Biomedical subjects

S Yazawa

Publications and source records attributed to S Yazawa.

At least 109 records · Page 6Linked to original sources

PubMed1990

A fibronectin-related synthetic peptide, Pro-Ala-Ser-Ser, inhibits fibronectin binding to the cell surface, fibronectin-promoted cell migration in vitro, and cell migration in vivo.

The biological activity of the amino acid sequence consisting of the immediate carboxyl terminus side of the Arg-Gly-Asp-Ser (RGDS) amino acid sequence in the cell-binding domain of intact fibronectin (FN) molecules was examined using synthetic peptides [RGDS, Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP), Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro (RGDSPASSKP), Pro-Ala (PA), Pro-Ala-Ser (PAS), Pro-Ala-Ser-Ser (PASS), and Pro-Ala-Ser-Ser-Lys (PASSK)]. These peptides were applied to the primary mesenchyme cells (PMCs) of the sea urchin, Clypeaster japonicus. In vitro immunohistochemistry indicated that the binding of exogenous FN to the PMC surface was inhibited by the peptides RGDSPASSKP and PASS, but not by RGDS, GRGDSP, PA, or PAS. PASS and RGDS introduced into the blastocoel also inhibited PMC migration in vivo. FN-promoted PMC migration in vitro was also inhibited by PASS and RGDS. The present results indicate that the PASS peptide inhibits FN binding to the PMC surface and promotes PMC migration, suggesting that the FN molecule uses the PASS amino acid sequence to bind to the PMC surface and to promote PMC migration in the blastocoel.

Amino Acid Sequence↗

PubMed1990

A simple procedure for isolation of tumor-associated antigens by affinity chromatography using fucose-specific Aleuria aurantia lectin.

An affinity column containing L-fucose specific Aleuria aurantia lectin was used for the efficient separation of tumor-associated antigens. Five of six glycoconjugates antigens tested, carcinoembryonic antigen (CEA), CA19-9, sialyl Lewis X-i, DU-PAN-2 and CA125, bound to the affinity gel and eluted in high yield with 20 mM L-fucose, but alpha-fetoprotein, which is known to contain fucose in the carbohydrate chain, passed through the column. This column was also proved to be useful for group separation of CA19-9, sialyl Lewis X-i and Leb antigens from a serum sample with gastric cancer.

Antibodies, Monoclonal↗

PubMed1989

Serum alpha(1----3)-L-fucosyltransferase, carcinoembryonic antigen, and sialyl Lewis X-i antigen levels in lung cancer.

Serum alpha(1----3)-L-fucosyltransferase activity was measured in 58 patients with lung cancer, 27 benign diseases, and in 100 healthy controls. The levels of enzyme activity were significantly higher in the sera of patients with cancer when compared to those in benign diseases and healthy controls. The elevation of the enzyme activity correlated with the clinical stages and to the size of the primary tumors. Follow-up studies with various stages showed that the enzyme activity was useful in tracking the clinical course of disease after surgery. To evaluate the usefulness of this enzyme as a diagnostic marker, carcinoembryonic antigen (CEA) and sialyl Lewis X-i antigen levels were also measured. The results indicate that alpha(1----3)-L-fucosyltransferase could be a more specific tumor marker than such tumor-associated antigens in lung cancer.

Carcinoembryonic Antigen↗

PubMed1989

CEA levels in peritoneal washings from gastric cancer patients as a prognostic guide.

Carcinoembryonic antigen (CEA) levels were determined in the peritoneal washings from 44 patients with gastric cancer to evaluate the usefulness for a predictor of postsurgical prognosis. Seventeen of the 21 patients (80.9%) with serosal invasion showed elevated levels of CEA, whereas most of the patients with no serosal invasion (22/23) showed low levels of CEA and did not develop peritoneal metastasis. All patients with positive cytology showed elevated levels of CEA in the peritoneal washings. Therefore, CEA levels in the peritoneal washings could be an adjunctive tool for predicting the postsurgical prognosis in gastric cancer.

Carcinoembryonic Antigen↗

PubMed1989

Tumor-related elevation of serum (alpha 1----3)-L-fucosyltransferase activity in gastric cancer.

(alpha 1----3)-L-Fucosyltransferase activity was measured in serum samples from 90 gastric cancer patients, 10 patients with benign diseases and 100 healthy controls. The enzyme activity was significantly elevated in the serum samples of patients with cancer compared to those from patients with benign diseases (P less than 0.01) and healthy controls (P less than 0.001). The elevation of the enzyme activity was found to correlate strongly with the clinical stage of disease. The sensitivity of (alpha 1----3)-L-fucosyltransferase was also demonstrated to be high in comparison with the tumor-associated antigens, such as carcinoembryonic antigen and sialylated Lewis X-i. Follow-up studies of (alpha 1----3)-L-fucosyltransferase in 11 cancer patients with disease at different stages showed that the enzyme activity could be useful for monitoring the post-surgical course of the disease. These results suggest that (alpha 1----3)-L-fucosyltransferase activity has a clinically important potential as a tumor marker in gastric cancer.

Biomarkers, Tumor↗

PubMed1988

Cancer-associated elevation of alpha(1----3)-L-fucosyltransferase activity in human serum.

GDP-fucose:N-acetylglucosaminide alpha(1----3)-L-fucosyltransferase activity was measured in sera of patients with various cancers using a synthetic substrate, N-acetyl-2'-O-methyllactosamine, as an acceptor. One hundred twenty-four of the 169 patients showed significantly high levels of the enzyme activity when compared to healthy controls, irrespective of the location of their tumor. However, enzyme levels were in the normal range in patients with non-neoplastic diseases, such as infectious disease, liver disease, and other inflammatory problems as well as in leukemic patients. The chromatofocusing profile of the enzyme using PBE-94 gel over a pH gradient from pH 6.0 to 4.0 demonstrated that the level of enzyme eluted at pH 5.4 was markedly elevated in the sera of stomach and ovarian cancer patients. A correlation was established between alpha(1----3)-L-fucosyltransferase activity and the presence of malignancy which may be used to evaluate the utility of the enzyme as a tumor marker.

Biomarkers, Tumor↗

PubMed1988

Purification and characterization of N-acetyl-D-galactosamine-binding lectin from Falcata japonica.

An N-acetyl-D-galactosamine-binding lectin from Falcata japonica seeds was purified by affinity column chromatography of N-acetyl-D-galactosamine coupled to epoxy-activated Sepharose 6B. A 1000-fold purification of lectin was obtained from the crude extracts. The purified lectin agglutinated blood group A red cells, but neither blood group B nor O red cells. Polyacrylamide gel electrophoresis of the lectin showed one diffuse band. Molecular weights of 125,000 and 117,000 were estimated by gel filtration and ultracentrifugal analysis, respectively. SDS-polyacrylamide gel electrophoresis of the lectin also showed a single band which has a molecular weight of 34,000. Therefore, the lectin molecule was estimated to be a tetramer composed of four identical non-covalently bound subunits. F. japonica lectin was a glycoprotein containing 5% total carbohydrate, and the amino acid composition was characterized by a high content of aspartic acid, serine and glycine, a low content of methionine and the absence of cysteine.

ABO Blood-Group System↗

PubMed1988

The presence of CA19-9 in serum and saliva from Lewis blood-group negative cancer patients.

Eighteen cancer patients showed high levels of CA19-9 in sera, even though the blood-group phenotypes of their red blood cells were Le(a-b-). Seven of these patients (group I) were determined as Le(a-b-) from both red blood cells and saliva consistently, whereas eleven other patients (group II) secreted either Le(a) or Le(b) antigen in saliva and showed the expression of incompatible Lewis blood-group antigens. GDP-fucose: N-acetyl-glucosaminide alpha(1----4)-L-fucosyltransferase was demonstrated to be present in salivas from both group I and group II. These results suggest that a cancer-associated alteration of Lewis blood-group antigen expression occurs in cancer patients.

Antigens, Neoplasm↗

PubMed1987

Androgen receptor, testosterone uptake and karyotype in androgen-dependent mouse tumor (SC 115) and its androgen-independent subline (CS 2).

Content of androgen receptor, retention of injected testosterone and karyotype of SC 115, androgen-dependent tumor, were compared with those of CS 2, an androgen-independent subline derived from SC 115. Although Bmax was less than that of SC 115, androgen receptor was present in the cytosol and the nuclear extract from CS 2. To examine the ability for androgen retention, a large amount of testosterone was injected into tumor-bearing mice, and the amount of androgen in the crude nuclear and postnuclear fractions of tumors was compared. In both fractions, retention of injected androgen was higher in the SC 115 than in the CS 2. Since most of the injected testosterone was not metabolized in the tissues and the injection of testosterone 5 alpha-reductase inhibitor showed no significant influence on the growth rate of the SC 115, intracellular active androgen was assumed to be testosterone in these tumor cells. As the CS 2 was tetraploid, the androgen independency of the CS 2 seems to be related to chromosomal changes.

Animals↗

PubMed1987

Synthetic antigens as immunogens: Part II: Antibodies to synthetic T antigen.

Antibody to the carbohydrate moiety of T antigen was developed. The synthetic antigen (Gal beta 1----3 GalNAc alpha 1----OC6H4N = N-BSA) was prepared by coupling the diazonium salt of the disaccharide derivative Gal beta 1----3 GalNAc alpha 1----OC6H4NH2 (o) with bovine serum albumin. Specificity of the antibody produced was examined with structurally related synthetic saccharides using the enzyme immunoassay technique. The presence of a glycosyl group at 0-6 of either the Gal or the GalNAc residue of the disaccharide Gal beta 1----3 GalNAc did not prevent binding of the antisera to the saccharide moiety. However, the antisera did not bind either the trisaccharide moiety NeuAc2----3 Gal beta 1----3 GalNAc alpha 1----OC6H4NO2 (o) or GlcNAc beta 1----3 Gal beta 1----3 GalNAc alpha OBn. These observations indicate that antibody approach to the antigen is to the 0-3 side of the terminal galactose in the disaccharide Gal beta 1----3 GalNAc. We have also observed that the antibody prefers Gal beta 1----3 GalNAc alpha 1----to Gal beta 1----3 GalNAc beta 1----disaccharide derivatives in its binding capacity. The antibody was found to bind natural T antigen present on neuraminidase-treated red blood cells and, by immunohistochemical analysis, it was found to bind to naturally occurring T antigen on breast tumor cells.

Antibodies↗

PubMed1987

Synthetic antigens as immunogens: Part I. The combining site specificities of antibodies formed in rabbits to synthetic disaccharide alpha-L-Fuc-(1----3)-D-Gal.

Antibody to chemically synthesized Fuc alpha 1----3 Gal-1----OC6H4N = N bovine serum albumin was developed. Specificity analysis using related synthetic saccharides was performed. The antisera were shown to be specific for both sugars in the disaccharide, to the 1----3 positional linkage and to the alpha anomeric configuration. Immunohistochemical staining was performed on benign disease and adenocarcinoma tissue of the colon. 5/8 of the benign colon polyp tissue and 4/6 of the colonic adenocarcinoma tissue showed strong granular cytoplasmic staining of the epithelia cells lining the ducts. None of the six normal colon tissues tested showed any reactivity. Immunohistochemical staining was also performed on tissue from benign disease and from carcinoma of the mammary gland. 2/5 of the tissue from benign disease of the breast and 3/6 of the tissue from breast carcinoma showed strong granular cytoplasmic staining of the ductal epithelial cells.

Adenocarcinoma↗

PubMed1986

N-acetyl-beta-D-glucosaminyltransferases related to the synthesis of mucin-type glycoproteins in human ovarian tissue.

The presence of N-acetyl-beta-D-glucosaminyltransferases in microsome preparations from human ovarian tissues was investigated with UDP-GlcNAc and several synthetic oligosaccharides as acceptors. The products were identified by paper chromatography and the linkage of the 2-acetamido-2-deoxy-beta-D-glucopyranosyl group incorporated into oligosaccharides was determined by exoglycosidase digestions, 1H-n.m.r. spectroscopy, and methylation analysis. These results showed that ovarian microsome preparations contain both beta-(1----3)- and beta-(1----6)-N-acetyl-D-glucosaminyltransferase activities which might be involved in the synthesis of mucin-type glycoproteins. Substrate competition tests suggested that both UDP-GlcNAc:-Bn glycoside of beta-D-GlcpNAc-(1----6)-alpha-D-GalpNAc [GlcNAc to GalNAc] and -Bn glycoside of beta-D-Galp-(1----3)-[beta-D-GlcNAc-(1----6)]-alpha-D-GalpNAc [GlcNAc to Gal] beta-(1----3)-N-acetyl-D-glucosaminyltransferase activities reside in a single enzyme species.

Carbohydrate Conformation↗

PubMed1986

alpha-L-fucosidase from aspergillus niger: demonstration of a novel alpha-L-(1----6)-fucosidase acting on glycopeptides.

An alpha-L-fucosidase which hydrolyzes fucose from alpha-(1----6)-linkage to N-acetylglucosamine was found in Aspergillus niger. The enzyme was purified by affinity chromatography with bovine IgG glycopeptide-Sepharose 4B. The enzyme preparation released fucose from bovine IgG glycopeptide and fucosylated asialoagalactofetuin, but failed to cleave 1----2, 1----3 or 1----4 linkages of alpha-L-fucosides.

Acetylglucosamine↗

PubMed1986

Use of N-acetyl-2'-O-methyllactosamine as a specific acceptor for the determination of alpha-L-(1----3)-fucosyltransferase in human serum.

A synthetic substrate, N-acetyl-2'-O-methyllactosamine, was employed as a specific acceptor for alpha-L-(1----3)-fucosyltransferase from human serum. The fucosyl linkage of the product from this substrate was characterized by hydrolysis with a specific alpha-L-(1----3)/(1----4)-fucosidase. Using this acceptor, the pH optimum for the serum alpha-L-(1----3)-fucosyltransferase was 6.5. The enzyme was activated by Mn2+ or Mg2+ ions and was inhibited by EDTA. The apparent Km for this enzyme using N-acetyl-2'-O-methyllactosamine was 20.4 mM and Vmax was 5.6 pmol/h/ml serum.

Amino Sugars↗

PubMed1986

Elevated serum alpha(1----3)-L-fucosyltransferase activity with synthetic low molecular weight acceptor in human ovarian cancer.

Serum alpha(1----3)-L-fucosyltransferase activity was measured in 29 ovarian cancer patients with active disease, 26 ovarian cancer patients with no clinical evidence of disease and 23 healthy females. N-Acetyl-2'-O-methyl-lactosamine was used as the acceptor for the enzyme. The level of the enzyme activity was significantly (P less than 0.05) higher in the serum of patients with known tumor when compared to healthy controls and patients with no clinical evidence of disease.

Amino Sugars↗

PubMed1986

Elevated activities of blood group Le gene dependent alpha(1----3)-L-fucosyltransferase in human saliva of Lewis negative patients with epithelial ovarian cancer.

Levels of alpha(1----3)-L-fucosyltransferase activities were measured in salivas of patients with ovarian cancer. GDP-L-Fuc:GlcNAc alpha(1----3)-fucosyltransferase was found elevated in patients known to have epithelial ovarian cancer, irrespective of their ABH and Lewis blood group phenotypes. GDP-L-Fuc: Glc alpha(1----3)-fucosyltransferase was also elevated in both Lewis positive and negative patients, although the enzyme activity was very low or absent in Lewis negative healthy controls.

Female↗

PubMed1984

Isolation of fucosyl glycoproteins from human erythrocyte membranes by affinity chromatography using Aleuria aurantia lectin.

Fucosyl glycoproteins were fractionated from a sialoglycoprotein preparation of human erythrocyte membrane by using Aleuria aurantia lectin (AAL) coupled to Sepharose 4B. The affinity eluates were characterized as having high fucose content and significant H activity as measured in terms of N-acetylgalactosamine (GalNAc) incorporation with A1-enzyme and hemagglutination inhibition assay with anti-H sera, and the unadsorbed fractions contained low levels of fucose and were devoid of apparent H activity. Neuraminidase treatment of the material improved the recovery of the affinity eluate. Thus, 66% of the applied asialoglycoprotein was recovered in the eluate, though only 10% of the untreated material was bound and eluted. Moreover, a fucose-rich and H-active fraction was obtained through the affinity chromatography of the previously unbound fraction after neuraminidase treatment. In sodium dodecyl sulfate-gel electrophoresis, the main component of both the unadsorbed and eluted fraction was revealed to be PAS-1 glycoprotein. These results indicate that AAL-Sepharose was effective for isolating fucose-containing compounds from the membrane glycoprotein especially after neuraminidase treatment. The reasons for the appearance of H activity in the affinity eluates are discussed.

Asialoglycoproteins↗

PubMed1983

Immunochemical properties of human plasma alpha 1 leads to 2 fucosyltransferase specified by blood group H-gene.

A beta-galactoside alpha 1 leads to 2 fucosyltransferase (H-enzyme) from human group O plasma which provides H blood group specificity to erythrocyte membranes has been purified approximately 22,000-fold by chromatography on DEAE-Sepharose CL-6B, GDP-hexanolamine-Sepharose 4B and SP-Sephadex C-50. The molecular weight of the H-enzyme was estimated to be 150,000 by gel filtration. Human group O erythrocyte membranes which had lost their H blood group activity by the action of alpha 1 leads to 2 fucosidase were fucosylated by the transferase, and restored the H activity. Radioactive L-fucose appeared to be incorporated into glycolipid blood group substances of erythrocyte membranes. The activity of the alpha 1 leads to 2 fucosyltransferase from human plasma, stomach mucosa, erythrocyte membranes and porcine stomach mucosa were specifically inhibited by the rabbit antiserum immunized with the preparation of human plasma H-enzyme. The anti-plasma H-enzyme antiserum did not inhibit the activities of alpha 1 leads to 3 N-acetylgalactosaminyltransferase (A-enzyme), alpha 1 leads to 3 galactosyltransferase (B-enzyme), and beta-N-acetylglucosaminide alpha 1 leads to 3 and alpha 1 leads to 4 fucosyltransferases from human plasma and stomach mucosa.

ABO Blood-Group System↗