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PubMed1984

Hypolipidemic activity of 3-N-(1',8'-Naphthalimido)propionic acid in rodents.

3-N-(1',8'-Naphthalimido)propionic acid was synthesized and shown to effectively lower both serum cholesterol and triglyceride levels in rats and mice. In hyperlipidemic mice, serum lipid levels were lowered significantly, approaching normal levels of cholesterol and below normal levels of triglyceride. The serum lipid levels were reduced due to accelerated clearance of cholesterol via the biliary route as well as a lowering of available acetyl CoA in the cytoplasm for liver de novo cholesterol and triglyceride syntheses. The liver regulatory enzyme of fatty acid and triglyceride syntheses were depressed by drug treatment. Significant reduction of liver lipids as well as the lipid content of the lipoprotein fractions were observed. The agent possessed a safe therapeutic index when used as a hypolipidemic agent.

Animals↗
PubMedDate not supplied

Induction of fetal hemoglobin by propionic and butyric acid derivatives: correlations between chemical structure and potency of Hb F induction.

Short-chain fatty acids (C2-C9) induce fetal hemoglobin synthesis in primary cell cultures, primates, and patients. We carried out experiments to test whether relationships exist between chemical structure and the Hb F-inducing potential of several short-chain fatty acid derivatives. BFUe cultures were performed in the presence of propionic and butyric congeners, covering the full spectrum of substitutions of these molecules, including polar and non-polar groups, esters, and double bonds. We found that the fetal hemoglobin inducibility is related to the chemical structure of the inducing compound. This structure-activity relation depends on the length of carbon chain, the nature of the substitutions, and the position of more potent substitutions on the carbon chain. It appears that substitutions enhancing the inducibility of these compounds are (with decreasing potency): methyl > phenyl > hydroxy >> amino groups. Placement of these substitutions at a position distal to the carboxyl group enhances gamma-globin inducibility. Presence of the carboxyl group is prerequisite for gamma-globin inducibility.

Butyrates↗
PubMedDate not supplied

Structure of the PCCA gene and distribution of mutations causing propionic acidemia.

Propionyl-CoA carboxylase (PCC, EC 6.4.1.3) is a mitochondrial, biotin-dependent enzyme that functions in the catabolism of branched-chain amino acids, fatty acids with odd-numbered chain lengths, and other metabolites. It catalyzes the ATP-dependent carboxylation of propionyl-CoA to d-methylmalonyl-CoA. PCC is composed of two types of subunits, likely as alpha4beta4 or alpha6beta6, with the alpha subunit containing the covalently bound biotin prosthetic group. A genetic deficiency of PCC activity causes propionic acidemia, a potentially fatal disease with onset in severe cases in the newborn period. Affected patients may have mutations of either the PCCA or PCCB gene. In this study, we have determined the structure of the human PCCA gene which, at the present time, is only partially represented in the databases. Based on reported ESTs and confirmed by RT-PCR, we also redefine the translation initiation codon to a position 75 nucleotides upstream of the currently accepted initiation codon. We show the distribution of mutations, including three identified in this study, and renumber all reported mutations to count from the new initiation codon. The gene spans more than 360 kb and consists of 24 exons ranging from 37 to 335 bp in length. The introns range in size from 104.bp to 66 kb. We have also determined the nucleotide sequence of approximately 1 kb of the 5'-flanking region upstream of the ATG translation initiation site. The proximal 400 bp of the 5'-flanking region shows a high G + C content (67%) and is part of a putative 1-kb CpG island that extends into exon 1 and part of intron 1. The putative promoter lacks a TATA box but contains two AP-1 sites and a conservatively defined consensus GC box, the latter characteristic of the core binding sequence of the Sp1 transcription factor.

Alternative Splicing↗
PubMed1995

A novel splicing mutation in propionic acidemia associated with a tetranucleotide direct repeat in the PCCB gene.

Propionic acidemia is an inborn error of organic acid metabolism caused by a deficiency of propionyl Coenzyme A (CoA) carboxylase. cDNAs sequenced from a beta subunit deficient Japanese patient (no. 187) showed an in-frame 57-bp deletion in one allele. Genomic DNA analysis revealed a four-nucleotide deletion of bases 3 to 6 in the 3' intron adjacent to the deleted exon, which disrupted the consensus 5' splice signal and caused exon skipping. This deletion removed one-half of a tetranucleotide direct repeat at the splice junction and presumably resulted from slipped mispairing.

Acyl Coenzyme A↗
PubMed1994

An iontophoretic study of the effects of alpha-amino-hydroxy-5-methyl-4-isoxazole propionic acid lesions of the nucleus basalis magnocellularis on cholinergic and GABAergic influences on frontal cortex neurones of rats.

Unilateral lesions of the nucleus basalis magnocellularis (NBM) produced by alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid in rats caused, 8-10 weeks after the lesion, a 94% reduction in cortical acetylcholinesterase fibres and reduced activities of acetylcholinesterase and choline acetyltransferase by 70-80% in the frontal cortex ipsilateral to the lesion. In anaesthetized unlesioned control rats, iontophoretic administration of acetylcholine and carbachol produced atropine-sensitive inhibition and excitation of frontal cortical neurones, effects similar to those produced by electrically stimulating the NBM. The lesion reduced cortical neuronal firing rates but increased the percentage and sensitivity of neurones responding to acetylcholine, the predominant response changing from inhibition to excitation; response duration increased but latency was unaffected. The size of the response of individual neurones to carbachol, but not the percentage of sensitive neurones, was also increased in lesioned animals. The proportion of neurones responding to bicuculline and their individual sensitivities were increased by the lesion, suggesting that the lesion increased GABAergic tone; responses to glutamate were unchanged. The lesion did not affect the proportion of neurones in which acetylcholine modulated neuronal responses but reversed the nature of the modulation to predominantly excitatory; excitation was the predominant response to electrical forepaw stimulation in unlesioned control animals. This suggests a possible interaction between GABAergic and cholinergic mechanisms in selective attention and processing of cognitive information. Acute administration of di-isopropyl fluorophosphate to unlesioned animals significantly increased the number of frontal cortical neurones responding to acetylcholine, without affecting individual neuronal sensitivity or responses to carbachol and glutamate. The similarity of these effects to those of acetylcholine in lesioned animals suggests that the increased sensitivity to acetylcholine in the latter was due to loss of acetylcholinesterase, enabling diffusion of acetylcholine to more distant neurones. However, acetylcholinesterase does not hydrolyse carbachol and therefore it is necessary to postulate a different post-synaptic mechanism to explain the lesion-induced increases in the sensitivities of individual neurones to carbachol and to acetylcholine; interpretation of experimental findings should take these two mechanisms into account.

Acetylcholine↗
PubMed1986

The influence of extracellular buffer concentration and propionate on lactate efflux from frog muscle.

Lactate efflux from frog sartorius muscles was measured following a lactate load of about 18 mumol X g-1 induced by a 4-min period of stimulation. Lactate efflux rate was buffer concentration dependent. The initial efflux rate increased from about 150 nmol X g-1 X min-1 in 1 mM MOPS buffer to 400 nmol X g-1 X min-1 in 25 mM MOPS buffer. The addition of 20 mM propionate reduced mean intracellular pH by about 0.2 units and increased lactate efflux rate by 70% at the highest buffer concentration and 400% at the lowest buffer concentration. The observed results are in reasonable agreement with predictions based on a model in which net efflux is limited by diffusion of both buffer and lactate in the extracellular space. Transmembrane lactate efflux appears to consist of two components, one of which is proton linked and carried either by undissociated lactic acid or coupled proton-lactate transport, the other being carried by independent lactate ions.

Animals↗
PubMed1980

Pharmacokinetics of 2-(p-methylallylaminophenyl) propionic acid, alminoprofene, in man after single and multiple oral doses.

2-(p-methylallylaminophenyl) propionic acid, alminoprofene (INN), a new antalgic drug, was administered orally to men as a single (300 mg) and multiple doses (300 mg three times daily). Plasma and urine concentrations of alminoprofene were determined by gas-liquid chromatography. After the single oral dose, the peak plasma level (36.2 to 41.5 mg/l) was reached within 0.5 -1.5 h. the biological half-life ranged from 2.5 to 3.2 h. During chronic administration of alminoprofene, steady-state equilibrium was established within 24 h. The urinary excretion of alminoprofene as unchanged product and as glucuronide was very important.

Administration, Oral↗
PubMed1995

The management and outcome of propionic and methylmalonic acidaemia.

The management of the severe variants of methylmalonic and propionic acidaemia remains difficult. With conventional therapy of diet, carnitine and antibiotics, mortality is high and long-term complications are common. Liver transplantation appears to be an important alternative.

Humans↗
PubMed1993

Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia.

Propionic acidaemia is an inborn error of organic acid metabolism caused by deficiency of propionyl-CoA carboxylase (PCC). Enzyme deficiency can result from mutations in either of the non-identical alpha- and beta-subunits. We have screened genomic DNA from patients with defects in the beta-subunit from two ethnic groups (Caucasians and Japanese) and detected three types of mutations in the same exon of the coding sequence of the beta-subunit: an insertion/deletion that replaces 14 nucleotides with 12 nucleotides of unrelated sequence and eliminates an Msp I site; a 3-bp deletion of a single isoleucine codon immediately proximal to that Msp I site; and a C-->T transition in the same Msp I site. The insertion/deletion was detected only in Caucasian patients in 11 of 34 mutant alleles; the C-->T transition was found only in Japanese patients in 4 of 12 mutant alleles. Following digestion of genomic DNA by Msp I, both of these mutations were detected on Southern blots by the presence of a 2.7-kbp band; they can be distinguished from one another by allele-specific oligonucleotide hybridization following PCR amplification. These results underscore the independent origin of the mutations in the two populations and suggest a key role of this exon in the beta-subunit of PCC.

Amino Acid Metabolism, Inborn Errors↗
PubMed1986

Direct identification of propionylcarnitine in propionic acidaemia: biochemical and clinical results of oral carnitine supplementation.

Urinary short-chain acylcarnitine in a patient with propionic acidaemia and low levels of free carnitine was found to consist mainly of propionylcarnitine. The compound was isolated by sequential paper and thin layer chromatography and identified by ammonia desorption chemical ionization mass spectrometry. Treatment of the patient with oral carnitine supplements led to a near-normalization of the plasma free carnitine concentrations and an increase in his muscle tone. The propionylcarnitine excretion rose and there was a simultaneous decrease in the methylcitrate output. Carnitine treatment did not prevent the occurrence of an episode of metabolic decompensation.

Amino Acid Metabolism, Inborn Errors↗
PubMed1992

Decreased selenium intake and low plasma selenium concentrations leading to clinical symptoms in a child with propionic acidaemia.

A child with biotin-non-responsive propionic acidaemia treated with a propiogenic amino acid-restricted diet presented with an elevated blood mean corpuscular volume (MCV) of 93.1 fl, indicative of macrocytosis, and unusual hair texture with hypopigmentation. Plasma selenium concentration at this time was subnormal (45.9 micrograms/L), and calculated dietary selenium intake was 4.7 micrograms/day. After 4 months of selenium supplementation (50 micrograms/day) plasma selenium concentration normalized (97.7 micrograms/L) in conjunction with a reduced MCV (84.0 fl) and a dramatic improvement in hair growth, colour and length. Two additional periods off and on selenium supplementation, of varying time intervals, resulted in similar clinical changes. We conclude that these clinical changes were due to a deficient intake of dietary selenium.

Amino Acid Metabolism, Inborn Errors↗
PubMed1980

Propionic acidaemia presenting with pancytopaenia in infancy.

A 2-month-old infant presented with vomiting, lethargy and pancytopaenia. She was found to have propionic acidaemia, and the activity of propionyl-CoA carboxylase in cultured fibroblasts was defective (McKusick 23200). Abnormal amounts of glycine, 3-hydroxypropionate, methylcitrate, tiglyglycine, propionylglycine, 2-methylacetoacetate, 2-methyl-3-hydroxybutyrate, 3-oxovalerate and 3-hydroxyvalerate were found in body fluids. It appears that the organic acidaemia leads to an inhibition in the maturation of cells in the bone marrow.

Amino Acid Metabolism, Inborn Errors↗
PubMed1988

Forced synthesis of trace amounts of juvenile hormone II from propionate by corpora allata of a juvenile hormone III-producing insect.

Corpora allata of the cockroach Diploptera punctata normally synthesize only the isoprenoid juvenile hormone III (JH III). Only under extreme in vitro conditions (absence of carbon sources other than propionate) do they produce trace amounts of the homoisoprenoid JH II in addition to JH III. The specificity of the in vitro synthesis of JH III by D. punctata is thus consistent with the observed lack of homoisoprenoid JHs in this insect.

Animals↗
PubMed1992

Three cases of opportunistic infection caused by propionic acid producing Corynebacterium minutissimum.

Propionic acid producing strains of Corynebacterium minutissimum were isolated from three patients with opportunistic infections. One neutropenic patient was undergoing chemotherapy for prolymphocytic leukemia; the other two patients were undergoing hemodialysis and peritoneal dialysis respectively. An unusual feature of these three strains was their resistance to several antibiotics, which is seldom seen in diphtheroids other than Corynebacterium jeikeium and CDC group D2.

Aged↗
PubMed1982

Increased excretion of four acetyl-CoA precursors during clinical episode of propionic acidaemia.

Propionic acidaemia (McKusick 23200) is caused by reduced activity of propionyl-CoA carboxylase (EC 6.4.1.3). A number of metabolites characteristic of this disease are excreted in patients' urine. We have developed a method of chemical diagnosis using gas chromatography-mass spectrometry (GC-MS). Since our first chemical diagnosis (Matsumoto et al., 1978), we have diagnosed seven patients. Profiles of urinary acids, however, varied from patient to patient. Factors affecting these profiles may be genetic make-up, age, or the patient's clinical and nutritional conditions. We have compared two metabolic profiles of a girl under different clinical conditions and found increased excretion of acetyl-CoA precursors during clinical episodes.

Acetyl Coenzyme A↗
PubMed1980

Combined iminoglycinuria and cystine- and dibasic aminoaciduria in patients with propionic acidaemia and 3-methylcrotonylglycinuria.

Urinary amino acids have been determined in six patients with propionic acidaemia, one of whom also showed 3-methylcrotonylglycinuria. Two patients, including the subject with 3-methylcrotonylglycinuria, showed a gross aminoaciduria with features of both cystinuria and iminoglycinuria. We suggest a defect in certain amino acid transport systems in some patients with these disorders.

Amino Acid Metabolism, Inborn Errors↗