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The role of net charge on the renaturation of reduced lysozyme by the sulfhydryl-disulfide interchange reaction.

Reduced and acetylated lysozymes are basic proteins. When their amino groups were variously acetylated and then renatured by sulfhydryl-disulfide (SH-SS) interchange reaction at pH 8.0, the final folding yield decreased as the number of positive charges decreased. The final folding yield of native and Ac1 lysozyme, with one positive charge eliminated, was less sensitive to increasing protein concentration than that of Ac2 lysozyme, where two positive charges had been eliminated. The final folding yield of reduced Ac2 lysozyme increased in the presence of 1 M urea, which reduced the aggregation of unfolded lysozyme. Thus, the aggregation of unfolded lysozymes, which leads to a decrease in the final folding yield, was found to be heavily dependent on their net charges. Moreover, the final folding yield of reduced lysozyme was shown to be increased by use of cystamine as an oxidizing reagent in comparison with 2-hydroxyethyl disulfide or dithiodiglycolic acid. This may support the idea that the final folding yield is influenced by electrostatic interaction between unfolded lysozymes in the early stage of renaturation. In contrast, the concentration dependency of the final folding yield of Ac1 lysozyme was different from those of carboxymethylated His15 and Asp106 lysozymes whose positive net charges were similar to that of Ac1 lysozyme. On the basis of the observations, it is suggested that the formation of the aggregates in the renaturation process might also be affected by the structure of the unfolded state of lysozyme in solution.

Acetylation↗

In vitro nitric oxide effects on basal and gonadotropin-releasing hormone-induced gonadotropin secretion by pituitary gland of male crested newt (Triturus carnifex) during the annual reproductive cycle.

The objective of this study was to test the possible nitric oxide (NO) involvement in pituitary gonadotropin secretion in the male crested newt, Triturus carnifex. Pituitaries were incubated in vitro with medium alone, GnRH, NO donor (NOd, sodium nitroprusside), NO synthase inhibitor (NOSi, Nomega-nitro-L-arginine methyl ester), cGMP analogue (cGMPa, 8-bromo-cGMP), soluble guanylate cyclase inhibitor (sGCi, cystamine), GnRH plus NOSi, GnRH plus sGCi, and NOd plus sGCi during the annual reproductive cycle: pre-reproduction, reproduction (noncourtship and courtship), and the refractory, recovery, and estivation periods. To determine pituitary gonadotropin secretion indirectly, newt testes were superfused in vitro with preincubated pituitaries, and androgen release was determined. NO synthase (NOS) activity and cGMP levels were assessed in the preincubated pituitaries. Medium alone- and GnRH-preincubated pituitary increased androgen secretion during pre-reproduction, noncourtship, courtship, and recovery; the GnRH-induced increase was higher than the medium alone-induced increase during pre-reproduction, noncourtship, and recovery. NOd and cGMPa increased androgens in all reproductive phases considered except courtship; the NOd- and cGMP-induced increase was higher than the medium alone-induced increase during pre-reproduction, noncourtship, and recovery. NOS activity was highest during courtship and lowest during the refractory and estivation periods. GnRH increased NOS activity during pre-reproduction, noncourtship, and recovery. Cyclic GMP levels were highest during courtship and lowest during the refractory period and estivation. GnRH increased cGMP levels during pre-reproduction, noncourtship, and recovery, while NOd did so during all reproductive phases considered. These results suggest that basal and GnRH-induced gonadotropin secretion are up-regulated by NO in the pituitary gland of the male Triturus carnifex.

Androgens↗

Nitric oxide-stimulated increase in intracellular cGMP modulates gap junction coupling in rat neocortex.

In the present study we demonstrate that gap junction coupling between developing layer II/III pyramidal cells in rat sensorimotor cortex is strongly modified by the nitric oxide (NO)/cyclic guanosine monophosphate (cGMP) system. Dye coupling was revealed by intracellular injection of the gap junction-permeable tracer neurobiotin into single neurones. Following incubation of slices with sodium nitroprusside, a source of NO, the size of dye-coupled cell clusters was significantly reduced. In many cases, 2-3 cells remained strongly dye-coupled. These effects were blocked by intracellular injection of the guanylyl cyclase inhibitor cystamine and mimicked by both application of the membrane-permeant cGMP analogue 8-Br-cGMP and intracellular injection of cGMP. cGMP injection also induced a 60% increase in neuronal input resistance. These results indicate that NO modulates gap junction coupling in the developing neocortex via stimulation of guanylyl cyclase.

Animals↗

Stimulation of h(2)s emission from pumpkin leaves by inhibition of glutathione synthesis.

The effect of inhibitors of glutathione (GSH) synthesis, namely gamma-methyl glutamic acid, d-glutamic acid, cystamine, methionine-S-sulfoximine (MSX), buthionine-S-sulfoximine, and GSH itself, on the emission of H(2)S was investigated. All these compounds stimulated H(2)S emission from pumpkin (Cucurbita pepo L. cv Small Sugar Pumpkin) leaf discs in response to sulfate. MSX and GSH were the most effective compounds, stimulating H(2)S emission from leaf discs of mature pumpkin leaves by about 80% in response to sulfate. Both inhibitors did not appreciably enhance H(2)S emission in response to l-cysteine and inhibited H(2)S emission in response to sulfite.Treatment with MSX or GSH enhanced the uptake of sulfate by pumpkin leaf discs, but did not affect the incorporation of sulfate into reduced sulfur compounds. Inhibition of GSH synthesis by MSX or GSH caused an increase in the pool size of cysteine, and, simultaneously, reduced the incorporation of labeled sulfate into cysteine. The incorporation of labeled sulfate into the sulfite and sulfide pools of the cells are stimulated under these conditions.These observations are consistent with the idea that inhibition of GSH synthesis leads to an elevated cysteine pool that inhibits further cysteine synthesis. The H(2)S emitted under these conditions appears to arise from diversion of a precursor of the sulfur moiety of l-cysteine. Therefore, stimulation of H(2)S emission in response to sulfate upon inhibition of GSH synthesis may reflect a role of H(2)S emission in keeping the cysteine concentration below a critical level.

Journal Article↗

Origin of acetate in spinach leaf cell.

Mitochondria were isolated from spinach (Spinacia oleracea L.) leaves using a Percoll gradient step. The high purity of the organelle fraction is demonstrated by electron microscopy and biochemical parameters. In the matrix space of these mitochondria, a short-chain acyl-coenzyme A hydrolase is present that converts acetyl-coenzyme A to acetate and coenzyme A with reasonable rates (K(m), 150 micromolar; V(max), 140 nanomoles acetate formed milligram(1) protein hour(-1)). The enzyme is product inhibited by coenzyme A-sulfhydryl, other thiols are ineffective; however, the disulfides 5,5'-dithio-bis-(2-nitrobenzoate) and cystamine stimulate the hydrolysis. The possible role of this mitochondrial enzyme as a means of generating free acetate from pyruvate via acetyl-coenzyme A in the mitochondria of mature spinach leaves is discussed. It is suggested that free acetate moves rapidly from the mitochondrion to the chloroplast where acetyl-coenzyme A synthetase, solely localized in this organelle, converts the metabolically inert free acetate to the highly active acetyl-coenzyme A.

Journal Article↗

Stable expression of transfected human involucrin gene in various cell types: evidence for in situ cross-linking by type I and type II transglutaminase.

Involucrin is a 68-kd precursor of the cornified envelope in keratinocytes. During terminal differentiation, involucrin becomes covalently cross-linked to other proteins by a membrane-anchored calcium-activated transglutaminase (TG) to form part of the cornified envelope. To better understand this process, we have used vector-mediated gene transfer to express human involucrin in a variety of cell types. Authentic involucrin protein was expressed in Chinese hamster ovarian (CHO) cells (fibroblasts), PtK2 rat kangaroo kidney cells (simple epithelial), and rat epidermal keratinocytes (stratifying squamous epithelial). The expression vector included an independent transcription unit encoding the aminoglycoside phosphotransferase gene (neo-r) allowing selection of stable involucrin-positive, G418-resistant clonal cell lines. In each cell type, involucrin levels were comparable to the endogenous expression observed in SCC-13 cells. Immunofluorescence localization studies revealed a uniform involucrin distribution throughout the cytoplasm in each cell type. Elevation of intracellular calcium resulted in cross-linking of involucrin in both CHO cells and rat keratinocytes, a process that was inhibited by EDTA and cystamine. In contrast, no cross-linking was observed in PtK2 cells or long-term passaged rat keratinocytes. Transglutaminase assays showed that rat keratinocytes contain predominantly a particulate (type I) form, whereas CHO cells contain only soluble TG (type II). PtK2 cells and long-term passaged keratinocytes, which were unable to cross-link involucrin, contained barely detectable TG activity. These results indicate 1) that involucrin is an efficient in situ substrate for both type I and type II transglutaminase and 2) that involucrin cross-linking is strictly TG dependent.

Animals↗

ATP-independent proteolysis of globin cyanogen bromide peptides in rabbit reticulocyte cell-free extracts.

The catabolism of two rabbit globin cyanogen bromide peptides in cell-free extracts of ATP-depleted rabbit reticulocytes has been studied. Proteolysis of the peptides (3533 and 5957 molecular weight) proceeded rapidly in the absence of ATP, had a pH optimum of approximately 7.8, and was inhibited by omicron-phenanthroline, N-ethylmaleimide, cystamine zinc and cobalt ions, and puromycin peptide high-molecular-weight aggregates. Proteolysis of puromycin peptides was inhibited by the rabbit globin cyanogen bromide peptides. The ability of cell-free extracts of degrade the globin cyanogen bromide peptides decreased with the reticulocyte maturity. Blocking the globin cyanogen bromide peptide amino groups by succinic and maleic anhydride treatment decreased susceptibility to degradation. It is suggested that the globin cyanogen bromide peptides might provide model substrates, replacing puromycin peptides, for the investigation of ATP-independent proteolytic events.

Adenosine Triphosphate↗

Precise localization of several covalent RNA-RNA cross-link in Escherichia coli 16S RNA.

The RNA-RNA cross-linking reagent N-acetyl-N'-(p-glyoxylyl-benzoyl)cystamine, which reacts via its glyoxal residue with guanines not involved in G X C base pairs, has been used to introduce reversible RNA-RNA cross-links into Escherichia coli 16S rRNA. A two-dimensional gel method has been devised for the separation of the cross-linked oligonucleotides, and the precise location of guanines involved in four of these cross-links has been determined by sequencing the oligonucleotides. One cross-link involves guanosines 1315 and 1360 situated in two hairpin end loops of domain III. The other cross-links involves pairs of guanosine situated within the same hairpin end loops.

Base Composition↗

A kinetic study on pantetheinase inhibition by disulfides.

The mammalian enzyme pantetheinase, which hydrolyzes pantetheine to pantothenic acid and cysteamine, is inhibited by many thiol reagents and activated by thiols. Two thiol groups of different reactivity and accessibility are involved in the catalytic process [Ricci, G., Nardini, M., Chiaraluce, R., Duprè, S. & Cavallini, D. (1986) Biochim. Biophys. Acta 870, 82-91]. The inhibition kinetics by some natural and synthetic disulfides [pantethine, cystamine, 5,5'-dithiobis(2-nitrobenzoic acid), 4,4'-dithiodipyridine and oxidized mercaptoethanol] has been studied by two experimental approaches, either by monitoring activity after incubation of the enzyme with the inhibitor or by determining the progress curves in the presence of substrate and inhibitor. Data reported here indicate that pantetheinase reacts irreversibly with various disulfides in a time-dependent manner with the formation of a mixed disulfide apparently preceeded by a conformational change, giving a modified E* form with new kinetic parameters. This modified form may be further competitively inhibited by disulfides interacting with the enzyme at the active site.

Amidohydrolases↗

Alteration of cerebral taurine biosynthesis in spontaneously hypertensive rats.

Cerebral taurine biosynthesis in a spontaneously hypertensive rat (SHR) has been studied. Cysteine sulfinic acid (CSA) and cysteic acid (CA), possible key intermediates in taurine biosynthesis, were found in the rat brain, whereas no cysteamine-cystamine was detected. In the brain of SHR, a statistically significant decrease in the contents of CSA, CA, and taurine was noted in the cerebellum, hypothalamus, and striatum as compared with normotensive Wistar Kyoto rats. Similarly, it was demonstrated that the activity of cysteine dioxygenase, the enzyme catalyzing cysteine to CSA, was attenuated significantly in the same brain areas of SHR. In contrast, no alteration in the activity of CSA decarboxylase, the enzyme converting CSA to hypotaurine or CA to taurine, was observed. A decline in the percent conversion of [14C]cysteine to [14C]taurine was found also in tissue homogenates from the cerebellum, hypothalamus, and striatum of SHR, indicating that the declines in taurine content may be due to an attenuation of taurine biosynthesis, possibly at the step involving cysteine dioxygenase.

Animals↗

Non-adrenergic, non-cholinergic relaxation of the bovine retractor penis muscle: role of S-nitrosothiols.

1. This study examined the possibility that an S-nitrosothiol, rather than nitric oxide, functions as the non-adrenergic, non-cholinergic (NANC) inhibitory neurotransmitter in the bovine retractor penis (BRP) muscle. 2. Treatment of BRP muscle with either of two sulphydryl inactivating agents, diamide (1 mM) and N-ethylmaleimide (0.3 mM), inhibited NANC relaxation and this was prevented by pretreating tissues with L-cysteine (3 mM), L-glutathione (3 mM) or dithiothreitol (3 mM). Inhibition was not specific, however, since the inactivating agents also inhibited the relaxant actions of authentic nitric oxide (0.3 microM), glyceryl trinitrate (0.001-1 microM) and isoprenaline (0.01-1 microM). 3. Reacting nitric oxide with L-cysteine in nominally oxygen-free solution at pH 3, followed by purging to remove free nitric oxide and neutralisation, produced greater and more prolonged relaxant activity when assayed on rabbit aortic rings than could be attributed to nitric oxide alone. H.p.l.c. analysis of the mixture identified a new peak distinct from either L-cysteine or nitric oxide which was responsible for the relaxant activity. The spectral absorption of this new compound had two bands with peaks at 218 and 335 nm. 4. Using a series of structural analogues of L-cysteine (all at 15 mM) it was found that removal of the carboxyl group (L-cysteamine), replacement of the carboxyl with an ester function (L-cysteine methyl ester) or substitution at the amino group (N-acetyl-L-cysteine) had no effect on the ability to generate relaxant activity upon reaction with nitric oxide (0.1 mM). In contrast, substitution at the sulphydryl group (S-methyl-L-cysteine, L-cysteinesulfinic acid and L-cysteic acid), or formation of disulphides(L-cystine and L-cystamine) led to a complete loss of ability to generate relaxant activity. L-Glutathione was also able to react with nitric oxide to produce relaxant activity, and this too was blocked upon substitution of the free sulphydryl group (S-methyl-L-glutathione). A free sulphydryl group was therefore required to generate relaxant activity following reaction with nitric oxide.5. Reacting L-cysteine (10 mM) with nitric oxide (~ 3 mM) under more stringent oxygen-free conditions followed by purging to remove free nitric oxide resulted in the generation of low relaxant activity and small absorption peaks at 218 and 335 nm and these were unaffected upon exposure to the air. In contrast, admitting air to the reaction chamber before purging enhanced both relaxant activity and the absorption peaks at 218 and 335 nm by some 40 fold and the solution turned pink due to the appearance of another absorption peak at 543 nm. This enhanced relaxant activity was not due to nitrogen dioxide being the reactive species, since at 0.1 mM this gas failed to react with L-cysteine to generate relaxant activity, and at 1 mM generated less activity than the equivalent concentration of nitricoxide.6. The relaxant activity generated by reacting nitric oxide with L-cysteine or L-glutathione was abolished following treatment with haemoglobin (3 MicroM), methylene blue (10 MicroM) or Nmethylhydroxylamine(100 MicroM), but was unaffected by N0-nitro-L-arginine (30 MicroM). Furthermore, two agents that generate superoxide anion, pyrogallol (0.1 mM) and hydroquinone (0.1 mM), also inhibited this relaxant activity as well as that induced by authentic nitric oxide (0.3 MicroM) but as previously reported, had no effect on relaxation induced by NANC nerve stimulation. Superoxide dismutase(100 u ml1) reversed the actions of pyrogallol and hydroquinone but had no effect on NANC relaxation.7. In conclusion, the reaction of nitric oxide with L-cysteine or L-glutathione generates relaxant activity which exceeds that of nitric oxide alone and probably results from formation of S-nitrosocysteine and S-nitrosoglutathione, respectively. The effects of pyrogallol and hydroquinone suggest that the NANCneurotransmitter is a superoxide anion-resistant, nitric oxide-releasing molecule and that neither S-nitrocysteine nor S-nitrosoglutathione is a suitable candidate for this.

Animals↗

Cysteine stimulation of glucose oxidation in thyroid tissue.

Oxidation of D-glucose-C(14) by bovine thyroid slices was stimulated by cysteine, 2-aminoethanethiol, and cystamine. Amino acids tested, other than cysteine, were not stimulatory, except tyrosine and arginine to a slight degree. The pattern of stimulation resembled that brought about by thyroid-stimulating hormone. Stimulation of labeled CO(2) production was greater when glucose-1-C(14) rather than glucose-6-C(14) was the substrate.

Amino Acids↗

Cysteamine: differential x-ray protective effect on Chinese hamster cells during the cell cycle.

Cysteamine present during x-irradiation protects synchronized Chinese hamster cells in culture against lethal damage at all stages of the cell cycle. The effect is greatest for cells irradiated at sensitive stages such as G(1) and least for resistant cells; for example, late S (dose-modifying factors 4.2 and 2.7, respectively). The effect of 50 millimolar cysteamine is to render almost invariant the normally variant x-ray age response for lethality. This suggests that there are two components of x-ray damage, only one of which is age dependent, and it is against this component that cysteamine protects the cell. Cystamine, however, has no protective effect upon these cells at any stage of the cell cycle.

Animals↗

Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent.

Pineal N-acetyltransferase can be inactivated in broken cell preparations by cystamine through a mechanism of thiol-disulfide exchange. Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin. These findings suggest that a disulfide-containing peptide with high reactivity toward N-acetyltransferase may participate in the intracellular regulation of this enzyme.

Acetyltransferases↗

Interferon induction by radioprotective mercaptoalkylamines and derived thiophosphates.

Radioprotective thiols (five mercaptoalkylamines and four derived thiophosphates) induced interferon and resistance to virus infection. Interferon production occurred in human and mouse nonlymphoid cell cultures. One of the thiols, S,2-aminoethylisothiourea, given intraperitoneally, protected mice against two unrelated viruses--Semliki forest virus and Herpesvirus hominis type 1. Two structurally different radioprotective thiols--the disulfide cystamine and L-cysteine--were unable to induce the firus resistance state or interferon.

Animals↗

Intestinal receptor for heat-stable enterotoxin of Escherichia coli is tightly coupled to a novel form of particulate guanylate cyclase.

A novel form of particulate guanylate cyclase tightly coupled by cytoskeletal components to receptors for heat-stable enterotoxin (ST) produced by Escherichia coli can be found in membranes from rat intestinal mucosa. Intestinal particulate guanylate cyclase was resistant to solubilization with detergent alone, with only 30% of the total enzyme activity being extracted with Lubrol-PX. Under similar conditions, 70% of this enzyme was solubilized from rat lung membranes. The addition of high concentrations of sodium chloride to the extraction buffer resulted in greater solubilization of particulate guanylate cyclase from intestinal membranes. Although extraction of intestinal membranes with detergent and salt resulted in greater solubilization of guanylate cyclase, a small fraction of the enzyme activity remained associated with the particulate fraction. This activity was completely resistant to solubilization with a variety of detergents and chaotropes. Particulate guanylate cyclase and the ST receptor solubilized by detergent retained their abilities to produce cyclic GMP and bind ST, respectively. However, ST failed to activate particulate guanylate cyclase in detergent extracts. In contrast, guanylate cyclase resistant to solubilization remained functional and coupled to the ST receptor since enzyme activation by ST was unaffected by various extraction procedures. The possibility that the ST receptor and particulate guanylate cyclase were the same molecule was explored. ST binding and cyclic GMP production were separated by affinity chromatography on GTP-agarose. Similarly, guanylate cyclase migrated as a 300,000-dalton protein, while the ST receptor migrated as a 240,000-dalton protein on gel filtration chromatography. Also, thiol-reactive agents such as cystamine and N-ethylmaleimide inhibited guanylate cyclase activation by ST, with no effect on receptor binding of ST. These data suggest that guanylate cyclase and the ST receptor are independent proteins coupled by cytoskeletal components in membranes of intestinal mucosa.

Animals↗

Group B Streptococcus capsular polysaccharide-cholera toxin B subunit conjugate vaccines prepared by different methods for intranasal immunization.

Group B Streptococcus (GBS) type III capsular polysaccharide (CPS III) was conjugated to recombinant cholera toxin B subunit (rCTB) using three different methods which employed (i) cystamine and N-succinimidyl-3-(2-pyridyldithio)propionate (SPDP), (ii) carbodiimide with adipic acid dihydrazide (ADH) as a spacer, or (iii) reductive amination (RA). The CPS III-rCTB conjugates were divided into large- and small-molecular-weight (M(r)) fractions, and the immunogenicities of the different preparations after intranasal (i.n.) immunization were studied in mice. Both large- and small-M(r) conjugates of CPS III-rCTB(RA) or CPS III-rCTB(ADH) induced high, almost comparable levels of CPS-specific immunoglobulin G (IgG) in serum, lungs, and vagina that were generally superior to those obtained with CPS III-rCTB(SPDP) conjugates or a CPS III and rCTB mixture. However, the smaller-M(r) conjugates of CPS III-rCTB(RA) or CPS III-rCTB(ADH) in most cases elicited a lower anti-CPS IgA immune response than the large-M(r) conjugates, and the highest anti-CPS IgA titers in both tissues and serum were obtained with the large-M(r) CPS III-rCTB(RA) conjugate. Serum IgG anti-CPS titers induced by the CPS III-rCTB(RA) conjugate had high levels of specific IgG1, IgG2a, IgG2b, and IgG3 antibodies. Based on the effectiveness of RA for coupling CPS III to rCTB, RA was also tested for conjugating GBS CPS Ia with rCTB. As for the CPS III-rCTB conjugates, the immunogenicity of CPS Ia was greatly increased by conjugation to rCTB. Intranasal immunization with a combination of CPS Ia-rCTB and CPS III-rCTB conjugates was shown to induce anti-CPS Ia and III immune responses in serum and lungs that were fully comparable with the responses to immunization with the monovalent CPS Ia-rCTB or CPS III-rCTB conjugates. These results suggest that the GBS CPS III-rCTB and CPS Ia-rCTB conjugates prepared by the RA method may be used in bivalent and possibly also in multivalent mucosal GBS conjugate vaccines.

Administration, Intranasal↗

Beta-lactam biosynthesis in a gram-negative eubacterium: purification and characterization of isopenicillin N synthase from Flavobacterium sp. strain SC 12.154.

The occurrence, localization, and extraction of isopenicillin N-synthase (IPNS) were investigated in the gram-negative low-level beta-lactam producer Flavobacterium sp. strain SC 12.154, which forms deacetoxycephalosporin and excretes the cephabacin 7-formamidocephalosporin. IPNS was detected with anti-IPNS antibodies raised against the Cephalosporium acremonium enzyme. The flavobacterium enzyme, whose molecular mass (38 kilodaltons) and cofactor requirements resemble those of the fungal and Streptomyces enzymes, is formed at the transition from growth to the stationary phase. It was extracted into the polyethylene glycol phase of a polyethylene glycol-Ficoll-dextran three-phase system and was purified by quaternary aminoethyl ion-exchange chromatography, gel filtration, covalent chromatography on cystamine-Sepharose, and fast-protein liquid chromatography on Mono Q. The enzyme was characterized with respect to sulfhydryl requirement, inhibition by disulfides and metal ions, pH and temperature dependence, and stimulation by polyethylene glycol and low Triton X-100 concentrations, as well as by several amino acids, including alpha-aminoadipic acid and cysteine. The Km for alpha-aminoadipyl-cysteinyl-D-valine was 0.08 mM. An inactive membrane-associated form of IPNS was detected together with a beta-lactamase active on isopenicillin N. The system has been suggested as a model for the study of endogenous functions of beta-lactams in bacteria.

Blotting, Western↗