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PubMed1980

Evidence of a specific complex between adriamycin and negatively-charged phospholipids.

Membrane-model systems (monolayers, small unilamellar vesicles) were used to study the interaction between adriamycin (ADM) and phospholipids. Adsorption of 3H-labeled adriamycin on different phospholipid monolayers demonstrated the specificity of adriamycin for negatively-charged phospholipids (cardiolipin, phosphatidylserine, phosphatidic acid). The stoichiometry has been found to be approx. 2 mol (1.8) adriamycin per mol cardiolipin and approx. 1 mol (0.75) adriamycin per mol phosphatidylserine and phosphatidic acid. No adsorption was detected with neutral lipids. Surface-potential measurements confirm the formation of a complex stabilized by electrostatic interactions without penetration of the drug into the lipid lipophilic phase. Some adriamycin derivatives were used to discriminate between the ionized hydrophilic and hydrophobic contributions in the complex formation. The absorption spectrum of adriamycin in the presence of cardiolipin resembles the behavior of the ADM-DNA complex. Moreover, the association constants of the two complexes are very similar (cardiolipin-ADM, 1.6 . 10(6) . M-1; ADM-DNA, 2.4 . 10(6) . M-1). To explain the high affinity of cardiolipin for adriamycin, we proposed that two essential interactions are responsible for the complex stabilization: an electrostatic interaction between the protonated amino groups of the sugar residues and the ionized phosphate residues, and an interaction between adjacent anthraquinone chromophores. These data strongly suggest competitive behavior between a membrane site and the target. Consequently, it must be assumed that the lipidic components of the cell membrane structure may be an important determinant in the behavior of adriamycin. This observation should be kept in mind in the building of new derivatives.

Calorimetry↗
PubMed1992

Recent health policy initiatives in Nordic countries.

Health care systems in Sweden, Finland, and Denmark are in the midst of substantial organizational reconfiguration. Although retaining their tax-based single source financing arrangements, they have begun experiments that introduce a limited measure of competitive behavior in the delivery of health services. The emphasis has been on restructuring public operated hospitals and health centers into various forms of public firms, rather than on the privatization of ownership of institutions. If successful, the reforms will enable these Nordic countries to combine their existing macroeconomic controls with enhanced microeconomic efficiency, effectiveness, and responsiveness to patients.

Contract Services↗
PubMed2003

Indirect effects of contaminants in aquatic ecosystems.

Contaminants such as petroleum hydrocarbons, heavy metals and pesticides can cause direct toxic effects when released into aquatic environments. Sensitive species may be impaired by sublethal effects or decimated by lethality, and this ecological alteration may initiate a trophic cascade or a release from competition that secondarily leads to responses in tolerant species. Contaminants may exert direct effects on keystone facilitator and foundation species, and contaminant-induced changes in nutrient and oxygen dynamics may alter ecosystem function. Thus, populations and communities in nature may be directly and/or indirectly affected by exposure to pollutants. While the direct effects of toxicants usually reduce organism abundance, indirect effects may lead to increased or decreased abundance. Here we review 150 papers that reference indirect toxicant effects in aquatic environments. Studies of accidental contaminant release, chronic contamination and experimental manipulations have identified indirect contaminant effects in pelagic and benthic communities caused by many types of pollutants. Contaminant-induced changes in behavior, competition and predation/grazing rate can alter species abundances or community composition, and enhance, mask or spuriously indicate direct contaminant effects. Trophic cascades were found in 60% of the manipulative studies and, most commonly, primary producers increased in abundance when grazers were selectively eliminated by contaminants. Competitive release may also be common, but is difficult to distinguish from trophic cascades because few experiments are designed to isolate the mechanism(s) causing indirect effects. Indirect contaminant effects may have profound implications in environments with strong trophic cascades such as the freshwater pelagic. In spite of their undesirable environmental influence, contaminants can be useful manipulative tools for the study of trophic and competitive interactions in natural communities.

Animals↗
PubMed2004

Biochemical regulation of mammalian AMP-activated protein kinase activity by NAD and NADH.

AMP-activated protein kinase (AMPK) serves as an energy-sensing protein kinase that is activated by a variety of metabolic stresses that lower cellular energy levels. When activated, AMPK modulates a network of metabolic pathways that result in net increased substrate oxidation, generation of reduced nucleotide cofactors, and production of ATP. AMPK is activated by a high AMP:ATP ratio and phosphorylation on threonine 172 by an upstream kinase. Recent studies suggest that mechanisms that do not involve changes in adenine nucleotide levels can activate AMPK. Another sensor of the metabolic state of the cell is the NAD/NADH redox potential. To test whether the redox state might have an effect on AMPK activity, we examined the effect of beta-NAD and NADH on this enzyme. The recombinant T172D-AMPK, which was mutated to mimic the phosphorylated state, was activated by beta-NAD in a dose-dependent manner, whereas NADH inhibited its activity. We explored the effect of NADH on AMPK by systematically varying the concentrations of ATP, NADH, peptide substrate, and AMP. Based on our findings and established activation of AMPK by AMP, we proposed a model for the regulation by NADH. Key features of this model are as follows. (a) NADH has an apparent competitive behavior with respect to ATP and uncompetitive behavior with respect to AMP resulting in improved binding constant in the presence of AMP, and (b) the binding of the peptide is not significantly altered by NADH. In the absence of AMP, the binding constant of NADH becomes higher than physiologically relevant. We conclude that AMPK senses both components of cellular energy status, redox potential, and phosphorylation potential.

AMP-Activated Protein Kinases↗
PubMed2004

Competitive interactions between retinal ganglion axons for tectal targets explain plasticity of retinotectal projection in the servomechanism model of retinotectal mapping.

The mechanism of topographic mapping of retinal ganglion cells to the midbrain was previously elucidated by the servomechanism model, which is based on the fact that cells expressing Eph-receptors respond specifically to surface expressing membrane-bound ephrin-ligands at a critical level. The retina has increased nasal-to-temporal gradient of Eph receptor-density, and the optic tectum/superior colliculus has increased rostral-to-caudal gradient of membrane-bound ephrin-ligand. An axon from the retina has an identification tag of a certain level of Eph-receptor density depending on its retinal position, and adheres to the site on the tectum/superior colliculus expressing ephrin-ligands at a critical ligand-density level. The servomechanism model rigidly defines positions of axon terminals on the midbrain. However, optic nerve regeneration experiments combined with halved retina or tectum show a plastic or flexible mapping (expansion, compression and transposition of tectal projections). To reconcile the discrepancy between the rigid model and the plastic behavior, competition between retinal axon terminals for a target site was introduced to the servomechanism. The servomechanism/competition model succeeded in computer simulations of the plastic mapping of retinal axons on the tectum. Recent experiments of upregulated ligand-density on the tectum during nerve regeneration and the role of axonal competition are discussed.

Algorithms↗
PubMed2005

Behavioral and anatomical effects of quinolinic acid in the striatum of the hemiparkinsonian rat.

Parkinson's disease (PD), a hypokinetic disorder, and Huntington's disease (HD), a hyperkinetic disorder, share the fact that in the motor pathways the dysfunction starts in the striatum. In PD the projection neurons are overactive due to decreased inhibitory regulation by lost dopamine afferents, while in HD the output from the striatum is insufficient due to loss of projection neurons. This study aimed to determine whether the introduction of a mild HD condition in the PD striatum can counter the hypokinetic condition. The experiment was carried out in the 6-OHDA rat model for PD in which amphetamine, 5 mg/kg, evokes an asymmetric rotation response toward the side of the 6-OHDA lesion (ipsilateral rotation). The response to amphetamine in this study was fractionated into multiple components and measured automatically. After baseline measurements, the subjects were divided into four groups. Group I was unilaterally sham-lesioned in medial, central, and lateral striatum. Group II was injected quinolinic acid (QA) 20 nM in medial, central, and lateral striatum. Group III was injected QA 60 nM in central striatum. Group IV was injected QA 120 nM in central striatum. The effects of QA were measured weekly. The sham lesions in Group I had no effects. In Group II, ipsilateral rotation was reduced and replaced by oral stereotypy, a competitive behavior. In Group III, ipsilateral rotation decreased, but to a lesser degree than in Group II. In Group IV, QA had no effects. Histological findings show a unilateral loss of tyrosine immunoreactive (TH) neurons in substantia nigra and of fibers in striatum in all subjects. In addition, in Group II the striatum was atrophied. These findings suggest that the shift in Group II from ipsilateral rotation to oral stereotypy after QA was due to reduced striatal output caused by a loss of projection neurons, a loss insufficient to induce HD symptoms, but sufficient to counter the PD condition.

Adrenergic Agents↗
PubMed2005

On sexual behavior and sex-role reversal.

Sex is not about reproduction; sex is about (re-)combination of DNA. Sex, not reproduction, always involves physical contact between two individuals; to achieve this, strategies of sexual behavior evolved. Sexual behavior, therefore, did not evolve as part of a reproductive strategy, but evolved to enable exchange of genetic material. In multicellular organisms the situation is more complicated than in unicellular organisms, as it is impossible for each cell within a multicellular body to have sex with another cell. Hence, evolution selected a system in which the possibility to have sex was limited to only one cell-line: the germ cells. As a result, sex adopted the character of fertilization, and sex and reproduction became inseparably linked. Still, in some species, including humans, sexual behavior still exhibits features of its evolutionary past: in humans (like in bonobo's) most sexual activity and many sexual behavioral patterns have nothing to do with reproduction (masturbation, homosexual behavior, for example); in humans, sexual behavior also became associated with other strategic objectives, such as intensifying the pair bond, expression of love or power. Different genders - male and female - evolved, and each gender evolved typical gender-related sexual and reproductive strategies as well. In most multicellular species, these strategies became inextricably mixed, and sexual behavior increasingly more - and in most species even exclusively - 'served' the interests of reproduction: sexual behavior became more or less synonymous with reproductive behavior. In most species, the 'mix' of sexual and reproductive strategies evolved into typical gender-related patterns of behavior, that is, in typical 'sex-roles'. Often, males are bigger and more 'beautiful' (= more intensely ornamented) than females; males compete with each other for access to females; males court females, while females choose males ('female choice'). However, ecological circumstances may cause a reversal of sex-roles, resulting in a situation in which females are bigger and more intensely ornamented than males, females compete for access to males, females court males and only males invest in care for the young, provided they are relatively certain of their paternity. Also, as in the case of the spotted hyena, females may be highly virilized and be socially dominant. This 'sex-role reversal' is seen, e.g., when males are relatively rare due to high predation pressure, or when the process of reproduction is very risky for the same reason: then it is 'better' that males, with their plenty of sperm, are wasted, than females with their few, precious eggs. It can be argued, with women being the fair sex, exhibiting competitive behavior and with an actively displaying courtship, and with men investing heavily in their offspring, meanwhile taking all (cultural) kinds of measures to guarantee their paternity, that humans, too, exhibit some degree of sex-role reversal.

Animals↗
PubMed1976

Conformations of lysine-sensitive aspartokinase.

1. The technique of differential thermal and proteolytic inactivation has been employed as a conformational probe for the lysine-sensitive aspartokinase (EC 2.7.2.4) of Escherichia coli B. 2. L-Amino acid inhibitors of this enzyme each induce a characteristic enzyme conformation. This is evidenced by rates of thermal and proteolytic inactivation and Arrhenius activation energies for thermal inactivation which are characteristic of the amino acid present. 3. Phenylalanine and leucine binding are mutually exclusive as evidenced by competitive behavior in thermal inactivation experiments, suggesting a hydrophobic amino acid binding site with broad specificity. 4. The phenylalanine-dependent conformation and the leucine-dependent conformation differ considerably. In comparison with the native enzyme, the former is more labile to proteolysis by trypsin whereas the latter is more stable. First-order rate constants for thermal inactivation of the phenylalanine- and leucine-dependent conformations are, respectively, about one-half and one-tenth that of the native enzyme. 5. Items 3 and 4 taken together suggest that the conformations are ligand induced and do not arise via ligand stabilization of spontaneously arising conformers.

Aspartate Kinase↗
PubMed1988

Structure-activity studies on inhibition of choline uptake by a mouse brain synaptosomal preparation: basic data.

Over 80 substances were studied for their inhibition of high-affinity uptake of [3H]choline into a mouse brain synaptosomal fraction. Kinetic experiments tested a number of them for competitive behavior. A minimal provisional model for the choline uptake process is envisioned that is consistent with current data and with relevant observations in the literature. There are two hydrophilic anionic sites on the choline transporter that are separated from each other by a cationic hydrophobic domain. Association of choline in a Na+-dependent manner with one or both of the sites is necessary for the transport of choline to take place. The choline binding anionic sites are sufficiently large and/or flexible to allow attachment of cationic moieties larger than choline. The cationic hydrophobic domain of the transporter is flexible, probably tending to planarity. The length of the hydrophobic region between the anionic sites is approximately that of 10 extended methylene groups, and the minimal width is approximated by the distance across the condensed ring system of chlorpromazine. The probability of attachment of the highly hydrophilic choline to its binding sites is increased both by hydrogen-bonding to a proton-acceptor within the anionic sites and by repulsion from the cationic hydrophobic region. A number of substances that potently and competitively inhibit high affinity choline uptake possess quaternary ammonium groups and neutral or negatively charged lipophilic groups. In general, substances in which two quaternary ammonium groups are separated by an appropriately configured hydrophobic group and which can combine with both anionic sites and the hydrophobic region between them are more potent inhibitors than monoquaternary substance with the same or similar groups. However, substances with a single high-affinity quaternary group and an appropriately structured hydrophobic group, e.g. the trimethoxy-3-butynyl quaternary ammonium compounds, possess inhibitory efficacies similar to those shown by the most potent bisquaternaries. The above suggests that further delineation of the characteristics of the structures of the above sites of the transporter could lead to devisal of more potent reversible inhibitors of choline uptake than now are available.

Animals↗
PubMed2006

Stimulation of P-glycoprotein ATPase by analogues of tetramethylrosamine: coupling of drug binding at the "R" site to the ATP hydrolysis transition state.

The multidrug resistance efflux pump P-glycoprotein (Pgp) couples drug export to ATP binding and hydrolysis. Details regarding drug trajectory, as well as the molecular basis for coupling, remain unknown. Nearly all drugs exported by Pgp have been assayed for competitive behavior with rhodamine123 transport at a canonical "R" drug binding site. Tetramethylrosamine (TMR) displays a relatively high affinity for Pgp when compared to other rhodamines. Here, we present the construction and characterization of a library of compounds based upon the TMR scaffold and use this set to assess the determinants of drug binding to the "R" site of Pgp. This set contained modifications in (1) the number, location, and conformational mobility of hydrogen-bond acceptors; (2) the heteroatom in the xanthylium core; and (3) the size of the substituent in the 9-position of the xanthylium core. Relative specificity for coupling to the distal ATP catalytic site was assessed by ATPase stimulation. We found marked ( approximately 1000-fold) variation in the ATPase specificity constant within the library of TMR analogues. Using established methods involving ADP-Vi trapping by wild-type Pgp and ATP binding by catalytic carboxylate mutant Pgp, these effects can be extended to ATP hydrolysis transition-state stabilization and ATP occlusion at a single site. These data support the idea that drugs trigger the engagement of ATP catalytic site residues necessary for hydrolysis. Further, the nature of the drug binding site and coupling mechanism may be dissected by variation of a drug-like scaffold. These studies may facilitate development of novel competitive inhibitors at the "R" drug site.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1985

[Competition of solid and fluid liposomes for binding and metabolism with lipids from the cell surface].

The competitive behavior of solid vs. fluid liposomes in liposome-cell adsorption and cell-to-liposome lipid transfer processes was investigated with L cells and FBT epithelial sheets. Binding and transfer experiments have demonstrated that: solid liposomes adhere to the cell surface as integral vesicles retaining the entrapped substance; fluid liposomes are partly disintegrated at the cell surface with concomitant entry of entrapped substances into the cytoplasm, while their lipids remain on the cell surface; fluid liposomes that escape lysis dissociate from the cell taking away cell lipid molecules. No lipid transfer occurs between the plasma membrane and solid liposomes. Cell-bound solid liposomes interfere with the transfer of cell lipids to fluid liposomes, while these in turn inhibit the binding of solid liposomes to the cell surface.

Animals↗
PubMed1996

An evolutionarily conserved binding site for serine proteinase inhibitors in large conductance calcium-activated potassium channels.

Complementary DNA coding for the channel-forming alpha-subunit of a large conductance Ca(2+)-activated K+ channel (maxi Kca channel) was cloned from bovine aortic smooth muscle cells. This cloned mammalian KCa channel (Bslo) and its homolog from Drosophila (Dslo) were expressed in the HEK293 human embryonic kidney cell line. Both Bslo and Dslo KCa channels were sensitive to inhibition by the internally applied serine proteinase inhibitors: bovine pancreatic trypsin inhibitor (BPTI, KD = 7.0 microM for Bslo and 2.6 microM for Dslo) and chicken ovoinhibitor (OI, KD = 1.5 microM for Bslo and 11.4 microM for Dslo). BPTI and OI are members of the Kunitz and Kazal families of proteinase inhibitors, respectively. The approximately 60-residue inhibitory domains of these proteins have a different tertiary structure except in the region of a loop formed by approximately 6 residues, in which the peptide backbone adopts a similar conformation complementary to the active site cleft of many serine proteinases. At the single-channel level, BPTI and OI were found to inhibit KCa channels by a similar mechanism involving the production of discrete low-conductance events. These two inhibitors also exhibited competitive behavior, suggesting that they bind to an overlapping site. Kinetic characterization revealed that the dissociation rate of BPTI from the bovine KCa channel is fast (k(off) = 0.41 s-1), whereas that from the Drosophila KCa channel is slow (k(off) = 9.0 x 10(-4) s-1) and indicative of a strong molecular interaction. The stable complex of BPTI and trypsin was inactive as a KCa channel inhibitor, further supporting the idea that the trypsin inhibitory loop of BPTI recognizes a specific site on the channel protein. These results lead to the conclusion that the alpha-subunit of maxi KCa channels contains a conserved proteinase inhibitor binding site. We hypothesize that this site corresponds to a C-terminal domain of the channel protein that structurally resembles serine proteinases.

Amino Acid Sequence↗
PubMed2002

Binding characteristics of cetirizine and levocetirizine to human H(1) histamine receptors: contribution of Lys(191) and Thr(194).

Competition experiments with [(3)H]mepyramine showed that cetirizine and its enantiomers, levocetirizine and (S)-cetirizine, bound with high affinity and stereoselectivity to human H(1) histamine receptors (K(i) values of 6, 3, and 100 nM, respectively). Cetirizine and levocetirizine were 600-fold more selective for H(1) receptors compared with a panel of receptors and channels. Binding results indicated that the interaction between cetirizine, its enantiomers, and histamine is compatible with a competitive behavior, in contrast with the noncompetitive profile of cetirizine and levocetirizine observed in isolated organs. Binding kinetics provided a suitable explanation for this observation, because levocetirizine dissociated from H(1) receptors with a half-time of 142 min; that of (S)-cetirizine was only 6 min, implying that the former could act as a pseudo-irreversible antagonist in functional studies. The carboxylic function of levocetirizine seemed responsible for its long dissociation time. Indeed, hydroxyl or methyl ester analogs dissociated more rapidly from H(1) receptors, with half-times of 31 min and 7 min, respectively. The importance of the carboxylic function of levocetirizine for the interaction with the H(1) receptor was further supported by the results from the mutation of Lys(191) to Ala(191). This mutation decreased the dissociation half-time of levocetirizine from 142 to 13 min and reduced its affinity from 3 to 12 nM, whereas the affinity and dissociation kinetics of hydroxyl and methyl ester analogs were hardly affected. The mutation of Thr(194) reduced the binding stereoselectivity by selectively enhancing the affinity of the distomer.

Alanine↗
PubMed1999

The assessment of antagonist potency under conditions of transient response kinetics.

The muscarinic acetylcholine receptor antagonists, atropine and pirenzepine, produced an apparent insurmountable antagonism of muscarinic M(1) receptor-mediated intracellular Ca(2+) mobilization in Chinese hamster ovary (CHO) cells when tested against the agonists carbachol or xanomeline. Each antagonist caused a dextral shift of the agonist concentration-response curves with depression of the maximum response that was incomplete (i.e., saturated) and which varied with the pairs of agonist and antagonist. Equilibrium competition binding assays found no deviation from simple, reversible competitive behavior for either antagonist. The relative rates of dissociation of unlabeled atropine and pirenzepine were also assessed in radioligand kinetic studies and it was found that atropine dissociated from the receptor approximately 8-fold slower than pirenzepine. Numerical dynamic simulations suggested that the insurmountability of antagonism observed in the present study was probably a kinetic artifact related to the measurement of transient responses to a non-equilibrated agonist in the presence of a slowly dissociating antagonist. Importantly, the patterns of antagonism observed included a saturable depression of agonist maximal response, a mode of antagonism that is incompatible with the previously described phenomenon of hemi-equilibrium states. Monte Carlo simulations indicated that reasonable, semi-quantitative estimates of antagonist potency could be determined by a minor modification of standard methods, where equieffective agonist concentrations, rather than EC(50) values, are compared in the absence and presence of antagonist. Application of the latter approach to the functional data yielded estimates of antagonist potency that were in excellent agreement with those derived from the equilibrium binding assays, thus indicating that the present method can be useful for quantifying antagonist potency under non-equilibrium conditions.

Animals↗
PubMed1992

Protein-DNA interactions at the H4-site III upstream transcriptional element of a cell cycle regulated histone H4 gene: differences in normal versus tumor cells.

Upstream sequences of the H4 histone gene FO108 located between nt -418 to -213 are stimulatory for in vivo transcription. This domain contains one protein/DNA interaction site (H4-Site III) that binds factor H4UA-1. Based on methylation interference, copper-phenanthroline protection, and competition assays, we show that H4UA-1 interacts with sequences between nt -345 to -332 containing an element displaying sequence-similarity with the thyroid hormone response element (TRE). Using gel retardation assays, we also demonstrate that H4UA-1 binding activity is abolished at low concentrations of Zn2+ (0.75 mM), a characteristic shared with the thyroid hormone (TH) receptor DNA binding protein. Interestingly, phosphatase-treatment of nuclear proteins inhibits formation of the H4UA-1 protein/DNA complex, although a complex with higher mobility (H4UA-1b) can be detected; both complexes share identical protein-DNA contacts and competition behaviors. These findings suggest that phosphorylation may be involved in the regulation of H4-Site III protein/DNA interactions by directly altering protein/protein associations. H4-Site III interactions were examined in several cell culture systems during cell growth and differentiation. We find that H4UA-1 binding activity is present during the cell cycle of both normal diploid and transformed cells. However, during differentiation of normal diploid rat calvarial osteoblasts, we observe a selective loss of the H4UA-1/H4-Site III interaction, concomitant with an increase of the H4UA-1b/H4-Site III complex, indicating modifications in the heteromeric nature of protein/DNA interactions during downregulation of transcription at the cessation of proliferation. Transformed cells have elevated levels of H4UA-1, whereas H4UA-1b is predominantly present in normal diploid cells; this alteration in the ratio of H4UA-1 and H4UA-1b binding activities may reflect deregulation of H4-Site III interactions in transformed cells. We propose that H4-Site III interactions may contribute, together with protein/DNA interactions at proximal regulatory sequences, in determining the level of H4-FO108 histone gene transcription.

Base Sequence↗
PubMedDate not supplied

New arrangements, new scrutiny. The IRS reconsiders hospital-physician relationships at tax-exempt facilities.

The pressure to maintain adequate operating margins has forced many not-for-profit hospitals to adopt more overtly competitive behavior than they have in the past. However, in struggling to remain economically viable, these facilities should carefully avoid actions that would threaten their tax-exempt status. Not-for-profit facilities should be particularly careful that their arrangements with physicians, which often appear designed to increase referrals, do not violate the criteria according to which the Internal Revenue Code extends tax exemption to charitable organizations. Section 501(c)(3) of the code exempts organizations "no part of the net earnings of which inures to the benefit of any private shareholder or individual." According to this provision, "insiders" (i.e., those with a personal interest in or opportunity to influence organization activities from the inside) are entitled to no more than reasonable payment for their goods or services. The Internal Revenue Service (IRS) takes the position that, as employees or individuals having a close professional working relationship with a hospital, physicians are insiders. Thus a hospital that pays physicians what the IRS judges to be more than fair market value for services (or charges physicians less than fair market value for office rental) may find its exemption in jeopardy. If not-for-profit hospitals want to maintain their tax-exempt status, they must be certain the arrangements they enter into with physicians truly further their exempt purpose: to promote the health of the community.

Charities↗
PubMed2003

Growth physiology and competitive interaction of obligately chemolithoautotrophic, haloalkaliphilic, sulfur-oxidizing bacteria from soda lakes.

Two different groups of haloalkaliphilic, obligately autotrophic, sulfur-oxidizing bacteria belonging to the genera Thioalkalimicrobium and Thioalkalivibrio have recently been discovered in highly alkaline and saline soda lakes. To understand response to their extreme environment and different occurrence in soda lakes, the growth kinetics and competitive behavior of several representatives have been characterized in detail using batch and pH-controlled continuous cultivation. The bacteria belong to the true alkaliphiles, growing within the pH range 7.5-10.6 with maximum growth rate and maximum growth yield at pH 9.5-10. On the basis of their response to salt content, three groups can be identified. All the Thioalkalimicrobium strains and some of the Thioalkalivibrio strains belonged to the moderate halophiles. Some of the Thioalkalivibrio strains from hypersaline soda lakes were extremely salt-tolerant and capable of growth in saturated soda brines. The Thioalkalimicrobium strains demonstrated relatively high specific growth rates, low growth yield, high maintenance, and extremely high rates of thiosulfate and sulfide oxidation. In contrast, the Thioalkalivibrio strains, in general, were slow-growing, high-yield organisms with lower maintenance and much lower rates of oxidation of sulfide and thiosulfate. Moreover, the latter survived starvation much better than Thioalkalimicrobium. Different growth characteristics and salt resistance appear to determine the outcome of the enrichment cultures from different soda lakes: Thioalkalimicrobium dominated in the enrichments with freshly obtained samples from diluted soda lakes at low-medium salinity, while Thioalkalivibrio was the predominant organism in enrichments from aged samples and at hypersaline conditions. In mixed thiosulfate-limited chemostat cultures at low salinity, Thioalkalimicrobium strains (mu(max)=0.33 h(-1)) out-competed Thioalkalivibrio strains (mu(max)=0.15 h(-1)) at D>0.02 h(-1). The overall results suggest that Thioalkalimicrobium and Thioalkalivibrio represent two different ecological strategies.

Bacteria↗
PubMed1983

The effects of several ligands on the potassium-vanadate interaction in the inhibition of the (Na+ + K+)-ATPase and the Na+, K+ pump.

Inhibition by vanadate of the K+-dependent p-nitrophenylphosphatase activity catalyzed by the (Na+ + K+)-ATPase partially purified from pig kidney showed competitive behavior with the substrate, K+ and Mg2+ acted as cofactors in promoting that inhibition. Ligands which inhibited the K+-dependent p-nitrophenyl phosphate hydrolysis (Na+, nucleotide polyphosphates, inorganic phosphate) protected against inhibition by vanadate. The magnitude of that protection was proportional to the inhibition produced in the absence of vanadate. In the presence of only p-nitrophenyl phosphate and Mg2+, or when the protective ligands were tested alone, the activation of p-nitrophenyl phosphate hydrolysis by K+ followed a sigmoid curve in the presence as well in the absence of vanadate. However, the combination of 100 mM NaCl and 3 mM ATP resulted in a biphasic effect of K+ on the p-nitrophenyl phosphate hydrolysis in the presence of vanadate. After an initial rise at low K+ concentration, the p-nitrophenylphosphatase activity declined at high K+ concentrations; this decline became more pronounced as the vanadate concentration was increased. This biphasic response was not seen when a nonphosphorylating ATP analog was combined with Na+ (which favors the nucleotide binding) or with inorganic phosphate (a requirement for K+ - K+ exchange). Experiments with inside-out resealed vesicles from human red cells showed that in the absence of Na+ plus ATP, K+ promoted vanadate inhibition of p-nitrophenylphosphatase activity in a nonbiphasic manner, acting at cytoplasmic sites. On the other hand, in the presence of Na+ plus ATP, the biphasic response of p-nitrophenyl phosphate hydrolysis is due to K+ acting on extracellular sites. In vanadate-poisoned intact red blood cells, the biphasic response of the ouabain-sensitive Rb+ influx as a function of the external Rb+ concentration failed to develop when there was no Na+ in the extracellular media. In addition, in the absence of extracellular Na+, external Rb+ did not influence the magnitude of inhibition. The present findings indicate that external K+ favors vanadate inhibition by displacing Na+ from unspecified extracellular membrane sites.

Biological Transport, Active↗