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Biomedical subjects

Y Endo

Publications and source records attributed to Y Endo.

At least 757 records · Page 42Linked to original sources
PubMed1981

Stimulation of protein-bound iodine formation by lipid extracts from hog thyroid microsomes.

The lipid materials extracted from hog thyroid microsomes were found to contain factors which stimulated both the NADPH oxidation by NADPH-cytochrome c reductase and PBI formation by a reconstituted system containing the reductase as a hydrogen peroxide generator and thyroid peroxidase. For both reactions, the stimulating activity in the extracts from the other subcellular fractions was less than that observed in the extracts from microsomal fraction. Lipids extracted from hog liver microsomes did not show any NADPH oxidation stimulating activity. Thin-layer chromatography of the lipid extracts from thyroid microsomes revealed the presence of at least two stimulating factors differing in chromatographic behaviour. At least one of the stimulating factors separated on TLC stimulated the oxygen consumption accompanied by generation of hydrogen peroxide due to the NADPH oxidation by NADPH-cytochrome c reductase. From these results it was suggested that in thyroid microsomes, but not in liver microsomes, there were stimulating factors extractable by chloroform-methanol. The factors could stimulate NADPH oxidation by NADPH-cytochrome c reductase followed by generation of hydrogen peroxide, resulting in the enhancement of PBI formation coupled with thyroid peroxidase.

Animals↗
PubMed1981

Iodide transport of thyroid plasma membranes.

Plasma membranes consisting of closed vesicles were isolated from hog thyroid homogenate. The membrane vesicles showed uphill transport of iodide from an external medium containing monovalent cations, of which K+ induced iodide transport more potently than Na+. The activity of the iodide transport expressed as T/M[I-] was as little as 3 to 11 in the presence of K+, but was invariably present. The ratio reached a maximum within about 10 min and then decreased fairly rapidly to unity. The addition of SCN- or CIO-4 to the external medium inhibited iodide transport. The transport activity was found to be maximum at pH 7.0 to 7.5 in the external medium. A kinetic study showed that the transport rate was saturated with respect to the iodide concentration. These observations suggested the presence of a carrier-mediated iodide transport system which was coupled with K+ flux across the plasma membrane.

Animals↗
PubMed1981

Plasma beta-thromboglobulin and platelet factor 4 in patients with chronic renal failure and effect of hemodialysis.

Significantly increased levels of plasma beta-thromboglobulin (beta-TG) (76.8 +/- 25.5 ng/ml, p less than 0.01) were observed in 24 patients with chronic renal failure (blood urea nitrogen (BUN) greater than 20 mg/100 ml), as compared with normal subjects (13.2 +/- 5.6 ng/ml). The increase in beta-TG was highly correlated with BUN (r = 0.651, p less than 0.01), creatinine (r = 0.778, p less than 0.01) and creatinine clearance ( t = -0.723, p less than 0.01). Plasma platelet factor 4 (PF4) and normal 5.0 +/- 2.0 ng/ml) also increased significantly to 8.5 +/- 3.4 ng/ml (p less than 0.01). However, statistical correlation between beta-TG and PF4 was not found in these patients. The reason is thought to be due to differences in molecular weight (PF4 8,000 MW; beta-TG 36,000 MW) and half-life time (PF4 30 min; beta-TG 100 min), and due to the difficulty in calculating statistically the correlation because of the narrow distribution of PF4 levels. The high levels of beta-TG (89.4 +/- 3.4 ng/ml) showed a further increase (109.4 +/- 5.8 ng/100 ml, p less than 0.01) after dialysis. This is thought to be due to hemoconcentration, because other blood factors such as RBC, WBC, platelets, fibrinogen, etc were elevated by about 20% during hemodialysis and because no adhesion of platelets to the cellulose membrane did occur. The increase in PF4 levels at 15 min (55.2 +/- 19.6 ng/ml, p less than 0.01) and 1 hr (23.7 +/- 8.4 ng/ml, p less than 0.01) of hemodialysis from the level before it (7.7 +/- 1.3 ng/ml) is thought to be caused the effect of heparin infusion. The change in PF4 was not accompanied by the change in beta-TG. During hemodialysis the decrease of other platelet functions such as adhesiveness, aggregation induced by ADP, collagen and PF3 remained unchanged.

Adult↗
PubMed1981

Study of agglutination of mouse mammary carcinoma (FM3A) cell induced by egg agglutinin of Rana catesbiana. II. Phytohemagglutinin P and protamine.

When mouse mammary carcinoma (FM3A) cells were treated with egg agglutinin of Rana catesbiana for 15 min at 25 degrees C, percent total particle number of both cell aggregates and single cells was in direct proportion to the cell electrophoretic mobility. Phytohemagglutinin P mediated agglutination proceeded with biphasic kinetics: the higher the concentration of phytohemagglutinin P the shorter was the lag period between the first and second stages of agglutination. In protamine-mediated agglutination, the percent total particle number was reduced at low concentrations, while the electrophoretic mobility reduced only at high concentrations. Agglutinating and cytotoxic activities of these three reagents were in an intimate relation: the higher the agglutinating activity, the greater was their cytotoxic activity.

Agglutination↗
PubMed1981

A new protease in hog thyroid lysosomes. I. The presence of a leupeptin-sensitive protease in the soluble fraction of thyroid lysosomes.

The presence of protease activity at pH 7.5 and at acidic pH was demonstrated in the soluble fraction of lysosomes which were prepared from hog thyroid homogenates by subcellular fractionation. The ratios of specific activity measured at pH 7.5 to that at pH 3.5 were 0.07 to 0.08 for casein (at pH 7.5) or haemoglobin (at pH 3.5) as substrate and 0.13 for iodoamino acid-releasing activity from thyroglobulin as substrate. The protease activity measured at pH 7.5 was inhibited by inhibitors for neutral type protease, such as leupeptin, and by sulfhydryl inhibitors, such as iodoacetamide, indicating that the protease was a leupeptin-sensitive protease and contained a sulfhydryl group for its active site. Insensitiveness of the protease activity to di-isopropyl fluorophosphate excluded the involvement of a serine group at the active site. At pH 5.5 the proteolytic and iodoamino acid-releasing activities using casein and thyroglobulin, respectively, were also investigated. Several lines of evidence suggested that both activities measured at pH 5.5 were due to a mixture of acidic and leupeptin-sensitive protease activities.

Animals↗
PubMed1981

A new protease in hog thyroid lysosomes. II. A partial purification and characterization of a leupeptin-sensitive protease.

A leupeptin-sensitive new protease was partially purified from hog thyroid lysosomes. The purification procedure included solubilization by hypotonic treatment of lysosomes, and Sephacryl S-300 and Sephadex G-100 gel chromatography, and the purification ratio was 10-fold from lysosomes. The pH optimum of the protease activity was around 5.5 and its molecular weight was estimated to be 22 000 by gel filtration. 2-Mercaptoethanol activated the hydrolysis of protein substrates and its effect was most pronounced in the case of thyroglobulin as substrate. Among the inhibitors used, leupeptin, antipain, toluenesulfonyl-lysine chloromethyl ketone and, to a lesser degree, chymostatin and toluene-sulfonyl-phenylalanine chloromethyl ketone effectively inhibited the hydrolysis of casein by the enzyme at pH 5.5, whereas pepstatin did not inhibit the activity significantly. The enzyme activity was also inhibited by sulfhydryl inhibitors such as iodoacetamide, p-chloromercuribenzoate, and N-ethylmaleimide. The release of iodoamino acids from thyroglobulin by the enzyme was inhibited in the same manner by the inhibitors used in the hydrolysis of casein. The physiological role of the new protease is discussed in comparison with cathepsin B and L found in liver lysosomes.

Animals↗
PubMed1981

Hepatic drug-metabolizing enzyme activities and anti-inflammatory potency of hydrocortisone in rats with granulomatous inflammation.

Experimental granuloma pouches were induced in the dorsum of Sprague-Dawley rats by the subcutaneous injection of either carrageenin or agar. In the former inflammation model, the hepatic activities of aminopyrine N-demethylase and aniline hydroxylase and the contents of cytochromes P-450 and b5 were reduced significantly from control and pentobarbital sleeping time was prolonged. Hydrocortisone inhibited significantly the increased vascular permeability, exudation and proliferation of the carrageenin-induced granuloma in the daily, oral dose of 10 mg/kg for 3 days. On the other hand, the animals with agar granuloma pouch did not show any decline of the hepatic drug metabolism and a same dosage level of hydrocortisone showed substantially no inhibitory effect on the agar granuloma. Consequently, it is suggested that impairment of the hepatic drug metabolism may be responsible for the increased potency of hydrocortisone in the carrageenin-induced granuloma.

Agar↗
PubMed1980

Structural studies of the sugar chains of human parotid alpha-amylase.

Human parotid amylase can be separated into three families of isoenzymes (A', A, and B) by Sephadex G-75 column chromatography. Isoenzymes in family B were free from carbohydrate, while those in family A were all glycoproteins. The carbohydrate moieties of family A isoenzymes were released from their polypeptide portions by hydrazinolysis and labeled by reduction with NaB[3H]4. The yield of total radioactive oligosaccharides indicated that family A isoenzymes all contain single asparagine-linked sugar chains in one molecule. The radioactive oligosaccharides were fractionated into one acidic and two neutral oligosaccharide fractions by paper electrophoresis and paper chromatography. By sequential exoglycosidase digestion in combination with a methylation study, their structures were determined to be: Gal beta 1 leads to 4 (Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2Man alpha 1 leads to 6[Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2Man alpha 1 leads to 3]Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 and 3[Gal beta 1 leads to 4 GlcNAc beta 1 leads to 2Man alpha 1 leads to 3 and 6]Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc Gal beta 1 leads to 4(Fuc alpha 1 leads to 3) GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc.

Amylases↗
PubMed1980

An enzyme immunoassay for the measurement of anti-thyroglobulin autoantibody in human serum.

An enzyme-linked sandwich immunoassay using human thyroglobulin conjugated with beta-D-galactosidase and silicone rods coated with human thyroglobulin was developed for the measurement of circulating anti-thyroglobulin autoantibody. The volume of serum needed for the assay was as little as 5 microliter. The sensitivity of the assay was approximately 7 x 10(-15) mol/tube of antithyroglobulin immunoglobulin G corresponding to 220 ng/ml of serum, which was equal to or rather higher than that of radioimmunoassay. The specificity of the assay was demonstrated by (1) parallelism of the standard curve with dilution of sample sera of patients with thyroid diseases, and (2) non-detectability of anti-thyroglobulin in autoantibody in the sera of normal subjects. The precision of the assay was proven by (1) sufficient recovery of antithyroglobulin immunoglobulin G added to serum, and (2) coefficients of variance within and between assays were 6.5 to 10.3% and 4.9 to 14.1%, respectively. No effect of thyroglobulin on the present assay was observed when the ratio of the amount of thyroglobulin to that of anti-thyroglobulin immunoglobulin G was lower than 1 : 10. Furthermore, a significant correlation was observed between anti-thyroglobulin autoantibody concentrations measured by our enzyme immunoassay and those by tanned red cell hemagglutination (r = 0.78), and between those by the enzyme immunoassay and those by radioimmunoassay (r = 0.80). The application to clinical samples ensured the high sensitivity and the adequate validity of the present assay.

Autoantibodies↗