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Biomedical subjects

I Matsuda

Publications and source records attributed to I Matsuda.

At least 253 records · Page 14Linked to original sources
PubMed1990

Carnitine status and blood ammonium levels in low birth weight infants.

Forty-three low birth weight infants appropriate for gestational age (AGA) were monitored to evaluate carnitine status in relation to blood ammonium levels. The infants were grouped into three depending on blood ammonium level on postnatal day 7: 62.9 +/- 3.8 mumol/L in group 1 (N = 13), 38.9 +/- 8.4 mumol/L in group 2 (N = 23), and 24.5 +/- 2.9 mumol/L in group 3 (N = 9). Plasma free carnitine levels decreased in all three groups (p less than 0.001) and plasma short chain acylcarnitine increased only in group 1 (p less than 0.002), compared to findings in normal infants. The blood ammonium level positively and negatively correlated to plasma short chain acylcarnitine (p less than 0.002) and plasma free carnitine levels (p less than 0.002), respectively. The reabsorption rate of free carnitine in renal tubules (RRFC) was decreased at rates of 37.5, 27.5, and 25% of infants in groups 1, 2, and 3, respectively. The acylcarnitine/free carnitine clearance ratio (RAFCC) was decreased in groups 1 (p less than 0.01) and 2 (p less than 0.05) compared with group 3. Thus, an accumulation of short chain acyl moieties and insufficiency in renal absorption of free carnitine are putative causes of lowered plasma free carnitine in infants with higher blood levels of ammonium. The possibility that the carnitine status regulates blood ammonium levels in low birth weight infants warrants continued investigation.

Ammonia↗
PubMed1990

Oral supplementation of vitamin K for pregnant women and effects on levels of plasma vitamin K and PIVKA-II in the neonate.

Levels of plasma vitamin K1 (VK1) and vitamin K2 (VK2) and protein-induced vitamin K absence-II (PIVKA-II) were measured in Japanese mothers and their newborn (N = 33). Twenty milligrams of VK1 (N = 11) or VK2 (N = 12) were given orally to randomly selected mothers 7 to 10 days prior to delivery. Means of plasma VK1 and VK2 concentrations were significantly higher in VK1 (p less than 0.01) and VK2 (p less than 0.01) treated mothers than in the controls at delivery, respectively. Similarly, these levels were significantly elevated in cord plasma in VK1 (p less than 0.05) and VK2 (p less than 0.05) treated groups, compared with findings in the control group, although there was a large concentration gradient between maternal and cord plasma (mostly less than one-tenth). A significant positive correlation was found in VK1 concentration between maternal and cord plasma (N = 33, p less than 0.01), and the proportion of PIVKA-II-positive infants was significantly lower in the VK treated groups than in the control group at birth (p less than 0.05). On the fifth postnatal day, mean levels of VK1 (p less than 0.01) and VK2 (p less than 0.01) in breast milk were significantly higher in the VK1 and VK2 treated mothers than in the control mothers, respectively. In the control group, 9 of 10 infants had a positive PIVKA-II, but no one in the treated groups was positive, thereby indicating significant differences between control and treated groups (p less than 0.01 and p less than 0.01, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Oral↗
PubMed1990

Elevated expression of proto-oncogenes during interleukin-5-induced growth and differentiation of murine B lineage cells.

Interleukin 5 (IL-5), a lymphokine produced by helper T cells, is involved in the regulation of growth and differentiation of B cells and other hematopoietic cells. To elucidate IL-5-mediated intracellular mechanisms, we have established IL-5-dependent and -independent murine early B cell lines, J6 and MJ88-1, respectively, and examined the effect of IL-5 on the expression of proto-oncogenes during proliferation. Two- to 3.5-fold increases in the levels of c-myb, c-myc, c-fos, and c-fms mRNA were observed in J6 cells, compared with those in MJ88-1 cells. Further, a role of IL-5 in the proto-oncogene expression during differentiation was examined by using thymidine-treated murine B-cell chronic leukemia BCL1-B20 cells with growth arrest. After 4-day culture, the amount of IgM secreted from BCL1-B20 cells was augmented 4-6 fold in the presence of IL-5. Although expression of c-myb, c-fos, and c-fms mRNA did not change, only c-myc mRNA expression was elevated within 30 min of stimulation with IL-5 and reached a maximal level by 1 hr. Addition of phorbol 12-myristate 13-acetate (PMA) or IL-4 to the culture of BCL1-B20 cells inhibited both the IL-5-mediated augmentation of IgM secretion and the elevated expression of c-myc mRNA. These findings suggest that the IL-5 signal may be associated with the up-regulation of c-myc expression.

Animals↗
PubMed1990

A case of severe pituitary dwarfism associated with prolactin and thyroid stimulating hormone deficiencies.

An extreme dwarf 10-year-old boy was described. His clinical features resemble those of isolated GH deficiency type 1A, but the Southern blot analysis showed no gross deletion in the GH structural gene. Endocrinological evaluations showed severe GH and PRL deficiencies, and mild TSH deficiency. The simultaneous deficiencies of anterior pituitary hormones in our patient resemble those of the Snell and Ames dwarf mice and suggest a common etiology. The evolutionary and embryological similarities between GH and PRL imply that mutations at a gene which controls GH and PRL production in somatotropes and lactotropes or at a gene of which product affects the embryological development from a common ancestral cell in the anterior pituitary gland may be a primary defect in our patient.

Animals↗
PubMed1990

Biochemical basis of prolidase deficiency. Polypeptide and RNA phenotypes and the relation to clinical phenotypes.

Cultured skin fibroblasts or lymphoblastoid cells from eight patients with clinical symptoms of prolidase deficiency were analyzed in terms of enzyme activity, presence of material crossreacting with specific antibodies, biosynthesis of the polypeptide, and mRNA corresponding to the enzyme. There are at least two enzymes that hydrolyze imidodipeptides in these cells and these two enzymes could be separated by an immunochemical procedure. The specific assay for prolidase showed that the enzyme activity was virtually absent in six cell strains and was markedly reduced in two (less than 3% of controls). The activities of the labile enzyme that did not immunoprecipitate with the anti-prolidase antibody were decreased in the cells (30-60% of controls). Cell strains with residual activities of prolidase had immunological polypeptides crossreacting with a Mr 56,000, similar to findings in the normal enzyme. The polypeptide biosynthesis in these cells and the controls was similar. Northern blot analyses revealed the presence of mRNA in the polypeptide-positive cells, yet it was absent in the polypeptide-negative cells. The substrate specificities analyzed in the partially purified enzymes from the polypeptide-positive cell strains differed, presumably due to different mutations. Thus, there seems to be a molecular heterogeneity in prolidase deficiency. There was no apparent relation between the clinical symptoms and the biochemical phenotypes, except that mental retardation was present in the polypeptide-negative patients. The activities of the labile enzyme may not be a major factor in modifying the clinical symptoms.

Adolescent↗
PubMed1990

Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease.

A defect in the E1 beta subunit of the branched chain alpha-ketoacid dehydrogenase (BCKDH) complex is one cause of maple syrup urine disease (MSUD). In an attempt to elucidate the molecular basis of MSUD, we isolated and characterized a 1.35 kbp cDNA clone encoding the entire precursor of the E1 beta subunit of BCKDH complex from a human placental cDNA library. Nucleotide sequence analysis revealed that the isolated cDNA clone (lambda hBE1 beta-1) contained a 5'-untranslated sequence of four nucleotides, the translated sequence of 1,176 nucleotides and the 3'-untranslated sequence of 169 nucleotides. Comparison of the amino acid sequence predicted from the nucleotide sequence of the cDNA insert of the clone with the NH2-terminal amino acid sequence of the purified mature bovine BCKDH-E1 beta subunit showed that the cDNA insert encodes for a 342-amino acid subunit with a Mr = 37,585. The subunit is synthesized as the precursor with a leader sequence of 50 amino acids and is processed at the NH2 terminus. A search for protein homology revealed that the primary structure of human BCKDH-E1 beta was similar to the bovine BCKDH-E1 beta and to the E1 beta subunit of human pyruvate dehydrogenase complex, in all regions. The structures and functions of mammalian alpha-ketoacid dehydrogenase complexes are apparently highly conserved. Genomic DNA from lymphoblastoid cell lines derived from normal and five MSUD patients, in whom E1 beta was not detected by immunoblot analysis, gave the same restriction maps on Southern blot analysis. The gene has at least 80 kbp.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗
PubMed1990

Molecular basis of argininemia. Identification of two discrete frame-shift deletions in the liver-type arginase gene.

Argininemia results from a deficiency of arginase (EC 3.5.3.1), the last enzyme of the urea cycle in the liver. We examined the molecular basis for argininemia by constructing a genomic library followed by cloning and DNA sequencing. Discrete mutations were found on two alleles from the patient, a product of a nonconsanguineous marriage. There was a four-base deletion at protein-coding region 262-265 or 263-266 in exon 3 that would lead to a reading-frame shift after amino acid residue 87 and make a new stop codon at residue 132. The other was a one-base deletion at 77 or 78 in exon 2 that would lead to a reading-frame shift after residue 26 and make a stop codon at residue 31. For confirmation, genomic DNAs from the patient and from her parents were amplified by the polymerase chain reaction method. The patient was shown to be a compound heterozygote, inheriting an allele with the four-base deletion from the father and the other allele with the one-base deletion from the mother. These data seem to be the first evidence of a case of argininemia caused by two different deletion mutations.

Amino Acid Metabolism, Inborn Errors↗
PubMed1990

A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells.

Prolidase deficiency is an autosomal recessive disorder characterized by mental retardation and various skin lesions. Cultured skin fibroblasts were obtained from two independent patients with abnormal prolidase. Using the polymerase chain reaction, we amplified the entire coding region of human prolidase mRNA derived from patients' fibroblasts. Nucleotide sequence analysis of amplified cDNA products revealed a G to A substitution at position 826 in exon 12, where aspartic acid was replaced by asparagine at the amino acid residue 276, in cells from both patients. An analysis of the DNA showed that the substitution was homozygous. An expression plasmid clone containing a normal human prolidase cDNA (pEPD-W) or mutant prolidase cDNA (pEPD-M) was prepared, transfected, and tested for expression in NIH 3T3 cells. Incorporation of pEPD-W and pEPD-M resulted in the synthesis of an immunological polypeptide that corresponded to human prolidase. Active human enzyme was detected in cells transfected with pEPD-W, but not in those transfected with pEPD-M. These results were compatible with our observation of fibroblasts and confirmed that the substitution was responsible for the enzyme deficiency. As active prolidase was recovered in prolidase-deficient fibroblasts transfected with pEPD-W, this restoration of prolidase activity after transfection means that gene replacement therapy for individuals with this human disorder can be given due consideration.

Animals↗
PubMed1990

Lipid and apolipoprotein compositions of two species of ApoA-I containing lipoproteins in young girls with insulin-dependent diabetes mellitus.

Two species of lipoproteins containing apoA-I (A-ILp), lipoprotein containing apoA-I and apoA-II (LpA-I/A-II), and lipoprotein containing apoA-I but no apoA-II were isolated from 12 girls with insulin-dependent diabetes mellitus (IDDM) and from 19 healthy controls using affinity chromatography. When characterizing the lipid and apolipoprotein compositions, we noted compositional changes. In A-ILp, the levels of lipid, except for triglyceride, and the level of apoC-III were significantly higher in IDDM. In LpA-I/A-II, the levels of lipids, except for triglyceride, the levels of apoC-III, and the ratio of apoA-I to apoA-II were significantly higher in IDDM. In lipoprotein containing apoA-I but no apoA-II, the levels of all lipids and apolipoproteins in IDDM were similar to those in the controls. The percent phospholipid in A-ILp and LpA-I/A-II was significantly higher in IDDM. All of these changes of A-ILp are similar to those associated with the reduced risk in the nondiabetic population. However, apolipoprotein changes of LpA-I/A-II may possibly be related to the accelerated atherosclerotic processes noted in patients with IDDM.

Adolescent↗
PubMed1990

Isolated human growth hormone deficiency due to the hGH-I gene deletion with (type IA) and without (the Israeli-type) hGH antibody formation during hGH therapy.

Three Japanese patients with isolated growth hormone deficiency from two different families were shown to be homozygous for deletion of the structural gene for human growth hormone (hGH-I gene). These three patients had the same restriction fragment length polymorphism haplotypes. In patient No. 1, the growth rate initially responded well to pituitary human growth hormone, but growth rapidly ceased concomitantly with the development of high levels of anti-hGH antibodies. He again responded well to recombinant methionyl hGH and recombinant hGH without the methionine residue, even though having high hGH antibodies. Two siblings (Patients No. 2 and 3) showed a rather good response to pituitary hGH treatment without hGH antibodies ever being detected (the Israeli-type). hGH-I gene deletions may not necessarily result in hGH antibody formation. Heterogeneity has been observed in isolated hGH deficiency due to hGH-I gene deletion. hGH-I gene analysis should not be limited to patients with hGH antibody formation and subnormal growth responses to hGH therapy.

Adolescent↗
PubMed1990

Self-limited neonatal familial hyperparathyroidism associated with hypercalciuria and renal tubular acidosis in three siblings.

Three siblings with neonatal familial hyperparathyroidism diagnosed at age 4 months, 2 months, and 5 days, respectively, were treated. Hypercalciuria, nephrocalcinosis, and renal tubular acidosis were present in each child. In all three, there were higher responses of serum parathyroid hormone to serum calcium and higher elevation of serum calcium with oral calcium loading. The metabolism of vitamin D and calcitonin seemed to be intact. Hypercalcemia associated with the abnormal response of parathyroid hormone secretion disappeared when the children passed the age of approximately 2 years, although renal tubular acidosis and nephrocalcinosis remained. An autosomal recessive inheritance seems likely.

Acidosis, Renal Tubular↗
PubMed1990

[Effect of superoxide dismutase on serum sickness nephritis].

Antiinflammatory effect of recombinant human Cu, Zn superoxide dismutase (SOD) was studied in Wistar rats with serum sickness nephritis induced by egg albumin injection. Different dosages of SOD were given intramuscularly in nephritis rats as follows: 0 (group A), 2 (group B), 10 mg/kg/day (group C). Control rats were given 10 mg/kg/day of SOD. On day 52, histopathological examinations of the kidney were performed in all animals. Urinary albumin was 0.35 +/- 0.21, 0.24 +/- 0.14, 0.34 +/- 0.28 and 0.41 +/- 0.21 mg/day in group A, B, C and control, respectively on day 0, and 33.0 +/- 21.5, 1.52 +/- 0.54, 2.55 +/- 1.67 and 0.21 +/- 0.02 mg/day in group A, B, C and control, respectively on day 52. Daily administration of SOD significantly suppressed urinary albumin excretion (A vs B & C, P less than 0.05). Numbers of nucleus per one glomeruli in rats were 119 +/- 3.6, 76.3 +/- 6.7, 71.1 +/- 8 and 65.5 +/- 3.3 in group A, B, C and control, respectively (A vs B & C, p less than 0.01). The glomerular damage in serum sickness nephritis which was potentially induced by free oxygen radicals, would be prevented by the administration of SOD.

Albuminuria↗
PubMed1989

Structure of the ornithine transcarbamylase (OTC) gene and DNA diagnosis of OTC deficiency.

Complementary and genomic DNA clones corresponding to human ornithine transcarbamylase (OTC) have been isolated and analyzed. Restriction fragment length polymorphisms (RFCPs) on OTC gene locus were analyzed in Japanese female population. Based on these data, a prenatal diagnosis of OTC deficiency was carried out in a risk family. A C-to-T substitution was found in exon 5 of OTC gene is an another female patient.

DNA↗
PubMed1989

Protective effect of lipoproteins containing apoprotein A-I on Cu2+-catalyzed oxidation of human low density lipoprotein.

Two apoprotein A-I (apoA-I)-containing lipoproteins, one containing apoA-I and apoA-II (LpA-I/A-II) and the other containing only apoA-I (LpA-I), were examined for their effect on Cu2+-mediated oxidation of low density lipoprotein (LDL). The presence of LpA-I or LpA-I/A-II prevented LDL oxidation when assessed by the electrophoretic mobility, apoprotein B fragmentation and amounts of thiobarbituric acid-reactive substances. The protection of LDL oxidation by these lipoproteins was effective for up to 6 h, with LpA-I being more active than LpA-I/A-II. Results from these in vitro model experiments raise a possibility that LpA-I may play a role in protecting LDL from Cu2+-mediated oxidation.

Apolipoprotein A-I↗
PubMed1989

Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex.

We isolated from a placental cDNA library by immunoscreening a cDNA clone encoding the transacylase (E2b) precursor of the human branched chain alpha-keto acid dehydrogenase (BCKDH) complex. The cDNA insert consists of 2,649 base pairs with an open reading frame of 1,431 base pairs which can be translated into 477 amino acids and a 3'-untranslated region of 1,205 base pairs. The deduced amino acid sequence includes a leader peptide of 56 amino acid residues, a lipoyl-bearing domain, a E3-binding domain and an inner core domain. A mature human E2b subunit is likely to contain 421 amino acid residues with a calculated Mr 46,322. The nucleotide sequence of the open reading frame and the deduced amino acid sequence of the human E2b shows 91.6% and 92.0% homology with those of the bovine E2b subunit, respectively.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗