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Biomedical subjects

H Munakata

Publications and source records attributed to H Munakata.

At least 91 records · Page 5Linked to original sources
PubMed1984

Isolation and characterization of human placenta fibronectin.

Fibronectin was isolated from human placenta tissues and compared with human plasma fibronectin. Placenta and plasma fibronectins had similar amino acid compositions, immunological properties, and cell attachment-promoting activities, but differed in apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which could be accounted for at least partly by the difference in carbohydrate composition. Unlike plasma fibronectin, placenta fibronectin failed to form a precipitin line with concanavalin A in a double diffusion system. The non- or low-reactivity of placenta fibronectin with this lectin was also demonstrated by affinity chromatography with concanavalin A-agarose, in which more than 90% of the radiolabeled glycopeptides derived from placenta fibronectin was not retained on the gel. The two fibronectins also differed in the reactivity with Lens culinaris agglutinin of their glycopeptide fractions. These data indicate that placenta and plasma fibronectins are different in their carbohydrate structures and, therefore, suggest the presence of a tissue- or cell-specific mechanism for processing the carbohydrates of this glycoprotein.

Amino Acids↗
PubMed1984

Glycosaminoglycans of human colonic mucosa and colonic adenocarcinoma.

The mucosal scrapings of the normal human colons and the colonic adenocarcinoma tissues were digested with pronase, and the glycosaminoglycan fractions were prepared by fractionation with cetylpyridinium chloride after treatment with deoxyribonuclease. Chondroitin sulfate A/C, heparan sulfate, and hyaluronic acid were contained in the glycosaminoglycan fraction of the normal tissue, but dermatan sulfate was undetectable. In contrast, the glycosaminoglycan fractions derived from the tumors contained substantial amounts of dermatan sulfate together with the foregoing three glycosaminoglycans. The total content of glycosaminoglycans per wet tissue weight was elevated in the tumor tissues, which was consistent with histochemical findings.

Adenocarcinoma↗
PubMed1984

Comparison of glycosaminoglycans from thoracic aortas of several mammals.

Intima-media of porcine, canine, rabbit, and human thoracic aortas were separately digested with pronase, after extraction of fat. Glycosaminoglycan fractions were then separated from the resulting glycoconjugate fractions by precipitation with cetylpyridinium chloride. Glycosaminoglycan compositions were determined by sequential digestion with Streptomyces hyaluronidase, chondroitinase AC, chondroitinase ABC and heparitinase 1. All the tissues contained hyaluronic acid, chondroitin sulfates AC, dermatan sulfate and heparan sulfate. Of these glycosaminoglycans, chondroitin sulfates AC were the most prominent ones. Relatively large proportions of heparan sulfate were contained in these tissues except for canine aorta. It is noteworthy that the proportions of glycosaminoglycans in the intima-media of rabbit and human thoracic aortas with similar maturation were quite similar, although those of others differed from each other.

Animals↗
PubMed1984

Hormonal effects on glycosaminoglycans in thoracic aortas of rabbits.

Intima-media of thoracic aortas obtained from estrogen-treated, estrogen-progesterone-treated and sham-treated ovariectomized rabbits were separately digested with pronase after extraction of fat. Glycosaminoglycan fractions were then separated from the resulting glycoconjugate fractions by precipitation with cetylpyridinium chloride. The glycosaminoglycan levels increased after treatments with estrogen and estrogen-progesterone. Glycosaminoglycan compositions were determined by sequential digestion with Streptomyces hyaluronidase, chondroitinase AC, chondroitinase ABC and heparitinase 1. The proportions of dermatan sulfate and chondroitin sulfates AC increased after treatments with these hormones, while those of hyaluronic acid and heparan sulfate decreased. The changes of the proportions of dermatan sulfate and hyaluronic acid were dramatic. The changes of the glycosaminoglycan compositions with these hormones are thought to be an anti-atherosclerotic effect of these female hormones.

Animals↗
PubMed1984

Sulfated glycosaminoglycans synthesized in rabbit uterus.

The uteri obtained from the estrogen-treated rabbits were incubated with [35S] sulfate for 6 hr. The medium and the tissues were then separated from the incubation mixture and digested with pronase. Each digest was fractionated by DEAE-Sephadex A-25 (Cl- form) column chromatography. The radioactivity in the subfractions (M-0.9 M Fr and EI-0.9 M Fr) eluted with 0.9 M NaCl was the highest among six subfractions in both cases. The compositions of sulfated glycosaminoglycans in M-0.9 M Fr and EI-0.9 M Fr were examined by electrophoresis on cellulose acetate membrane and by gel filtration through Sephadex G-50, in combination with nitrous acid treatment and chondroitinase AC II digestion. The electrophoretograms indicated that sulfated glycosaminoglycans in EI-0.9 M Fr were chondroitin sulfates A and (or) C, heparan sulfate and dermatan sulfate, while those in M-0.9 M Fr were mostly chondroitin sulfates A and (or) C. Although heparan sulfate in M-0.9 M Fr was not detected on the electrophoretogram by staining with Alcian blue, it was considerably labelled with [35S]sulfate. This finding suggested that the specific radioactivity of this heparan sulfate was very high. The present data indicate that the estrogen-treated rabbit uterus actively synthesized sulfated glycosaminoglycans.

Animals↗
PubMed1984

Acidic glycopeptides isolated from young human aortas.

Intima-media of young human thoracic aortas were digested with pronase, after extraction of saline-soluble matters and fat. Glycopeptide fractions were separated from the resulting glycoconjugate fractions by fractionation with cetylpyridinium chloride. Acidic glycopeptides (0.15 M Fr and 0.3 M Fr) were then isolated from the glycopeptide fractions by DEAE-Sephadex A-25 (Cl- form) column chromatography. They contained glucosamine, galactose, mannose and sialic acid as the major sugars and glucose as the minor one, although the proportions of these constituents differed from each other. In addition, galactosamine and fucose were the minor sugars in 0.3 M Fr and 0.15 M Fr, respectively. 0.3 M Fr contained much more sulfate and amino acids than 0.15 M Fr. Aspartic acid, proline, glycine, threonine, glutamic acid, valine, serine and alanine were the major amino acids, amounting to 82-89% in total, in these acidic glycopeptides, although their contents differed from each other. It is noteworthy that the proportions of the constituents in the corresponding fractions from young boy and girl with the same age showed similar trend. Although the data indicated the heterogeneity of the carbohydrate and peptide chains of the acidic glycopeptides, the degree of the heterogeneity is smaller than that of sialoglycopeptides isolated previously from aged human aortas.

Aged↗
PubMed1984

Extraction of fibronectin from human normal and cirrhotic livers.

Tissue-associated fibronectin was extracted with 4 M urea from human normal and cirrhotic livers. The results of rocket immunoelectrophoresis indicated that the amount of fibronectin in cirrhotic liver was twice as much as that in normal liver. The collagen content was much higher in cirrhotic than in normal livers. These data suggested an important role of fibronectin in tissue fibrosis.

Fibronectins↗
PubMed1984

Sulfated proteoglycans synthesized in myometrium of the estrogen-treated rabbit.

Myometrium obtained from the estrogen-treated rabbit was incubated with [35S] sulfate, and the 35S-labeled proteoglycans were extracted from this tissue with 4 M guanidine hydrochloride. The extract was fractionated by CsCl density gradient centrifugation, followed by DEAE-cellulose column chromatography. The major proteoglycan fraction (D(1+2] was separated into two fractions (D(1+2)-I and D(1+2)-II) by gel filtration on Sepharose CL-4B. The compositions of the 35S-labeled glycosaminoglycans in 5 proteoglycan fractions (D(1+2)-I, D(1+2)-II, D3, D4, and D5) were analyzed by two dimensional cellulose acetate membrane electrophoresis after pronase digestion. All the fractions contained the 35S-labeled chondroitin sulfates A/C and heparan sulfate with the different proportions of the radioactivities. The results of the present study indicated that sulfated proteoglycans newly synthesized in myometrium of the estrogen-treated rabbit were considerably heterogeneous not only in the 35S-labeled glycosaminoglycan compositions but also in the molecular weight and buoyant density.

Animals↗
PubMed1983

Sialoglycopeptides obtained from a transplantable rat colorectal adenocarcinoma: a comparison with those from normal colonic mucosa.

A transplantable colorectal adenocarcinoma and the normal colonic mucosa derived from rats of ACI/N strain were digested successively with pronase, deoxyribonuclease, chondroitinase ABC, and heparitinase to obtain the corresponding glycopeptide fractions. The amino acid compositions of these two fractions suggested that the polypeptide backbones were quite similar. However, the electrostatic net charges of these fractions were shown to be different by cellulose acetate membrane electrophoresis, ion exchange chromatography, and measurement of sialic acid contents. The glycopeptide fraction derived from adenocarcinoma contained much greater quantities of less acidic glycopeptides than that derived from the normal colonic mucosa. The former exhibited much stronger blood group A and H activities than the latter. Moreover, the former reacted with Ricinus communis lectin I, whereas the latter did not react with this lectin. These results indicate that the carbohydrate structures of tumor sialoglycoproteins are different from those of the corresponding ones in the normal tissue from which the tumor has originated.

Amino Acids↗
PubMed1982

WDHA syndrome caused by VIP-producing ganglioneuroblastoma.

A 3 yr 11 mo-old girl showing classical symptoms of WDHA syndrome was transferred to our department of surgery. In preoperative examination, serum vasoactive intestinal peptide (VIP) was markedly elevated and pancreatic tumor was suspected. However, no tumor was found in the resected pancreas. Unfortunately, an unexpected adrenal tumor (ganglioneuroblastoma) was found in autopsy. The tumor was judged VIPO positive, immunohistochemically. This case was thought to be WDHA syndrome caused by VIPO-producing ganglioneuroblastoma (VIPoma).

Adenoma, Islet Cell↗
PubMed1982

Glycosaminoglycans of rat colorectal adenocarcinoma.

A transplantable colorectal adenocarcinoma and the normal colonic mucosa derived from rats of ACI/N strain were digested with pronase, and the glycosaminoglycan fractions were obtained by fractionation with cetylpyridinium chloride. The glycosaminoglycan fraction derived from the adenocarcinoma contained substantial amounts of chondroitin sulfate A/C, dermatan sulfate, heparan sulfate, and hyaluronic acid, whereas chondroitin sulfate A/C and dermatan sulfate were undetectable in that derived from the normal colonic mucosa. An increment in the heparan sulfate content was also apparent in the adenocarcinoma, while the level of hyaluronic acid appeared to be unchanged. Analyses of the extract of the tumor tissue with 5mM ethylenediaminetetraacetate (pH 7.0) indicated that heparan sulfate was present largely, if not completely, in the form of proteoglycan.

Adenocarcinoma↗
PubMed1981

Hormonal effects on the sulfation of sulfated glycoprotein in a particulate fraction of the endometrium of rabbit uterus.

A particulate fraction was separated from endometrial scrapings of the uterus of hormone- or sham-treated ovariectomized rabbit. The effects of estrogen and progesterone on the incorporation of [35S]sulfate from 3'-[35S]phosphoadenosine 5'-phosphosulfate (PAPS) into endogenous acceptors in the particulate fraction were investigated. Estrogen increased the incorporation of [35S]sulfate, but progesterone suppressed this effect. The results of DEAE-Sephadex A-25 (Cl-form) column chromatography of the pronase digest of the 35S-labeled substances indicated that the fraction eluted with 0.9 M NaCl (0.9 Fr) was most sensitive to the hormones. The major component in 0.9 Fr was resistant to crude heparinase, whereas the minor component was susceptible to this enzyme. The present observation, together with previous findings, suggested that the former was sulfated glycopeptide and the latter heparan sulfate. The results of the present study indicated that PAPS can serve as the direct "activated" sulfate donor in the enzymatic sulfation of sulfated glycoprotein in the particulate fraction, that the sulfation is greatly stimulated by pre-treatment of the rabbit with estrogen, and that the estrogen effect is suppressed by progesterone.

Animals↗
PubMed1981

Hormonal effects on the sulfation of sulfated glycoconjugates in the uterine endometrium of non-ovariectomized rabbit.

A particulate fraction was separated from endometrial scrapings of uterus of hormone-treated non-ovariectomized or intact rabbit. The effects of ovarial hormones on the incorporation of [35S]sulfate from 3'-[35S]phosphoadenosine 5'-phosphosulfate (PAPs) into endogenous acceptors in the particulate fractions were studied. Treatment of the animal with estrogen elevated the incorporation of [35S]sulfate, but exogenous progesterone suppressed this effect. The results of DEAE-Sephadex A-25 (Cl- form) column chromatography of the pronase digest of the 35S-labeled substances indicated that all the subfractions were sensitive to the hormones. The present observations, together with previous findings, suggest that the sulfation of sulfated glycoconjugates in the particulate fractions is stimulated by exogenous estrogen, but exogenous progesterone suppressed this effect, and also that endogenous ovarial hormones exert little influence on the effects of the present doses of these exogenous hormones on the sulfation. Therefore, non-ovariectomized rabbit can be used for rough evaluation of the effects of regular doses of these exogenous hormones on the sulfation of sulfated glycoconjugates in the uterine endometrium.

Adenine Nucleotides↗
PubMed1980

Isolation and characterization of a sulfated glycoprotein from a transplantable colorectal adenocarcinoma of rats.

A transplantable colorectal adenocarcinoma from rats of the ACI/N strain was extracted with 5 mM EDTA (pH 7.0), and fractionated by gel filtration on Sepharose 4B, followed by preparative poly(vinyl chloride) zone electrophoresis. An acidic glycoprotein (SGP) thus obtained was shown to be Homogeneous by electrophoresis on cellulose acetate membrane and on sodium dodecyl sulfate agarose gel. SGP contained 61.9% carbohydrate, 28.9% total amino acids and 1.4% sulfate. The major monosaccharides in SGP were galactose, glucosamine and galactosamine. Small quantities of sialic acid, L-fucose and mannose were also present. Threonine, serine, proline, glutamic acid and aspartic acid were the major amino acids of the protein moiety.

Adenocarcinoma↗
PubMed1980

Isolation and characterization of sulfated glycoproteins from the brush border fraction and the soluble fraction of rabbit small intestine.

The brush border fraction (Fr. P2) and the calcium chloride (10 mM)-soluble fraction (Fr. S) were separated from the small intestinal mucosa of rabbit. Sulfated glycoproteins, P-SGP and S-SGP, were then purified from Fr. P2 and Fr. S by zone electrophoresis and gel filtration, respectively. P-SGP and S-SGP were both electrophoretically homogeneous, although their mobilities differed from each other. P-SGP and S-SGP contained 61.8 and 35.% protein, 31.8 and 55.0% carbohdyrate, and 1.1 and 2.7% sulfate, respectively. The major constituent sugars in P-SGP and S-SGP were galactose and glucosamine, while mannose, sialic acid, and L-fucose were minor components. In addition, galactosamine was a major sugar in S-SGP, but a minor one in P-SGP. The major amino acids of the protein moiety of P-SGP were glutamic acid, aspartic acid, glycine, and alanine, while those of S-SGP were threonine, proline, glutamic acid, aspartic acid, serine, and glycine.

Amino Acids↗
PubMed1980

Heterogeneity of human urinary glycosaminoglycans.

Crude urinary glycosaminoglycans (GAG) obtained from normal adult men were fractionated by ethanol-fractionation, followed by Dowex 1 column chromatography. The resulting acidic subfractions were qualitatively analyzed for monosaccharide composition and examined by electrophoresis on cellulose acetate membrane and paper chromatography before and after mucopolysaccharidase digestions. Some of the major subfractions were also examined by gel filtration and infrared spectral analysis. The result showed that urinary GAG were extremely heterogeneous in the molecular size, negative charge and the chemical composition. Hyaluronic acid, heparan sulfate, chondroitin sulfates A and C, chondroitin, dermatan sulfate and keratan sulfate were found in wide distribution in these acidic subfractions. Of these GAG, chondroitin sulfate isomers were distributed into almost all acidic subfractions, indicating to be the most heterogeneous.

Adult↗