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Biomedical subjects

L Paulin

Publications and source records attributed to L Paulin.

63 records · Page 4Linked to original sources
PubMed1986

Cadaverine covalently linked to a peptidoglycan is an essential constituent of the peptidoglycan necessary for the normal growth in Selenomonas ruminantium.

Cadaverine links covalently to the D-glutamic acid residue of the peptidoglycan in Selenomonas ruminantium, a strictly anaerobic Gram-negative bacterium (Kamio, Y., Itoh, Y., and Terawaki, Y. (1981) J. Bacteriol. 146, 49-53). This report clarifies a physiological function of cadaverine in this organism by using DL-alpha-difluoromethyllysine, which had previously been shown to be a selective irreversible inhibitor of lysine decarboxylase of Mycoplasma dispar (Pösö, H., MaCann, P.P., Tanskanen, R., Bey, P., and Sjoerdsma, A. (1984) Biochem. Biophys. Res. Commun. 125, 205-210). DL-alpha-Difluoromethyllysine is now shown to be a potent and irreversible inhibitor of lysine decarboxylase of S. ruminantium in vitro; however, it did not inhibit the transfer of cadaverine to the alpha-carboxyl group of the D-glutamic acid residue of the peptidoglycan. DL-alpha-Difluoromethyllysine at 5 mM markedly inhibited the growth of the bacterium and caused rapid cell lysis. Immediately before the cell lysis, almost all cells became swollen, and such cells showed a loosened envelope structure when studied by electron microscopy. The peptidoglycan prepared from the DL-alpha-difluoromethyllysine-treated cells did not have covalently linked cadaverine. The growth inhibition by DL-alpha-difluoromethyllysine was completely reversed by adding cadaverine (1 mM) to the medium. Furthermore, the exogenous cadaverine was exclusively incorporated into the peptidoglycan in the presence of DL-alpha-difluoromethyllysine (5 mM), and a normal peptidoglycan was synthesized. The cell lysis and the formation of an abnormal cell structure were completely prevented by cadaverine added to the medium. We conclude that cadaverine covalently linked to the peptidoglycan in S. ruminantium is an essential constituent of the peptidoglycan and is required for cell surface integrity and the normal growth of S. ruminantium.

Alanine↗
PubMed1986

Reversible inhibition of flagella formation after specific inhibition of spermidine synthesis by dicyclohexylamine in Pseudomonas aeruginosa.

Dicyclohexylamine, which is an inhibitor of bacterial and mammalian spermidine synthase, greatly inhibited the synthesis of spermidine in Pseudomonas aeruginosa. The depletion of spermidine caused by dicyclohexylamine was accompanied by an inhibition of growth of bacteria. This inhibition was reversed by addition of 50 microM spermidine (but not putrescine or spermine) to growth medium. When its growth was inhibited Ps. aeruginosa also lost its motility. Electron microscopy showed a loss of flagella in spermidine-deficient bacteria: after 24 h 70% 85% of bacteria grown in the presence of dicyclohexylamine did not have flagella, whereas bacteria grown in the presence of dicyclohexylamine and spermidine had flagella. The loss of flagella was reversible, since after the inhibition of spermidine synthesis for 24 h, addition of 50 microM spermidine (but not putrescine or spermine) to the growth medium was able to restore the bacterial motility almost completely after a further 12 h growth period.

Cell Movement↗
PubMed1985

1-Aminooxy-3-aminopropane, a new and potent inhibitor of polyamine biosynthesis that inhibits ornithine decarboxylase, adenosylmethionine decarboxylase and spermidine synthase.

1-Aminooxy-3-aminopropane was shown to be a potent competitive inhibitor (Ki = 3.2 nM) of homogenous mouse kidney ornithine decarboxylase, a potent irreversible inhibitor (Ki = 50 microM) of homogeneous liver adenosylmethionine decarboxylase and a potent competitive (Ki = 2.3 microM) of homogeneous bovine brain spermidine synthase. It did not inhibit homogeneous bovine brain spermine synthase and it did not serve as a substrate for spermidine synthase. The compound did not inhibit tyrosine aminotransferase, alanine aminotransferase or aspartate aminotransferase, which are pyridoxal phosphate-containing enzymes like ornithine decarboxylase. The inactivation of adenosylmethionine decarboxylase was partially prevented by pyruvate, which is the coenzyme of adenosylmethionine decarboxylase, and by the substrate, adenosylmethionine. 1-Aminooxy-3-aminopropane at 0.5 mM concentration inhibited the growth of HL-60 promyelocytic leukemia cells and this inhibition was prevented by spermidine but not by putrescine.

Adenosylmethionine Decarboxylase↗
PubMed1983

GTP-insensitive ornithine decarboxylase in acetobacteria able to synthesize spermine.

Several Acetobacteria contained large amounts of spermine in addition to the putrescine and spermidine, which are the polyamines normally found in prokaryotes. A spermine synthase present in cell extracts of these Acetobacteria is the first example of this enzyme in prokaryotes. Dicyclohexylammonium sulphate inhibited both spermidine synthase and spermine synthase activities in Acetobacteria. Their ornithine decarboxylase was not stimulated by GTP nor inhibited by ppGpp and pppGpp (magic spots I and II) in contrast to ornithine decarboxylase of nearly all bacteria studied so far. However, their S-adenosyl-L-methionine decarboxylase resembled other prokaryotic adenosylmethionine decarboxylases in requiring Mg2+ ions in vitro for full activity.

Acetobacter↗
PubMed1983

Ornithine decarboxylase activity from an extremely thermophilic bacterium, Clostridium thermohydrosulfuricum. Effect of GTP analogues on enzyme activity.

The activity of ornithine decarboxylase has been detected for the first time in extracts of a thermophilic bacterium, Clostridium thermohydrosulfuricum. The temperature optimum of the thermoresistant ornithine decarboxylase was 55 degrees C and the pH optimum was 7.5. It required pyridoxal phosphate and a thiol (dithiothreitol) for activity. The activity of the enzyme was closely connected to the growth of the thermophilic bacteria, since the activity was highest during the logarithmic growth. The enzyme was not inhibited (in contrast to the enzyme from Escherichia coli) by putrescine, spermidine or other naturally occurring polyamines. When the effect of GTP and a number of GTP analogues was tested on the activity of the enzyme, it was observed that GTP or dGTP was necessary for the full activity. The modification of either the purine base or 5'-phosphate chain of GTP leads to a stimulation smaller than that caused by GTP. Modification of the 3'-carbon of the ribose part of GTP (magic spot I and II of Cashel and Gallant, Nature 221 (1969) 838-841) caused a distinct inhibition of the enzyme activity, indicating that ornithine decarboxylase contains at least two domains for binding of GTP. The enzyme was inhibited irreversibly by high concentrations (50 mM) of difluoromethylornithine. Extracts of the bacterium contained also arginine decarboxylase, but its activity was always very much lower than that of ornithine decarboxylase. The activity of arginine decarboxylase was inhibited irreversibly by difluoromethylarginine, which is an irreversible suicide inhibitor of bacterial arginine decarboxylase (Kallio, A., McCann, P.P. and Bey, P. (1981) Biochemistry 20, 3163-3166).

Carboxy-Lyases↗
PubMedDate not supplied

The secretory S complex in Bacillus subtilis is identified as pyruvate dehydrogenase.

We have cloned the operon for the Bacillus subtilis S complex, which has been suggested to be a component of the protein secretion machinery. The S-complex operon was found to encode 4 proteins, which were identified as subunits of pyruvate dehydrogenase (PDH). The Staphylococcus aureus membrane-bound ribosome protein (MBRP) complex has been considered to be a counterpart of the B. subtilis S complex. Here, we sequenced a fragment of the MBRP operon encoding the C-terminal part of E1 beta, the entire E2 and the N-terminal part of the E3 subunit of PDH, thus conclusively confirming the PDH identity of the MBRP complex as well. It appeared unlikely that PDH could be a primary component in protein secretion, thus disproving the previous hypothesis of the role of the S complex. However, attachment of the S complex (PDH) to the membrane and ribosomes may produce a biologically significant interaction.

Bacillus subtilis↗
PubMedDate not supplied

Cloning of the cDNA encoding rod photoreceptor cGMP-phosphodiesterase alpha and gamma subunits from the retinal degenerate Labrador retriever dog.

The nucleotide (nt) sequence of the cDNA encoding the retinal rod cyclic 3'5'-GMP phosphodiesterase (PDE) alpha and gamma subunits from two strains of dogs-(i) Labrador Retrievers homozygous for autosomally recessively inherited rod-cone degeneration and (ii) the wild-type Beagle-are reported. Cloning of these subunits was accomplished by polymerase chain reaction using retinal cDNA libraries as templates. The nt sequence of alpha PDE predicts a 861-amino-acid polypeptide which is 97.7 per cent and 96.9 per cent identical to the bovine and human counterparts, respectively. PDE gamma encodes an 87-amino-acid polypeptide differing from bovine and murine gamma subunits by only one amino acid. Since no differences were found between these two strains of dogs, the cause of the Labrador Retriever's degeneration remains to be determined.

3',5'-Cyclic-GMP Phosphodiesterases↗
PubMedDate not supplied

[Validazione della versione italiana del Brief Pain Inventory nei pazienti con dolore cronico].

BACKGROUND: The purpose of this study has been the validation of an Italian version of the Brief Pain Inventory (BPI), Breve Questionario per la valutazione del Dolore (BQVD), in patients with chronic pain not-caused by neoplastic illness. METHODS: The analysis has been proposed to 113 patients affected by different kinds of chronic pain of non-neoplastic origin while hospitalized, both as outpatients or as in-patients. The descriptive analysis of the specimen and of each item of the BPI has been carried out. Moreover, the psychometric characteristics of the analysis, intended as an instrument to describe intensity of pain and its interference in the various aspects of life have been investigated, evaluating with factorial analysis its validity both as a construct, and its internal coherence calculating the Cronbach's alpha of the whole instrument and of each identifier with factorial analysis. RESULTS: From the factorial analysis emerged a frame with three factors that have been identified as Pain intensity, Pain interference in emotional sphere and Interference in working activities. CONCLUSIONS: The Brief Pain Inventory can be considered a suitable useful instrument in the global evaluation of patients affected by chronic pain since its allows a contemporaneous analysis of three factors that characterize the phenomenon and contribute equally in defining the various facet of the pain universe. The Italian version of the BPI may be included in the essential evaluation instruments in the diagnosis and therapy of chronic pain.

Adult↗