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Biomedical subjects

N Azuma

Publications and source records attributed to N Azuma.

At least 127 records · Page 7Linked to original sources
PubMed1991

Increased concentrations of free light chain lambda in sera from chronic hemodialysis patients.

Serum levels of FLc were determined in 5 pre-HD CRF patients, 63 CRF patients receiving HD therapy, 15 CAPD and 40 healthy volunteers. The highest serum FLc concentration was observed in patients receiving HD. Concentrations of kappa- and lambda FLc were higher than normal in patients with CRF, and were about 4-fold and 1.8 fold greater than control values in HD patients, with a predominance of lambda chains. This HD-associated elevation of serum FLc strongly suggests a role for FLc in the etiology of light chain deposit disease and AL-amyloidosis. Lambda-FLc and beta 2-m exhibited similar patterns of change in the serum during the course of HD therapy. Further studies may reveal other pathological conditions other than CRF in which these polypeptides may play a role.

Carpal Tunnel Syndrome↗
PubMed1990

Histochemical studies on hyaluronic acid in the developing human retina.

Changes in the distribution of hyaluronic acid in the developing human retina were investigated histochemically with alcian blue staining and the Streptomyces hyaluronidase digestion method using 56 human embryos and fetuses ranging from 5 to 41 weeks of gestational age. Hyaluronic acid was first detected in the inner layer of the retina at 12 weeks. The site of accumulation extended towards the outer layer by 20 weeks. At the neonatal stage, longitudinal fibers, possibly the processes of Müller cells, were proved to contain hyaluronic acid. These findings suggest that Müller cells produce hyaluronic acid transiently from 12 weeks' gestation to the neonatal stage.

Aged↗
PubMed1990

Two isoforms of regulatory light chain of abalone smooth muscle myosin.

Abalone myosin contains two kinds of light chain, regulatory light chain (LC2) and essential light chain (LC1) according to SDS-PAGE. Three distinct light chain bands were observed on polyacrylamide gel electrophoresis of purified abalone myosin in the presence of urea (urea-PAGE). The slower two components showed had mobility on SDS-PAGE and they also showed regulatory activity as the regulatory light chain. They were termed LC2-a and LC2-b in order of increasing mobility on urea-PAGE and isolated by DE-32 ion exchange column chromatography in the presence 8 M urea. The ratio of LC2-a and LC2-b in the central portion of adductor muscle of abalone (LC2-a: LC2-b = 7:3) was different from that (1:1) in the peripheral portion. These results suggest that the two light chains are isoforms of the regulatory light chain. The amino acid compositions of LC2-a and LC2-b were very similar to each other except for the Cys content. The UV absorption spectra were also quite similar, as were the UV difference absorption spectra induced by Ca2+. Phosphorylation was not detectable with the myosin light chain kinase of chicken gizzard. The Ca2+ concentration dependencies of Mg-ATPase activity of LC2-a or LC2-b hybridized abalone myosin (a-myosin, b-myosin) were similar to each other in the absence of rabbit F-actin, but differed in the presence of actin. The b-myosin had a higher maximum value of actomyosin ATPase activity and a lower apparent binding constant of actin and myosin than a-myosin.(ABSTRACT TRUNCATED AT 250 WORDS)

Actins↗
PubMed1990

Molecular cloning and nucleotide sequence of the aminopeptidase T gene of Thermus aquaticus YT-1 and its high-level expression in Escherichia coli.

Aminopeptidase T (AP-T) is a metallo-dependent dimeric enzyme of Thermus aquaticus YT-1, an extremely thermophilic bacterium. We cloned the AP-T gene from T. aquaticus YT-1 into Escherichia coli using a synthetic oligonucleotide as a hybridization probe. The nucleotide sequence of the AP-T gene was found to encode 408 amino acid residues with GTG as a start codon. The molecular weight was calculated to be 44,820. The AP-T was overproduced in E. coli (about 5% of total soluble protein) when the start codon of the gene was changed from GTG to ATG, and the gene was downstream from the tac promoter. The AP-T expressed in E. coli was heat stable and easily purified by heat treatment (80 degrees C, 30 min). The N-terminal amino acid sequence of AP-T showed similarity with that of aminopeptidase II from Bacillus stearothermophilus.

Amino Acid Sequence↗
PubMed1990

Growth inhibition of BALB/c 3T3 cells by a high-molecular-weight mucin-like glycoprotein of human milk fat globule membrane.

PAS-O is a high-molecular-weight mucin-like glycoprotein of the human milk fat globule membrane, and originates from the lactating mammary epithelial cell membrane. The cell proliferation rate of BALB/c 3T3 cells was markedly reduced by addition of PAS-O to their culture medium, this inhibition being concentration-dependent (0-10 microgram/ml) and reversible. The inhibitory activity was removed by periodate or protease treatment of the glycoprotein. PAS-O may interact with 3T3 cells to mimic the effect of high cell density on growth. PAS-O, which has been recognized as a glycoprotein molecule carrying a differentiation antigen expressed on the mammary epithelial cell surface, may play a role in regulating the growth of the mammary cells.

Animals↗
PubMed1990

[Morphological and histochemical studies on the development of human conjunctival goblet cells].

This report deals with the development of human conjunctival goblet cells. Fifty-six eyes of human embryos and fetus ranging from 5 to 41 weeks of gestational age were used in this study. Glycosaminoglycans in the goblet cells were investigated histochemically using 1% alcian blue staining (pH = 2.5) and PAS reagent staining and sialidase (neuraminidase) digestion. At 8 weeks, goblet cells appeared in the forniceal area, and they extended to the palpebral and bulbar conjunctiva. These cells were already similar to adult goblet cells. Alcian blue staining and the enzyme digestion method revealed the existence of sialic acid in the goblet cells from 9 weeks. These results suggest that at the early developmental stage the goblet cells develop from the forniceal area. It is also indicated that the goblet cells in the early developmental stage are already similar to cells in the adult stage because they contain mainly sialic acid as glycosaminoglycans.

Adult↗
PubMed1989

[Morphological and immunohistochemical studies on degenerative changes of the retina and the optic nerve in neonatal rats injected with monosodium-L-glutamate].

Degenerative changes in the retina and the optic nerve were investigated morphologically and immunohistochemically following administration of monosodium-L-glutamate (MSG) in rats. MSG (5mg/g b.w.) was injected subcutaneously every other day for 5 times after birth. The retina and the optic disc was observed ophthalmoscopically at 1, 3 and 6 months after birth. At the same stage, morphological and immunohistochemical changes were also investigated under light microscopy. The neuron of the retinal ganglion cell was identified immunohistochemically with antiserum to neurofilament 200 kD (NF). Glial cells were stained with antisera to glial fibrillary acidic protein (GFAP) and S-100 beta protein, and myelin of oligodendrocytes was also stained with antiserum to myelin basic protein (MBP). Histologically the inner layer of the retina was selectively destroyed, and the optic nerve also showed degeneration, changing into a thin strand. The retinal vessels were narrow and coarse, however, they extended to the peripheral region. Although immunohistochemical staining with NF antiserum was scarcely detected both in the retina and in the optic nerve, glial stainings with GFAP and S-100 beta protein antisera were widely observed in the perivascular space of the retina and in the glial column of the optic nerve. These findings indicated that the ganglion cells and their neurons are significantly affected by MSG, but the retinal vessels and glial cells are rarely affected. Ophthalmoscopically, the optic discs of rats treated with MSG were small and deeply excavated. The vitreous vessels persisted in most cases even at 6th months after birth.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1989

[Experimental studies on microphthalmos formation in neonatal rats treated with monosodium-L-glutamate].

Changes in the eyeball size were investigated in rats treated with monosodium glutamate (MSG) during the neonatal period. Correlations among ocular size and degenerative changes of the retina and optic nerve were also studied ophthalmoscopically and histologically. Rats received MSG 5 times, 2 times or once. In rats which received MSG 5 times, the administration was made at 1, 3, 5, 7 and 9 days of birth. In rats, which received MSG 2 times, the administration was made on 2 subsequent days (1 and 2, 3 and 4, 5 and 6, 7 and 8, 9 and 10, 12 and 13 or 15 and 16 postnatal days). In the group of rats, which received MSG once, the administration was made on each from the 1st to the 15th postnatal day. Microphthalmos formation was clearly observed only in rats with 5 times and 2 times (9 and 10 days) injection of MSG. In these rats, narrowing of retinal vessels, paleness and excavation of optic disks were observed ophthalmoscopically. Total liquefaction of the vitreous body were seen in the same groups. Histological examinations also revealed degeneration of the inner layers of the retina. These findings indicated that the administration of MSG at critical stages during postnatal development induces disturbances of eyeball growth. It was also suggested that the growth of the eyeball is closely associated with the postnatal development of the retina.

Animals↗
PubMed1989

[Morphological studies on cataract and small lens formation in neonatal rats treated with monosodium-L-glutamate].

Changes in the transparency and size of lenses in rats were investigated following administration of monosodium-L-glutamate (MSG), MSG (5 mg/g b.w.) was injected subcutaneously on the 9th and 10th days after birth. Morphological changes of the lenses were examined ophthalmoscopically and histologically. Ophthalmoscopically, localized opacity was apparent at the posterior pole of the lens corresponding to the attached portion of hyaloid artery at 1 months of age. The incidence of cataract increased with age, reaching more than 75% at 4 months of age. Morgagni's globules were histologically detected in the opacity of the posterior lens cortex. Degenerative changes of the lens epithelium were observed in the mature cataract. However, the capsules of the lens were well preserved. The size and weight of the lens were smaller than those of controls. Although the pathogenesis of the cataract and small lenses are not clear at the moment, these findings indicate that administration of MSG could be an etiologic factor in cataract formation in the developing rat.

Animals↗
PubMed1988

Preparation of subfragment-1 from abalone smooth muscle myosin.

Myosin subfragment-1 (S1), which has one heavy chain (HC) (93 kDa) and two light chains (LC1 and LC2), was prepared by papain digestion of myosin from abalone-smooth muscle in the presence of Ca2+. The Ca-sensitivity of abalone S1 itself was not lost completely (about 30%). The tryptic digestion of S1 showed that in the presence of EDTA, S1 HC was split into 68, 55, and 23 kDa fragments, as in the presence of Ca2+, but 23 kDa was further degraded into 19 kDa. In contrast to the result in the presence of Ca2+, LCs disappeared in the early stage of reaction and Ca-ATPase activity decreased rapidly to about 70% of that of intact S1. This rapid decrease of Ca-ATPase activity seemed to be accompanied with the digestion of LCs. Therefore, LCs contribute to the protection of 23 kDa fragment from further digestion, to the maintenance of Ca-ATPase activity by stabilizing the structure of S1 to some extent in the presence of Ca2+. Since F-actin suppressed the cleavage of S1 HC to 68 and 23 kDa during tryptic digestion, it might be that 23 and 68 kDa corresponded to 20 kDa (C-terminal fragment) and to 50 + 25 kDa (N-terminal fragment) of skeletal myosin S1, respectively.

Actins↗
PubMed1988

Preliminary observation on pancreatic duct adenocarcinoma induced by intraductal administration of N-ethyl-N'-nitro-N-nitrosoguanidine in dogs.

Pancreatic duct adenocarcinoma was induced by intraductal administration of N-ethyl-N'-nitro N-nitrosoguanidine (ENNG) in two mongrel dogs. A dog received a total dose of 595 mg of ENNG during 12 months and was sacrificed. Duct obstruction was detected by pancreatography and duct adenocarcinoma was found. Another dog was given a total dose of 350 mg of ENNG during 8 months and was sacrificed 26 months after the first administration of the carcinogen. Duct adenocarcinoma was found. No pancreatic tumors were found in 2 dogs given intraperitoneal N-nitrosobis(2-oxopropyl)amine at a total dose of 4000 mg or in 2 dogs given Tween 60 only. These results suggest that the direct presence of a carcinogen in the pancreatic duct was able to induce duct adenocarcinoma in dogs.

Adenocarcinoma↗
PubMed1987

Purification and characterization of a novel metalloendopeptidase from Streptococcus cremoris H61. A metalloendopeptidase that recognizes the size of its substrate.

An endopeptidase (LEP-II), which has a unique substrate specificity, was purified to homogeneity by conventional chromatographic techniques from Streptococcus cremoris H61. The enzyme was a metalloendopeptidase since it was inhibited by EDTA and 1,10-phenanthroline; the metal-depleted enzyme could be fully reactivated by micromolar levels of Zn2+ and was not inhibited by specific inhibitors for serine or thiol protease. The molecular mass of the enzyme was estimated to be 80 kDa by Sephacryl S-300 gel filtration and high-performance liquid chromatography with a TSK-G3000SW column. The enzyme consisted of two identical subunits and the N-terminal sequence of LEP-II was determined up to the 19th residue. Although the enzyme had a broad substrate specificity it specifically hydrolyzed the peptide bonds involving the amino groups of hydrophobic amino acid residues. Various small polypeptides, such as alpha s1-CN(f1-23), alpha s1-CN(f91-100), oxidized insulin B chain, glucagon and some biologically active peptides were hydrolyzed. However, a variety of larger polypeptides or proteins, such as alpha s1-CN(f1-54), alpha s1-CN(f61-123), alpha s1-CN(f136-196), alpha s1-casein, beta-casein, and kappa-casein were not hydrolyzed. LEP-II recognized the size of its substrates, which were limited below a molecular mass of about 3.5 kDa.

Amino Acids↗
PubMed1987

A glyco-phosphoprotein in human milk.

A highly glycosylated phosphoprotein (HGPP) was isolated from a human casein fraction by reversed-phase high-performance liquid chromatography. This component contained carbohydrates to approximately 38.2% (w/w) and phosphorus to approximately 1.6% (w/w). The molecular weight of this HGPP as estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis approximately 41,000. Ultracentrifugal analysis revealed that the sedimentation coefficient of the HGPP was 2.6S in a buffer at pH 7.0 and 27 degrees C, but this component interacted with human k-casein and formed a complex with s = 10.4S.

Chromatography, High Pressure Liquid↗
PubMed1987

Common duct carcinoma and obstruction in female hamsters treated with N-nitrosobis(2-oxopropyl)amine and/or cholecystectomy.

Detailed histologic observations were performed on the head of the pancreas of hamsters treated with 10 mg/kg body weight N-nitrosobis(2-oxopropyl)amine (BOP) once a week for 6 weeks with or without cholecystectomy. Cholecystectomy was performed 5 weeks before starting BOP initiation. The incidence of head cancers was 100% and cholecystectomy did not affect pancreatic carcinogenesis by BOP. Common bile duct dilatation was produced by advanced pancreatic head carcinomas and microadenocarcinomas in common duct. Micro-adenocarcinomas were not macroscopically detected since the tumors were located in the lumen of common duct.

Adenocarcinoma↗
PubMed1987

[Absorption of 5-FU orally administered in a patient with postoperative gastric cancer under artificial dialysis].

A patient under artificial dialysis due to chronic renal failure suffered from gastric cancer concurrently. This patient underwent subtotal gastrectomy followed by consecutive oral administration of 5-FU (tablets) as a postoperative adjuvant chemotherapy. The 5-FU level in the peripheral blood on oral administration at 50 mg remained at 0.007-0.01 microgram/ml over 2 hours. This feature of 5-FU blood level is not seen in gastric cancer patients with normal renal functions on administration of 5-FU tablets, and it seems to approximate the features of a 5-FU prodrug level in the blood upon oral administration. Neither the influence of dialysis on the absorption of orally administered 5-FU nor side effects caused by 5-FU were observed. The above findings suggest that it may be possible to maintain a certain blood level of 5-FU and to perform adjuvant chemotherapy even in cancer patients under artificial dialysis, as long as the dose is controlled carefully.

Administration, Oral↗