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Biomedical subjects

A Mizoguchi

Publications and source records attributed to A Mizoguchi.

At least 145 records · Page 8Linked to original sources
PubMed1989

Intrasynaptosomal distribution of the ras, rho and smg-25A GTP-binding proteins in bovine brain.

We have purified to near homogeneity and characterized three small molecular weight (Mr) GTP-binding proteins, the c-Ki-ras protein (c-Ki-ras p21), the rho protein (rho p20) and a novel smg-25A protein (smg p25A), from bovine brain crude membranes. In the present studies, the intrasynaptosomal distribution of these 3 small Mr G protein has been investigated using bovine brain. ras p21 and rho p20 are found in the synaptosomal membrane fraction but not in the synaptosomal soluble fraction. In contrast, smg p25A is found in both the synaptosomal membrane and soluble fractions. These results indicate that the intrasynaptosomal distribution of these small Mr G proteins is different and suggest that they are involved in different neuronal functions.

Animals↗
PubMed1988

Histochemical studies of enzymes of the energy metabolism in postimplantation rat embryos.

Using histochemical procedures for the detection of lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), and cytochrome c oxidase (cytox), we investigated the levels of these enzymes of the energy metabolism in postimplantation rat embryos (9.5-12.5 days of gestation). On day 10.5 of gestation, the neural tube, somites, myocardium, and mesenchyme displayed moderate levels of LDH activity; this activity gradually increased in strength, so that, on day 12.5 of gestation, intense LDH activity was uniformly distributed in these intraembryonic tissues. In contrast to LDH, distinct regional differences in the distribution of SDH and cytox were detected. On day 10.5 of gestation, the myocardium exhibited weak to moderate SDH and cytox activity, and on day 11.5, the myocardial activity of these enzymes had become moderate to intense. However, in all other embryonic tissues, e.g., the neural tube and somites, only weak SDH and cytox activity was present. On day 12.5 of gestation, the myocardium displayed very intense SDH and cytox activity, whereas the mantle layer of the neural tube, the spinal ganglia, and the myotomes exhibited only moderate levels of SDH and cytox activity. In the matrix of the neural tube and mesenchyme, these enzyme activities remained at low levels. At electron microscopy, cytox activity was detectable in the spaces between the inner and outer membranes as well as in the intracristal spaces of mitochondria. In general, cytox activity increased in parallel with the differentiation of mitochondria (i.e., increased mitochondrial numbers and size, and the development of mitochondrial cristae), but when the distribution of the cytox activity was considered in detail, it was found to differ among mitochondria.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

A monoclonal antibody against a synthetic fragment of bombyxin (4K-prothoracicotropic hormone) from the silkmoth, Bombyx mori: characterization and immunohistochemistry.

Monoclonal antibodies were produced by immunizing mice with a synthetic decapeptide corresponding to the N-terminal portion of the A-chain of bombyxin, a peptide from Bombyx mori which activates the prothoracic glands of the saturniid moth, Samia cynthia ricini, and was previously called 4K-PTTH. We obtained a hybridoma clone secreting an antibody that recognized specifically bombyxin after treatments for disulfide-bond reduction but did not when untreated. Immunoblotting studies demonstrated the presence of highly heterogeneous immunoreactive components in Bombyx brain homogenates. Immunohistochemistry using this antibody indicated that bombyxin was produced by four pairs of mid-dorsal neurosecretory cells of the brain and transferred to and released from the corpora allata of Bombyx.

Animals↗
PubMed1986

Amino acid sequence of a prothoracicotropic hormone of the silkworm Bombyx mori.

We have determined the complete amino acid sequence of 4K-PTTH-II, one of three forms of the M(r) 4400 prothoracicotropic hormone of the silkworm Bombyx mori, active to brainless pupae of Samia cynthia ricini. Like vertebrate insulin, it consists of two nonidentical peptide chains (A and B chains). The A chain consists of 20 amino acid residues. The B chain is a mixture of four microheterogeneous peptides, two of which consist of 28 residues, and the other two, of 26 residues. 4K-PTTH-II has considerable sequence homology (40%) with human insulin, and it resembles porcine relaxin both in the carboxyl-terminal cysteine residue of the A chain and in the amino-terminal pyroglutamic acid residue of the B chain. The identical distribution of the six cysteine residues also indicates that 4K-PTTH-II belongs to the insulin family.

Journal Article↗
PubMed1986

Cell surface asparagine-linked sugar chains of human early myeloblastic leukemic cells (KG-1a).

The asparagine-linked sugar chains obtained from total cell surface membrane glycoproteins of human early myeloblastic leukemic cells (KG-1a cells) were studied. The sugar chains liberated by hydrazinolysis were purified by paper electrophoresis, paper chromatography, and Bio-Gel P-4 chromatography followed by analysis of exoglycosidase digestion and methylation study. Neutral oligosaccharides were all composed of high mannose type sugar chains. Acidic oligosaccharides were chiefly composed of typical bi-, tri-, and tetraantennary complex type sugar chains with Gal beta 1----4GlcNAc beta 1----groups and Neu-Ac alpha 2----3 or 6Gal beta 1----4GlcNAc beta 1----groups (in which Gal is galactosyl, GlcNac is N-acetylglucosamine, and NeuAc is N-acetylneuraminic acid) as side chains. Moreover the following two structures were identified in (in which Fuc is fucosyl): monosialyl bi- and triantennary sugar chains with a Gal beta 1----4(Fuc alpha 1----3)GlcNAc beta 1----group (X determinant) as one of the side chains; and monosialyl tetraantennary sugar chains with a Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc group (repeating N-acetyllactosamine unit) as one of the side chains. These data together with our previous studies on sugar chains of K562 cells [early erythroblast], adult erythrocytes [H. Yoshima, N. Shiraishi, A. Matsumoto, S. Maeda, T. Sugiyama, and A. Kobata, J. Biochem. (Tokyo), 91: 233-246, 1982], and HL-60 cells [promyelocyte] [A. Mizoguchi, S. Takasaki, S. Maeda, and A. Kobata, J. Biol. Chem., 259: 11943-11957, 1984] strongly suggest that the cell surface asparagine-linked sugar chains alter in an orderly fashion, systematically in association with lineage and maturation stages during hematopoietic cell differentiation.

Asparagine↗
PubMed1985

[Clinical evaluation of lenampicillin in the treatment of superficial suppurative skin and soft tissue infection. A double-blind study comparing amoxicillin].

A double-blind controlled clinical study between lenampicillin (LAPC), a newly developed oral ampicillin (ABPC) prodrug, and amoxicillin (AMPC) was conducted for the treatment of suppurative skin and soft tissue infection as grouped in 6 disease types. LAPC or AMPC were orally administered at a daily dose of 1,000 mg, in 4 equally divided doses. Each group was treated for 14 days. The results indicated that LAPC was equal to AMPC in evaluations of effectiveness and usefulness, although incidence of severe side effects was slightly lower in LAPC. The number of cases studied was 235 (115 in the LAPC group, 120 in the AMPC group). Among these, 10 patients (4 in LAPC, 6 in AMPC) were excluded and 12 patients (5 in LAPC, 7 in AMPC) dropped out. Final global improvement rating was evaluated in 213 patients (106 in LAPC, 107 in AMPC). General usefulness rating was evaluated in 215 patients (106 in LAPC, 109 in AMPC), and overall safety rating was evaluated in 231 patients (115 in LAPC, 116 in AMPC). Final global improvement rating of LAPC was, "cured", 55.7% and "cured" and "remarkably improved", 79.2%. The rate increased to 88.7% when "improved" was included. On the other hand, in the AMPC group, "cured" was 50.5%, and "cured" and "remarkably improved" was 76.6%. The rate increased to 91.6% when "improved" was included. No significant difference was found between the 2 drug groups. In overall safety rating of LAPC, "safe" was 93.9%, while in the AMPC group, "safe" was 94.0%. No significant difference was found between the 2 drug groups. Side effects were noted in 2 of 115 patients (1.7%) among the LAPC group and in 5 of 116 patients (4.3%) among the AMPC group. Incidence of severe side effects was slightly lower in LAPC (P less than 0.1). General usefulness rating of LAPC was, "remarkably useful", 56.6% and the rate increased to 86.8% when "useful" was included. In the AMPC group, "remarkably useful" was 51.4%, and increased to 84.4% when "useful" was included. No significant difference was found between the 2 drug groups.

Adult↗
PubMed1984

Changes in asparagine-linked sugar chains of human promyelocytic leukemic cells (HL-60) during monocytoid differentiation and myeloid differentiation. Decrease of high-molecular-weight oligosaccharides in acidic fraction.

Asialo-oligosaccharides obtained by sialidase digestion of asparagine-linked acidic sugar chains of promyelocytic leukemic cells (HL-60) differed in size distribution from those of cells induced to undergo myeloid or monocytoid differentiation. High-molecular-weight oligosaccharides which are predominant in HL-60 cells, decreased slightly during myeloid differentiation and markedly during monocytoid differentiation with concomitant increase of biantennary oligosaccharides. Structural analyses revealed that the induced monocytoid cells contain a series of complex-type oligosaccharides with bi-, tri-, and tetraantennary structures and high-molecular-weight oligosaccharides with N-acetyllactosamine repeating units, which show diversity in the presence or absence of the fucose residue linked to the reducing terminal N-acetylglucosamine, of the bisecting N-acetylglucosamine residue, and of the X-antigenic determinant in their outer chain moieties. Methylation analysis of each class of oligosaccharides of HL-60 cells and of their differentiated counterparts revealed the presence of similar heterogeneity in their structures, indicating that the difference is only quantitative. The results show that the shifts in size of the oligosaccharides found in the differentiated cells are derived from changes in outer chain formation and elongation of N-acetyllactosamine repeating units, and thus suggests that the decreased expression of N-acetylglucosaminyltransferases may be involved especially in the monocytoid differentiation program.

Asparagine↗
PubMed1984

Changes in asparagine-linked sugar chains of human promyelocytic leukemic cells (HL-60) during monocytoid differentiation and myeloid differentiation. Appearance of high mannose-type oligosaccharides in neutral fraction.

Structural changes in the asparagine-linked sugar chains of plasma membrane glycoproteins during myeloid and monocytoid differentiation were investigated by the use of an in vitro differentiation system for human promyelocytic leukemic cells (HL-60), which can be induced to more mature myeloid cells by exposure to dimethyl sulfoxide and to macrophage-like cells by a phorbol ester. The asparagine-linked sugar chains released from their plasma membranes by hydrazinolysis were separated into a neutral fraction and an acidic fraction composed of over ten components. The content of neutral oligosaccharides, which accounted for 8% of the total asparagine-linked sugar chains in HL-60 cells, increased slightly to 13% in dimethyl sulfoxide-induced cells and markedly to 33% in phorbol ester-induced cells. Structural analyses revealed that the neutral oligosaccharides of HL-60 cells are all of the complex type with a variety of Gal beta 1----4GlcNAc beta 1----units in their outer chain moieties and the following core structure: (sequence; see text) After myeloid and monocytoid differentiation, the total amount of neutral complex-type sugar chains did not change significantly, but newly found high mannose-type sugar chains contributed up to 3% and 24% of the total sugar chains, respectively.

Asparagine↗
PubMed1984

Isolation and some characterization of the prothoracicotropic hormone from Bombyx mori.

The prothoracicotropic hormone (PTTH) was isolated from adult heads of Bombyx mori. Fifty micrograms of pure PTTH was obtained from 648,000 heads through a 15-step purification procedure with a 2 X 10(6)-fold purification and an 8% recovery. Chemical analyses of this PTTH have shown that it is a single-chain peptide consisting of 40-43 amino acid residues (MW, 4330-4740), the N-terminus of which is glycine. As little as 0.1 ng of PTTH elicited adult development in a debrained pupa of Samia cynthia ricini. Five picograms of PTTH directly stimulated the prothoracic glands in vitro so as to enhance ecdysone release. The hemolymph ecdysteroids of brainless Samia pupae that were developed by PTTH injection increased with essentially the same pattern as in developing normal pupae.

Amino Acid Sequence↗
PubMed1983

The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. II. The carbohydrate composition of the glycopeptide cleavage product.

The carbohydrate groups present in the glycopeptide cleaved from purified [3H]-GlcNAc-rhodopsin by an enzyme from the retinal pigment epithelium were analyzed in terms of the size of the oligosaccharide chains, the sequence of the sugars and their anomeric linkages. These analyses were performed also on intact rhodopsin and an enzyme control. The oligosaccharides were cleaved from the peptide by means of hydrazinolysis. After reduction with NaB3H4, the oligosaccharides, purified by paper electrophoretic and paper chromatographic means, were digested sequentially with exoglycosidases, and the resultant digestion products examined by high-resolution gel filtration on Bio-Gel P-4 (-400). The size, sequence and anomeric configuration of the constituents of the oligosaccharides present in the glycopeptide were essentially identical to those present in intact purified rhodopsin, indicating the retention by the glycopeptide of the sugar chains of the intact molecule.

Animals↗
PubMed1982

Structures of the carbohydrate moieties of secretory component purified from human milk.

Secretory component purified from human milk contains four asparagine-linked sugar chains in one molecule. The sugar chains were released from the polypeptide portion of secretory component by hydrazinolysis as oligosaccharides and fractionated by paper electrophoresis and paper chromatography. The sugar chains of secretory component show an extraordinarily high multiplicity. By sequential exoglycosidase digestion in combination with methylation analysis, more than 40 structurally different sugar chains were found. They were all of biantennary complex type with either Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNac beta 1 leads to 4GlcNAc or Man alpha 1 leads to 6(Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc as their core portions and the multiplicity is produced by variety of the two outer chain moieties. The structures of outer chains found are GlcNAc beta 1 leads to 2, +/- NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2, Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2, GL beta 1 leads to 4GlcNAc beta 1 leads to 3Gal beta 1 leads to 4(+/- Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2, NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 3 Gal beta 1 leads to 4GlcNAc beta 1 leads to 2, Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 3Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2, and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 3Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2.

Carbohydrate Sequence↗
PubMed1982

Prothoracic glands of the saturniid moth Samia cynthia ricini possess a circadian clock controlling gut purge timing.

In the moth Samia cynthia ricini, timing of the release of prothoracicotropic hormone is controlled by a circadian clock in the cephalic organ (brain); while this hormone release is necessary for gut purge, the final timing of this event is controlled by a circadian clock in the prothoracic glands that gates release of ecdysone. The photoreceptor of the prothoracic gland clock(s) is extraocular and evidently in the glands themselves. Demonstration that the clock and its photoreceptor are in the prothoracic glands is based on a mixture of localized illuminations and the transplantation of glands from one larva to another.

Journal Article↗
PubMed1982

Cell surface glycoprotein and asparagine-linked sugar chain patterns of rat erythroleukemic cell lines.

In order to elucidate whether chromosomal change or induction of differentiation is correlated with the change of the patterns of cell surface glycoproteins and asparagine-linked sugar chains, glycoproteins and carbohydrates of five rat erythroleukemic cell lines (K1DB, D5A1, K2D, K2DA, and K4D) were studied by sodium dodecyl sulfate:polyacrylamide gel electrophoresis and hydrazinolysis followed by gel chromatography, respectively. The surface glycoprotein patterns of five cell lines were very similar, each containing four glycoproteins with molecular weights of 250,000, 115,000, 80,000, and 28,000, respectively. Only D5A1, which can be induced to erythroid differentiation, had two additional glycoproteins, with molecular weights of 135,000 and 65,000, respectively. All neutral oligosaccharides obtained from plasma membranes of five cell lines by hydrazinolysis were of the high-mannose type, and the acidic oligosaccharides were of the complex type with three different types of outer chains in various combinations: +/- NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc; Gal beta 1 leads to 3Gal beta 1 leads to 4GlcNAc; and Gal beta 1 leads to 4GlcNac beta 1 leads to 3Gal beta 1 leads to 4GlcNAc. An interesting finding was that two sugar chains, NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3(Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(+/-Fuc alpha 1 leads to 6)GlcNAcOT (in which the subscript OT indicates a NaB3H4-reduced oligosaccharide), were found only in surface carbohydrates of D5A1.

Animals↗