+) solution. In high [K+] solution, shifting strictly with EKc (Lopatin & Nichols, efflux is strongly inhibited by divalent cations (K; for Ba2+ block of spermidine 1995, J. Phys. abstr.). We have sought to efflux is - 0.1 mM), but not by tetraethylammonium ions or verapamil. explain these results in terms of a single file pore Spermidine efflux rates were not different between control oocytes and those B containing multiple ion binding sites. It has been expressing HRKI or IRKI inward rectifier K+ (Kir) channels. When the reported that the effects of 'crossover', and shift membrane potential was clamped, either by changing external [K+] in oocytes In j; Out f rectification with EK is not reproducible with expressing HRKI, or by 2-microelectrode voltage-clamp, spermidine efflux A ;blocking particles of valency > 1 (Hille & was shown to be strongly dependent on voltage, as expected for a simple ;-5,-/ Schwartz, 1978, J. Gen. Phys. 72, 409-442). electrodiffusive process, where spermidine3+ is the effluxing species. This However, this is not an 'intrinsic' problem of result arguLes against spermidine diffusing out as an uncharged species, or in I ll the barrier model, and even a simple 2-site, 3- exchange for similarly charged counterions, and is consistent with efflux Fig. IA. 'Crossover' and barrier scheme with a single polyamine binding occurring through a membrane channel. These results are the first conclusive shift of rectification for model site (Fig. I) can reproduce the observed behavior demonstration of a simple electrodiffusive pathway for spermidine efflux from in B in the presence of if one assumes strong binding of K+ ions in the at cells. 150 andi500 K = 150 selectivity filter, and electrostatic interaction mM. between polyamines and K+ ions inside the pore. Tu-Pos221 Tu-Pos222 A STOCHASTIC MODEL OF CELL-SUBSTRATE DETACHMENT VIA A MECHANICAL ANALYSIS OF A MICROPIPET ASPIRATED RED BLOOD CENTRIFUGATION. ((C. Zhu, J.W. Piper, and R.A. Swerlick*)) School of CELL LOADED BY A POINT FORCE. ((C. ZHU and S. CHESLA)) School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, GA, 30332; Mechanical Engineering, Georgia Institute of Technology, Atlanta, GA 30332 *Department of Dermatology, Emory School of Medicine, Atlanta, GA 30322 The micropipet technique is one of several experimental methods recently Cell-substrate adhesion and detachment are integral components of many employed to measure single bond detachment forces in cellular adhesion. This physiological processes. A mathematical model has been developed to describe method utilizes a micropipet aspirated red blood cell (RBC) as a force transducer. cell-substrate detachment in a commonly used centrifugation assay. The model Using a finite difference computational method, Evans et. al. (Biophys. J., vol. treats the detachment of a cell as a stochastic event which is capable of occurring at 59, p838-848, April 1991) analyzed this problem and clearly showed that the any force with a certain probability. Using an exponential relationship between technique was sensitive enough to make it attractive for measuring molecular binding affinity and bond force, we explored different representations and detachment strengths. However, the issue of accuracy was not addressed. The determined that Bell's formulation (Bell, Science, vol. 200, p.618-627, 1978) determination of the transducer accuracy and how it depends on experimental described our data better than the formulation of Dembo et al. (Proc. R. Soc. parameters is a non-trivial problem and requires rigorous mechanical analysis Lond.. vol. 234, p.55-83). Using this approach to determine bond formation and concerning cell deformation under a point load. We describe an analytical dissociation of the cell population, the fractions of the population adherent by any approach based on a boundary layer analysis in which the singularity at the pole number of bonds in equilibrium were solved in closed form. The model was (where the point load is applied) is handled by rescaling the thin shell equilibrium validated using an experimental system consisting of sialyl-Lewis X expressing equations to obtain an inner solution near the pole. This is then matched to an colon carcinoma (Colo-205) cells adherent to a plastic surface coated with a outer solution valid for the remaining cell membrane. A perturbation technique construct of E,selectin. By comparing the model prediction with the was used to decouple the governing equations of the stress field from those of the experimentally measured percentage of adherent cells for both a range of coating strain field, allowing the stress field to be statically determined and the deformed densities and various levels of imposed relative centrifugal force, we can estimate shape of the cell resolved. With this approach, a sensitivity evaluation of the the two-dimensional, no load affinity (Ka) for binding reaction between surface experinmental parameters important to an accurate force measurement is simplified, bound receptors and ligands as well as the ligand density on the carcinoma cells. as well as the solution for the RBC force-deformation relationship itself. The We have also estimated the maximum bond stretch (y) of the E-selectin - sLex presented solution is also compared and evaluated versus our own finite bond. This sub-angstrom value is in agreement with a previous estimation (Alon et difference derived solution and shows good agreement. (Supported by NSF grant al.. Nature, vol. 374, p.539-542, 1995). We are also able to predict the behavior of No. BCS-935037, NIH grant No. R29Al38282 and NIH training grant No. GM such a simplified binding system in response to changes in receptor-ligand binding 08433) characteristics such as Ka and y. (Supported by a grant from the Whitaker Foundation and NIH training grant No. GM08433) FOLDING AND SELF-ASSEMBLY II Tu-Pos223 Tu-Pos224 PROTEIN FOLDING AND ENZYMATIC ACTIVATION OF Low-Temperature Time-Resolved and Steady-State Fluorescence PSEUDOMONAS AERUGINOSA EXOTOXIN A. ((B.K. Beattie & A.R. Spectroscopy Studies of Five Single-Tryptophan Mfptants of E. coli Merrill)), Guelph-Waterloo Centre for Graduate Work in Chemistry, Dept. of Adenylate Kinase. ((T. Fulmer*', P. T. C. So*, M.Glaser, W. W. Mantulin*t)) Chem. and Biochem., Univ. of Guelph, Guelph, ON, Canada, NiG 2W1. *Laboratory of Fluorfscence Dynamics, Department of Physics, University of Illinois at (Spon. by Joan Boggs). Urbana-Champaign, Department of Biochemistry, University of Illinois at Urbana- Champaign, Urbana, IL 61801. Pseudomonas aeruginosa A Exotoxin (ETA) and its C-terminal peptide that The enzyme adenylate kinase (AK) from E. coli catalyzes the reaction ATP + AMP <==> includes the catalytic domain responsible for its ADP-ribosy[-transferase 2ADP in the presence of magnesium. Based on the comparison of several high-resolution x- (ADPRT) activity were studied by high performance size-exclusion liquid ray crystal structures, it is thought that the enzyme undergoes large domain movements upon chromatography (HPLC), fluorescence spectroscopy, and circular dichroism substrate binding. Because the wild type AK is devoid of tryptophans, it is reasonable to (CD) spectroscopy. The enzymatic function of ETA can be activated in vitro construct a library of single-tryptophan mutants, with the tryptophans placed in various by incubation with reducing agent (10 mM DTT) and denaturant (4 M urea) functionally and structurally important locations. These single-tryptophan mutants can then and the effect of various activation conditions (pH, urea, and DMT) on be used as probes of the protein dynamics of the wild-type enzyme and extensively enzymatic activity was studied. Upon enzymatic activation, structural characterized using a variety of fluorescence spectroscopic techniques. The present study changes induced within both proteins' structures were monitored by HPLC attempts to address the dynamics of the native state of the enzyme (see accompanying poster and CD spectroscopy. These changes were correlated with concomitant for unfolding studies). In order to slow the rate of interconversion between the native AK's alterations in the enzymatic activity of the proteins. The pH optimum of conformational states, it was necessary to do studies of the native-state dynamics at reduced - temperatures. AK was placed in a solution of 80% glycerol, and changes in time-resolved ADPRT activity for both ETA and PE40 was between 7.0
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