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Biomedical subjects

E Fujimori

Publications and source records attributed to E Fujimori.

At least 19 recordsLinked to original sources
PubMed1994

[Nutrition evaluation of female university students].

The self-evaluation of nutritional status, utilized as a teaching strategy of introductory nutrition course at Nursing School (São Paulo's University), gave a subsidy to this work. With this purpose, 50 female university students 3rd'semester (mean age was 21.7) were required to complete a three days food record and report their approximate height and weight. The analysis of food intake adequacy indicated that 98% of the students had insufficient intake (less than 90% of recommended of National Research Council-1980) of, at least, one of the nutrients (protein, calcium, iron, vitamin A, B1, B2, C and niacin). It was evidenced an inadequate intake (less than 90% of RDA) of calcium (80% of the students), vitamin A (72%), iron (64%), vitamin B1 (74%), vitamin B2 (56%) and vitamin C (34%). The inadequate intake was more frequently and serious (less than 60% RDA) for calcium (42%), vitamin A (20%) and iron (16%) showing a vitamins and minerals deficient diet.

Adult↗
PubMed1992

Protein-losing enteropathy and pancreatic involvement in a case of connective tissue disease.

A patient with connective tissue disease presenting with both protein-losing enteropathy and pancreatic involvement is reported. A 52-year-old female was admitted because of mild epigastralgia, anasarca and ascites. Serum albumin, transferrin and zinc, showed low levels. An Upper G.I. series and endoscopy showed thickened folds of the duodenum and the jejunum. Biopsy specimens revealed lymphangiectasia in edematous villi. 99mTc-labeled human serum albumin scintigram showed abnormal radioactivity in the small intestine 90 minutes after intravenous injection, indicating protein-losing enteropathy. Hypoalbuminemia was ameliorated by glucocorticoid therapy, but recurred twice when glucocorticoid treatment was tapered. Hypoalbuminemia has not occurred since intestinal lymphangiectasia was improved with glucocorticoid treatment. Levels of elastase 1 and lipase were high in serum and ascites on admission. Endoscopic retrograde pancreatogram showed no abnormalities. Serum pancreatic enzymes were also ameliorated by glucocorticoid therapy, but slightly high levels continued for about one year and a half. This case might have been diagnosed as systemic lupus erythematosus although mixed connective tissue disease was also suspected. There are few reports of protein-losing enteropathy and pancreatic involvement associated with connective tissue diseases. Protein-losing enteropathy and pancreatic involvement were ameliorated with glucocorticoid treatment, suggesting participation of immunological mechanisms.

Connective Tissue Diseases↗
PubMed1989

Cross-linking and fluorescence changes of collagen by glycation and oxidation.

The non-enzymatic glucosylation of collagen in vivo and in vitro produces blue-fluorescent cross-links very slowly. The mechanism of their formation is unknown. We investigated the role of oxidation in glycation. When native fluorescent collagen from old-rat tail tendon and its CNBr peptides were oxidized by chemically generated singlet oxygen, cross-linking occurred immediately, and the cross-linked products showed an increased blue fluorescence. Further cross-linking and development of blue fluorescence also were accelerated by singlet oxygen when oxidizing in vitro glucosylated collagen CNBr peptides. It was noted that the blue fluorescence developed at the expense of a near-UV fluorescence. This near-UV fluorophore, which is also present in native collagen, was found to be produced by the in vitro glucosylation of collagen and during the cross-linking by glucosylation was slowly converted to the blue fluorophore. These changes indicate the autoxidation of near-UV fluorescent intermediates to blue fluorescent cross-links during glucosylation. Non-enzymatic fructosylation, which occurs in vivo in certain proteins, was more effective than glucosylation in forming fluorophores and cross-links with collagen in vitro. Fructosylated fluorophores were found different from glucosylated products in their oxidation reactivities with singlet oxygen.

Animals↗
PubMed1988

Cross-linking of collagen CNBr peptides by ozone or UV light.

Insoluble collagen from rat tail tendon was digested with cyanogen bromide. The resultant peptides were dissolved in 0.1% SDS solution and separated by gel filtration and gel electrophoresis. Cross-linking occurred in CNBr-cleaved peptides when they were exposed to ozone or biologically effective UV (300 nm) radiation. The enhancement of a blue fluorescence at 430 nm (excited at 350 nm) was found to be associated with oxidized, cross-linked peptides. Polymeric peptides, formed in collagen with aging, also exhibited enhanced blue fluorescence.

Animals↗
PubMed1985

Changes induced by ozone and ultraviolet light in type I collagen. Bovine Achilles tendon collagen versus rat tail tendon collagen.

High-molecular-mass aggregates were made soluble from insoluble collagens of bovine Achilles tendon and rat tail tendon by limited thermal hydrolysis. These polymeric collagen aggregates were cross-linked by 390-nm-fluorescent 3-hydroxy-pyridinium residues (excited at 325 nm) in the former tendon and by unknown non-fluorescent residues in the latter. With the solubilized insoluble-collagens from both tendons, as well as with acid-soluble collagen from rat tail tendon, other 350-385-nm fluorescence intensities (excited at 300 nm) were found to be higher in monomeric chains than in dimeric and polymeric chains. Low levels of ozone inhibited fibril formation of acid-soluble collagen particularly from young rat tail tendon, reacting with tyrosine residues and the 350-385-nm fluorophores. Aldehyde groups, involved in cross-linking, were not effectively modified by ozone. beta-Components (alpha-chain dimers) were not efficiently dissociated even by higher doses of ozone compared to gamma-components (alpha-chain trimers). Polymeric chain aggregates from bovine Achilles tendon collagen, whose 3-hydroxy-pyridinium cross-links are cleaved by ozone, were more readily dissociated by ozone than those from rat tail tendon collagen. Ultraviolet (300-nm) light, which destroyed the 350-385-nm fluorophores, inhibited fibril formation less effectively than ultraviolet (275-nm) light, which is absorbed by tyrosine residues, and did not dissociate collagen polymers from rat tail tendon. On the other hand, ultraviolet (320-nm) light, absorbed by 3-hydroxy-pyridinium cross-links which were rapidly photolyzed, partially dissociated polymeric collagen aggregates from bovine Achilles tendon after subsequent heating.

Achilles Tendon↗
PubMed1985

Ultraviolet light- and ozone-induced changes in pyridinoline, a trisubstituted 3-hydroxypyridinium crosslink of collagen.

Pyridinoline photo-degraded with the formation of photoproducts absorbing diffusely around 260-290 nm (pH 7) and sharply at 232 nm (pH 1). Subsequent heating partially regenerated the original pyridinoline, also producing new products absorbing at 417/440 nm (pH 7) and 300/412 nm (pH 1). Pyridinoline (pH 7) and its new products (pH 7 and pH 1) also underwent ozone-induced degradation.

Amino Acids↗
PubMed1983

Cross-linking and fluorescence of pyrene-labeled collagen.

The pyrene-labeling of acid-soluble (type I) and acid-insoluble collagens from young and old rat tail tendon has been investigated. The pyrene excimer fluorescence is associated with stabilized pyrene labels bound to two adjacent aldehydes in monomeric young collagens. Polymeric young collagens, as well as monomeric and polymeric old collagens, tend to lose this specific arrangement. This is shown by salt and new chromatographic fractionation of monomeric and polymeric collagens. During denaturation, pyrene labels are released from saturated aldehydes in both alpha 1 and alpha 2 chains. This unstable pyrene-labeling is stabilized by NaBH4 reduction of the hydrazone bonds between aldehyde groups and pyrene-containing hydrazines. This stabilization reveals that alpha 1 contains more aldehyde groups than does alpha 2 in young collagen. Pepsin-solubilized, acid-insoluble collagens are partly cross-linked and, like acid-soluble collagens, exhibit the fluorescence of pyrene aggregates probably located at unidentified cross-links, different from unsaturated aldehyde-containing cross-links in acid-soluble collagens.

Aging↗
PubMed1983

Benzo[a]pyrene-collagen interactions.

In vitro interactions of benzo[a]pyrene (BaP) with acid-soluble type I collagen from rat tail tendon have been investigated. The fluorescence of BaP increases in the presence of collagen. Bound BaP inhibits the formation of collagen fibrils in solution. When BaP-collagen complexes are irradiated in air with UV (365 nm) light, BaP rapidly undergoes photooxidation with the further inhibition of fibril formation. Viscosity and circular dichroism (CD) studies show that neither BaP nor further UV-irradiation alters the size or helical conformation of the protein. During thermal denaturation of collagen, BaP fluorescence changes. Collagen from young rat tail tendon shows a pronounced drop at about 38 degrees C, whereas that from old rat tail tendon exhibits an increase with a plateau in the same temperature range. These anomalous changes are observed when tyrosine residues, present only in the non-helical terminal telopeptides of collagen, are excited at 275 nm, but not by direct BaP excitation at 387 nm. These findings suggest that the specific hydrophobic telopeptide region, which plays an important role in fibril formation, are affected by bound BaP.

Aging↗
PubMed1982

Crosslinking and photoreaction of ozone-oxidized calf-lens alpha-crystallin.

Direct-photo-oxidation, singlet oxygen-oxidation, or photosensitized oxidation can modify lens crystallins, causing an increase in blue fluorescence and covalent crosslinking. A relationship between these changes has not been elucidated. We now report results from experiments with ozone oxidation. When calf-lens alpha-crystallin is treated with zone oxidation. When calf-lens alpha-crystallin is treated with ozone, new absorption, fluorescence, and phosphorescence, which are characteristic of the oxidized product of tryptophan (N-formylkynurenine), appear at 320, 435, and 445 nm, respectively. In addition, in this ozonization of alpha-crystallin, its polypeptides are crosslinked by nondisulfide bonds. Irradiation of ozone-treated alpha-crystallin with near-ultraviolet (365 nm) light increases crosslinking and reduces the 320 nm absorbance with a concomitant appearance of a new absorption at about 420 nm. This photoproduct exhibits an intense fluorescence around 450 nm and a weak phosphorescence at 510 nm, with excitation peaks at 400, 415, and 422 nm. These findings are essentially the same as those observed in photo-oxidized alpha-crystallin, suggesting the involvement of the same tryptophan oxidized product in the modification of the lens protein.

Animals↗
PubMed1981

Fluorescent-labeled cross-links in collagen: pyrenesulfonylhydrazine.

Aldol condensation products of two lysyl-derived aldehyde (allysine) residues are involved in cross-linking of collagen. However, the distribution of these cross-links and their age-related changes remain largely unanswered. We have found that the unsaturated aldehydes of aldol condensation cross-links can be fluorescent labeled. When labeled with pyrenesulfonylhydrazine, pyrene dimers and excimers fluoresce at 383 and 485, nm, respectively. (The pyrene dimer is stable in benzene, whereas in polar solvents it exhibits an exponential decay to monomer fluorescing at 378 nm.) Dimers bound to collagen also decay to monomers, but at a more complicated, nonexponential rate. This dissociation in collagen is also associated with gradual decrease in the excimer fluorescence. While dissociated monomers appear to be reassociated by redialysis, the excimer is not regenerated. During fibril formation in vitro of the labeled collagen, two fluorescence changes take place: a very rapid decrease of the excimer fluorescence and a gradual increase of the monomer fluorescence. These changes indicate very early and early conformational changes at the nonhelical terminal telopeptides. The excimer fluorescence also decreases upon thermal and guanidine denaturation. Two different environments for excimer formation are suggested by the latter. It is concluded that pyrenesulfonylhydrazine offers a unique and sensitive probe for the proximity of aldehyde groups as well as for the mobility and conformation changes of the telopeptides in collagen.

Aging↗