Epithelial-myoepithelial carcinoma arising in the submandibular gland: a case report with immunohistochemical study.
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Adult↗
Biomedical subjects
T Muramatsu
Publications and source records attributed to T Muramatsu.
Purification and characterization of a dipeptidyl carboxypeptidase from the polychaete Neanthes virens resembling angiotensin I converting enzyme.
Dipeptidyl carboxypeptidase (DCP) is well known as a mammalian angiotensin I converting enzyme (ACE) which plays an important role in blood pressure homeostasis. DCP was purified from the whole body of a polychaete, Neanthes virens. The purified enzyme was homogeneous by SDS-PAGE, with a molecular mass of 71 kDa by SDS-PAGE and 69 kDa by gel filtration, indicating that it is monomeric. The isoelectric point was 4.5 and optimum pH for the activity was 8.0. It showed a specific activity of 466.8 U/mg, which is the highest of known DCPs. The enzyme hydrolyzed angiotensin I to angiotensin II and sequentially released Phe-Arg and Ser-Pro from the C-terminus bradykinin, but does not cleave imido-bonds. Activity was completely inhibited by 1 mM EDTA and 5 mM o-phenanthroline, but it was not affected by serine and aspartic protease inhibitors. The original activity of EDTA-inactivated DCP was restored by addition of cobalt, manganese or low concentrations of zinc. The Km and Vmax values of the enzyme for Bz-Gly-His-Leu were 0.56 mM and 600 mumol/min per mg, respectively. The Ki values for specific mammalian ACE inhibitors, such as captopril and lisinopril, were 1.38 and 2.07 nM, respectively. In conclusion, we have shown the existence of a DCP from the polychaete, N. virens, with similar properties to those of mammalian ACE.
Animals↗
Foreign gene expression by in vivo gene electroporation in the quail testis.
To investigate whether or not foreign gene expression is attained in the testis of living Japanese quails, a firefly luciferase reporter gene was transfected by in vivo electroporation (EP), and transcriptional activity of different promoters was compared. In addition, the effect of the Epstein-Barr virus self-replication sequence was also tested. The results showed that luciferase activity in the testis reached almost a plateau value at 50 V. Under this EP condition, no difference was found in transcriptional activity between the simian virus 40 (SV40) and miw promoters. The reporter gene expression in the quail testis was observed over 28 days after in vivo gene EP, although the activity gradually decreased, and the presence of the Epstein-Barr virus self-replication sequence in the SV40 promoter did not significantly prolong the luciferase activity. These results suggest that in vivo gene EP confers strong, though transient, foreign gene expression in the Japanese quail, and it may provide a new powerful approach for studies on transcriptional regulation of genes during proliferation and differentiation of spermatogenic cells in the quail testis.
Animals↗
A case of chronic infantile type of fucosidosis: clinical and magnetic resonance image findings.
Fucosidosis is a rare autosomal recessive disorder resulting from a deficiency of alpha-L-fucosidase. In this report, we describe clinical and magnetic resonance image (MRI) findings of a chronic infantile type patient heterozygous for a nonsense mutation and a large deletion. The disease onset occurred at 2-3 years of age. She was bound to a wheelchair at 6 years of age, and developed dystonia at the age of 13 years. Brain MRI at 13 years of age showed marked cerebral and cerebellar atrophy, high intensities in the white matter of the frontal and occipital lobes, and low intensities of the bilateral thalamus, striatum, substantia nigra, red nucleus and mamillary bodies on T2-weighted images. The low intensities of basal ganglia on T2-weighted images seems characteristic of lesions in fucosidosis.
Adolescent↗
The role of hepatitis C virus infection in glomerulopathy.
The characteristics and prevalence of hepatitis C virus (HCV)-associated glomerulopathy remain to be determined. To analyze the relationship between HCV infection and glomerulopathy, we enrolled three groups of individuals or patients. The first group consisted of 7776 individuals who were seen for routine checkups. The second group consisted of 86 patients with chronic hepatitis C, 40 patients with chronic hepatitis B, and 51 patients with non-viral liver diseases. The third group consisted of nine patients with HCV association glomerulopathy who underwent renal biopsy. Of the 7776 individuals undergoing medical checkups, 142 (1.8%) were positive for HCV antibody. The positive rate of proteinuria was significantly higher (P<0.030) in individuals with HCV antibody (2.1%) than in those without the antibody (0.6%). Abnormal levels of serum creatinine (5.8 vs. 0%, P=0.025) and complications of cryoglobulinemia (45 vs. 5%, P<0.001) were significantly more common in the 86 patients with chronic hepatitis C (5.8%) than in the 91 patients with other liver diseases. All patients with abnormal levels of serum creatinine had concomitant cryoglobulinemia. Of the nine patients with histologically proven HCV-associated glomerulopathy, four had cryoglobulinemia (all were type II). Elevations of serum creatinine level (4/4 vs. 0/5, P=0.048) and a glomerular legion of membranoproliferative glomerulonephritis (3/4 vs. 0/5, P=0.048), a severe type of glomerulonephritis, were more common in the four patients with cryoglobulinemia than in the remaining five patients. In conclusion, HCV infection was found to be significantly associated with glomerulopathy. In addition, the presence of cryoglobulinemia, which usually accompanies membranoproliferative glomerulonephritis, was found to be an indicator of renal insufficiency in patients with HCV-associated glomerulopathy.
Journal Article↗
Cloning and sequence analysis of a gene (aly PG) encoding poly(alpha-L-guluronate)lyase from Corynebacterium sp. strain ALY-1.
The aly PG gene, coding for a poly alpha-l-guluronate lyase (PG lyase) of Corynebacterium strain ALY-1, was cloned and sequenced. The gene consists of 768 bp encoding a signal peptide of 32 amino acids and a mature protein of 224 amino acids. Two disulfide bond cross-linkages were found to be formed between Cys-4 and Cys-51 and between Cys-200 and Cys-206 in the native PG lyase molecule. The deduced amino acid sequence of the Corynebacterium sp. aly PG gene exhibited 29% homology toward that of the Klebsiella pneumoniae, subsp. aerogenes aly A gene, with two conserved regions (the amino acid sequences from Y-102 to M-110 and from Y-221 to Q-229).
Journal Article↗
Solution synthesis and biological activity of human pleiotrophin, a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five disulfide bonds.
Human pleiotrophin (hPTN), a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five intramolecular disulfide bonds, was synthesized by solution procedure in order to demonstrate the utility of our strategy using our newly developed solvent system, a mixture of trifluoroethanol (TFE) and dichloromethane (DCM) or chloroform (CHL). The final protected peptide was synthesized by coupling two larger protected intermediates, Boc-(1-64)-OH and H-(65-136)-OBzl, in CHL/TFE (3:1; v/v) using 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) in the presence of 3,4-dihydro-3-hydroxy-4-oxo-1,2,3-benzotriazine (HOOBt). After removal of all protecting groups using the HF procedure followed by treatment with Hg(OAc)2, the fully deprotected peptide was subjected to an oxidative folding reaction. The product was confirmed as having the correct disulfide structure by examining the cystine peptides obtained by enzymatic digestions, and as possessing the same biological activities as those of the natural product. The N- and C-terminal half domains (1-64 and 65-136) were also synthesized, and measurement of their biological activities indicated that the C-terminal half domain displays almost all the activities of the full-length molecule, whereas the N-terminal half domain shows almost no activity. From these results, we were able to confirm that the C-terminal half domain is responsible for the expression of biological activities in the same manner as human midkine (hMK), another heparin-binding neurotrophic growth factor.
Amino Acid Sequence↗
Expression of desmoglein I and plakoglobin in skin carcinomas.
Reduction or absence of cell-cell adhesion molecules has been reported in various carinomas and the abnormal expression of these molecules contributes to the invasive and metastatic behavior of malignant tumor cells. In epidermal keratinocytes, the main cell-cell adhesion systems are adherens junctions and desmosomes. Previous studies have shown that, in skin carcinomas, the decreased expression of E-cadherin, major constitutional glycoprotein of adherens junctions, is associated with the invasive and metastatic ability of the tumor cells. In the present study, we examined the expression of desmoglein I and plakoglobin, the constitutional components of desmosomes, in various skin carcinomas such as basal cell carcinoma (BCC), squamous cell carcinoma (SCC), extramammary Paget's disease and Bowen's disease by an immunofluorescence method. In normal human skin, desmoglein I and plakoglobin were strongly expressed in the intercellular space of the epidermis except for the basal cell layer. In BCC and SCC, the expression of desmoglein I and plakoglobin was markedly reduced or absent in tumor cells. In carcinoma in situ of Paget's disease, compared with the normal epidermal cells surrounding tumor cell nests, the expression of these molecules was reduced in tumor cells. In Paget's disease with dermal infiltration of tumor cells, the expression of these molecules was almost absent throughout the epidermis. In Bowen's disease, the expression of desmoglein I was reduced in the dumping cells and dyskeratotic cells. These results suggest that the expression of desmosomal cadherin is reduced or absent in human skin carcinomas, and that reduction of these molecules may also contribute to the invasiveness and metastasis of skin carcinomas.
Adult↗
Immunohistochemical study of type-1 blood antigen expressions in thyroid tumors: the significance for papillary carcinomas.
Immunohistochemical expressions of type 1 blood group antigens were studied for 95 cases of thyroid tumors, including 29 follicular adenomas, 23 follicular carcinomas, and 43 papillary carcinomas, applying monoclonal antibodies against DU-PAN-2, CA19-9, Lewis(a) (Le(a)), and Lewis(b) (Le(b)). Normal thyroid tissue invariably failed to express all four antigens. In follicular adenomas, DU-PAN-2 and CA19-9 were focally expressed in 7% and 21% of cases, and in follicular carcinomas, CA19-9 expression was limited to one case (4%); all cases were negative for DU-PAN-2. No or little expression of Le(a) or Le(b) was observed in these follicular tumors. In contrast, DU-PAN-2, CA19-9, Le(a), and Le(b) were expressed in 98%, 84%, 33%, and 49% of 43 papillary carcinomas, respectively. The positive stainings were observed mainly on the luminal surface of the tumor cells. The number of tumor cells that expressed DU-PAN-2 generally was greater than that of tumor cells that expressed CA19-9, Le(a), or Le(b). There was no significant difference in antigen expressions in female papillary carcinomas between subjects who were younger and older than 50 years old. The results suggest that DU-PAN-2 would be a useful immunohistochemical marker for distinguishing papillary carcinomas from follicular tumors. These immunohistochemical profiles imply the following: the activity of alpha2-3 sialyltransferase, a specific glycosyltransferase, would be more strongly enhanced in papillary carcinomas than in follicular tumors; the antigen expressions in papillary carcinomas may not be related to the alteration of the female sex hormone environment.
Adenocarcinoma, Follicular↗
Recurrent mucinous carcinoma of the skin invading to the frontal skull base.
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Adenocarcinoma, Mucinous↗
Recalcitrant subcorneal pustular dermatosis and bullous pemphigoid treated with mizoribine, an immunosuppressive, purine biosynthesis inhibitor.
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Adult↗
Midkine binds specifically to sulfatide the role of sulfatide in cell attachment to midkine-coated surfaces.
Midkine is a heparin-binding polypeptide which is implicated in the control of development and repair of various tissues. Recognition of sulfate groups in glycosaminoglycans is important for its function. To elucidate further its mechanism of action, the interactions of midkine with sulfated glycolipids were studied. Of various glycolipids and lipids examined, midkine bound strongly to sulfatide and cholesterol-3-sulfate (CHO-3-SO4) in a dose-dependent manner but failed to bind to other standard glycolipids and lipids. The properties of midkine binding to sulfatide and to CHO-3-SO4 differed in their sensitivity to inhibition by anionic polysaccharides, salt concentration and unlabeled midkine. Heparin inhibited midkine binding to sulfatide but weakly inhibited its binding to CHO-3-SO4. Liposomes bearing sulfatide carried out significant interactions with immobilized midkine, whereas those bearing CHO-3-SO4 did not. Incorporation of sulfatide into 32D cells and trypsinized COS cells enhanced 125I-labelled midkine binding, whereas incorporation of ganglioside or galactosylceramide had no effect. Furthermore, sulfatide-incorporated cells enhanced cell attachment to midkine-coated coverslips. These results indicate that midkine binds to sulfatide under physiological conditions and the midkine-sulfatide interaction may be important in controlling cell attachment.
Adsorption↗
A heparin-binding growth factor, midkine, binds to a chondroitin sulfate proteoglycan, PG-M/versican.
Midkine is a heparin-binding growth factor with survival-promoting and migration-enhancing activities. In order to understand the regulation of midkine signaling, we isolated midkine-binding proteoglycans from day 13 mouse embryos, when midkine is intensely expressed. Deglycosylation followed by SDS/PAGE revealed various protein bands; one of these was identified as PG-M/versican by in gel trypsin digestion and sequencing the resulting peptides. PG-M/versican isolated from day 13 mouse embryos bound midkine with a Kd of 1.0 nM. Pleiotrophin/heparin-binding growth-associated molecule, which has a structure related to midkine, was also bound similarly. Digestion with chondroitinase ABC, AC-I or B abolished the binding to midkine. Heparin as well as chondroitin sulfate D and E inhibited the binding. After chondroitinase ABC digestion, the midkine-binding PG-M/versican released 4-sulfated, 6-sulfated, 2, 6-disulfated and 4,6-disulfated unsaturated disaccharides. These results suggest that midkine binds to a polysulfated domain in the chondroitin sulfate chain with a region of dermatan sulfate structure. This proteoglycan may modulate the midkine activity, as binding to midkine can enhance midkine action by concentrating it to the cell periphery or inhibit the action by competing with the binding to a signaling receptor.
Amino Acid Sequence↗
Homo-oligomer formation by basigin, an immunoglobulin superfamily member, via its N-terminal immunoglobulin domain.
Basigin (Bsg) is a highly glycosylated transmembrane protein with two immunoglobulin (Ig)-like domains. A number of studies, including gene targeting, have demonstrated that Bsg plays pivotal roles in spermatogenesis, implantation, neural network formation and tumor progression. In the present study, to understand the mechanism of action of Bsg, we determined its expression status on the plasma membrane. Cotransfection of Bsg expression vectors with two different tags clarified that Bsg forms homo-oligomers in a cis-dependent manner on the plasma membrane. If the disulfide bond of the more N-terminally located Ig-like domain was destroyed by mutations, Bsg could not form oligomers. In contrast, the mutations of the C-terminal Ig-like domain or N-glycosylation sites did not affect the association. The association of mouse and human Bsgs, which exhibit high homology in the transmembrane and intracellular domains but low homology in the extracellular domain, was very weak as compared with that within the same species, suggesting the importance of the extracellular domain in the association. If the extracellular domain of the human Ret protein was replaced with the N-terminal Ig-like domain of Bsg, the resulting chimera protein was associated with intact wild-type Bsg, but not if the C-terminal Ig-like domain, instead of the N-terminal one, of Bsg was used. No oligomer formation took place between the intact wild-type Ret and Bsg proteins. In conclusion, these data indicate that the N-terminal Ig-like domain is necessary and sufficient for oligomer formation by Bsg on the plasma membrane.
Animals↗
Distinct expression of midkine and pleiotrophin in the spinal cord and placental tissues during early mouse development.
Midkine and pleiotrophin comprise a family of heparin-binding growth factors, and are expressed in overlapping tissues during the mid- to late-gestation periods of mouse development. Their distinct expression during early mouse development, as revealed by in situ hybridization, was reported. Midkine was expressed in the embryonic ectoderm from as early as embryonic day (E5.5). In the neural tube midkine was expressed specifically in the neuroepithelium, that is, in the whole area of the neural tube at E9.5, and in the ventricular zone from E10.5-13.5. At E15.5, when the neuroepithelium disappeared, midkine concomitantly became undetectable. In contrast, pleiotrophin expression started exclusively in the neural plate at E8.5, and in the lateral plate of the neural tube at E9.5. It then became restricted to a dorsal ventricular zone from E11.5-13.5, and finally to the central gray neurons at E15.5. Moreover, pleiotrophin was expressed in the ventral horns. Among placental tissues, midkine was detected in the chorion, the fetal component of the placenta, whereas pleiotrophin was found in the decidua basalis, the maternal component of the placenta. The distinct expression of midkine and pleiotrophin suggests their differential role in early development.
Animals↗
The single-stranded DNA- and RNA-binding proteins pur alpha and pur beta link BC1 RNA to microtubules through binding to the dendrite-targeting RNA motifs.
Neural BC1 RNA is distributed in neuronal dendrites as RNA-protein complexes (BC1 RNPs) containing Translin. In this study, we demonstrated that the single-stranded DNA- and RNA-binding protein pur alpha and its isoform, pur beta, which have been implicated in control of DNA replication and transcription, linked BC1 RNA to microtubules (MTs). The binding site was within the 5' proximal region of BC1 RNA containing putative dendrite-targeting RNA motifs rich in G and U residues, suggesting that in the cytoplasm of neurons, these nuclear factors are involved in the BC1 RNA transport along dendritic MTs. The pur proteins were not components of BC1 RNP but appeared to associate with MTs in brain cells. Therefore, it is suggested that they may transiently interact with the RNP during transport. In this respect, the interaction of pur proteins with BC1 RNA could be regulated by the Translin present within the RNP, because the binding mode of these two classes of proteins (pur proteins and Translin) to the dendrite-targeting RNA motifs was mutually exclusive. As the motifs are well conserved in microtubule-associated protein 2a/b mRNA as well, the pur proteins may also play a role(s) in the dendritic transport of a subset of mRNAs.
Animals↗
Serum midkine levels are increased in patients with various types of carcinomas.
The level of expression of midkine (MK), a heparin-binding growth factor, is increased in many types of human carcinomas. An enzyme-linked immunoassay, which utilizes a combination of rabbit and chicken antibodies revealed that serum MK level in the controls (n = 135) was 0.154 +/- 0.076 (mean +/- SD) ng ml(-1)with an apparent cut-off value as 0.5 ng ml(-1). Serum MK level was significantly elevated in the cancer patients (n = 150) (P< 0.001); 87% of the patients showed levels of more than 0.5 ng ml(-1). All ten types of cancer examined showed a similar profile of serum MK level. There was no or weak correlation between C-reactive protein level, a marker of inflammation, and serum MK level. Furthermore, in case of gastric carcinoma and lung carcinoma, patients with stage I carcinoma already showed elevated serum MK levels. The present results indicated that serum MK could serve as a general tumour marker with a good potential for clinical application.
Adult↗
Connexins in salivary glands.
Connexins (Cxs) make up a family of gap junction structural proteins that form hexameric assemblies in the plasma membranes of adjacent cells that interact to form intercellular channels. It has been demonstrated that many kinds of CXs are differentially expressed in a variety of tissues; however, there have been only a few studies of CX expression in rat salivary glands. The co-localization of CX26 and 32 was examined in the parotid glands. Double immunofluorescence revealed that CX26 and 32 were present in the same gap junction. Double immuno-electron microscopy showed co-localization of both CX26 and 32 on the same gap junctional membranes between acinar cells. These results suggest that CX26 and 32 may participate in regulation of secretory function and permeability of acinar cells in the rat parotid glands.
Animals↗