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Biomedical subjects

K Tomoda

Publications and source records attributed to K Tomoda.

At least 145 records · Page 8Linked to original sources

Type II collagen induced autoimmune salpingitis in the rat.

Previous studies showed type II collagen induced autoimmune salpingitis in Wistar rats. In this study we increased the number of animals and investigated whether or not type II collagen induced salpingitis is transferable by immune sera. Histopathological observations of salpingitis in the serum transferred rats were similar to those observed in the immunized rats but the degree of otopathological changes was less than that of immunized rats. Electronmicroscopic findings indicate an increased permeability in the capillaries and intercellular space and cellular infiltration in the submucosa of the immunized rats.

Animals↗

Serratia protease. Amino acid sequences of both termini, the 53 residues in the middle region containing the sole methionine residue, and a probable zinc-binding region.

Reexamination of the molecular mass and the amino acid composition of Serratia protease revealed the presence of 1 mol of methionine per mol of protein (about 46K daltons), and this was confirmed by BrCN cleavage followed by separation of the two fragments. The sole methionine residue was located near the middle region of the molecule. The amino(N)-terminal sequence was determined by Edman degradation of the protein and studies of several proteolytic peptides, establishing a sequence of 18 residues with a heterogeneous N-terminus. The carboxyl(C)-terminal sequence was determined by carboxypeptidase A digestion and tritium-labeling of the citraconylated C-terminal half segment to be -Phe-Ile-Val. The sequences of a total of 53 residues containing the methionine residue and a total of 38 residues containing two histidine residues were established by the application of various conventional methods to a BrCN peptide and several proteolytic peptides. The segment containing the histidine residues was homologous with that containing the two histidine residues chelating the zinc atom of thermolysin. The 38-residue segment may be directly connected to the 53-residue segment.

Amino Acid Sequence↗

Autonomic nervous system in human palatine tonsil.

The autonomic nervous system in the human palatine tonsil was studied systematically as follows: 1) Using the radio binding assay method, the presence of beta-adrenergic receptors and muscarinic-cholinergic receptors was demonstrated in the tonsil. 2) Using high performance liquid chromatography, the quantity of catecholamines in the tonsillar tissue was determined for the first time. 3) The distributions of sympathetic and parasympathetic nerves in the tonsillar tissue were demonstrated by fluorescence- or enzyme-histochemistry. 4) Cases of habitual tonsillitis were compared with cases of simple tonsillitis concerning the quantities of beta-adrenergic receptors and catecholamines. As a result, the difference in quantity of beta-adrenergic receptors between the two was insignificant, but the quantity of catecholamine was greater in the former.

Adrenergic Fibers↗

Closure of dural defects with proplast.

Defects of the dura mater, which are a source of cerebral spinal fluid leakage, may be produced by trauma and otologic and neurosurgical operations. Proplast was evaluated as a graft material to close dural defects in three animal models (cats). For comparison, temporalis fascia was similarly evaluated in an additional three cats. Microsurgical techniques were utilized to close the defects, and both materials successfully prevented cerebral spinal fluid leakage. Proplast, however, was judged superior when studied microscopically at three months. There was ingrowth of living dura into the Proplast and no evidence of inflammatory reaction.

Animals↗

Type II collagen-induced autoimmune endolymphatic hydrops in guinea pig.

Endolymphatic hydrops was induced in guinea pigs by immunizing them with native bovine type II collagen. Histopathologic changes consisted of moderate extension of the Reissner's membrane, spiral ganglion degeneration, atrophied organ of Corti, and mild atrophy of the surface epithelium in the endolymphatic duct. These findings suggest that an immune response directed against type II collagen--a type of collagen found in the membranous labyrinth, subepithelial layer of the endolymphatic duct, spiral ligament, and enchondral layer of the otic capsule--may induce endolymphatic hydrops.

Animals↗

Temporal bone findings in trisomy 13 with cyclopia.

Temporal bone findings in a fetus with trisomy 13 syndrome and cyclopia may be histopathologically characterized by the dysplasia of bony and membranous labyrinth and of the nervous system. In the left ear, there was a shortened cochlea housing a malformed Corti's organ appearing as a ribbonlike structure, an unexpected canal running obliquely through the scala tympani, a peculiar shape of the utricular macula and posterior canal crista, and a delayed ossifying process in the otic capsule. The poor development of the structures in the seventh and eighth nerves and their ganglions was observed in both ears. The type of anomaly can be classified as Mondini or Mondini-Alexander. The several anomalies might involve the organs that begin to develop during the period from five to eight gestational weeks.

Abnormalities, Severe Teratoid↗

Serum transfer of collagen-induced arthritis. II. Identification and localization of autoantibody to type II collagen in donor and recipient rats.

Collagen-induced arthritis can be transferred from immunized arthritic rats to unimmunized recipients by intravenous injection of an immunoglobulin concentrate of sera. This study identifies antibodies in the transfer concentrate which localize to the articular surface of cartilage in joints of recipients. Immunoglobulin can also be demonstrated in the same location in arthritic joints from rats after immunization. Antibody capable of transferring arthritis is present in donor rats over a period of at least 3 weeks and can be absorbed using homologous type II collagen. In addition, anti-type II collagen antibodies can be eluted from arthritic joints of rats with early disease.

Absorption↗

Type II collagen autoimmunity in otosclerosis and Meniere's Disease.

Antibodies to collagen types I, II, and IV were measured in patients with otosclerosis and patients with Meniere's disease. Levels of antibodies to type II collagen were significantly higher in these patients than in control subjects, while no differences were found among levels of antibodies to collagen type I or type IV. These observations suggest a possible role for type II collagen autoimmunity in the etiology of otosclerosis and Meniere's disease.

Autoantibodies↗

Initial sites of insulin cleavage and stereospecificity of carboxyl proteinases from Aspergillus sojae and Pycnoporus coccineus.

Initial cleavage sites of native insulin at a pH of about 3 and stereospecificity were investigated by fungal carboxyl proteinases (EC 3.4.23.6) from ASpergillus sojae, a species of fungi imperfecti, and Pycnoporus coccineus (formerly designated Trametes sanguinea), a wood deteriorating Basidiomycete, respectively. Fungal carboxyl proteinases were used as a model of vertebrate insulin degradation. A. sojae carboxyl proteinase I primarily hydrolyzed two peptide bonds located on the surface of native insulin monomer, the B16-B17 (Tyr-Leu) and B24-B25 (Phe-Phe) bonds, and secondarily the buried bonds, A15-A16 (Gln-Leu), B15-B16 (Leu-Tyr) and B14-B15 (ala-Leu), at pH 3.2 and 30 degree C. The initial cleavage sites of A. sojae carboxyl proteinases I towards native insulin were not identical with the initial cleavage sites towards the oxidized B chain of insulin. P. coccineus carboxyl proteinase Ia selectively hydrolyzed B14-B15 (Ala-Leu), B16-B17 (Tyr-Leu) and B24-B25 (Phe-Phe) bonds in the native insulin at pH 2.7. Based on these findings we suggest that the stereospecificity of the fungal carboxyl proteinases is similar to that of cathepsin D (EC 3.4.23.5), and that the synthesis and degradation of insulin may occur in microorganisms.

Amino Acid Sequence↗

A new method for evaluating mucolytic expectorant activity and its application. II. Application to two proteolytic enzymes, serratiopeptidase and seaprose.

Using our new method described in a preceding paper, in vivo effects of two proteolytic enzymes such as serratiopeptidase (SER) and seaprose (SAP) on sputa collected from bronchitis rabbits were examined. SER (20 mg/kg) and SAP (30 mg/kg) significantly reduced the viscosity of sputum (P less than 0.05) at the 1-3-h periods and the 4-6-h periods, respectively, after intraduodenal administration. 50 mg/kg of SER also significantly decreased not only viscosity (P less than 0.001) but also amount of freeze-dried substance (P less than 0.05) of sputum at the 1-3-h periods, but SAP did not affect the amount of dried substance. Both enzymes significantly increased the volume of sputum, probably as the result of liquefaction. Thus, mucolytic expectorant activity of both enzymes can be demonstrated first by the reduction in viscosity and next of the increase in volume of sputa. However, the decrease in amount of freeze-dried substance is not always in accord with the reduction viscosity.

Animals↗

A new method for evaluating mucolytic expectorant activity and its application. I. Methodology.

A new method for evaluating in vivo effect of mucolytic expectorants was devised. In this report, however, the focus is placed on methodology but not on pharmacology. Rabbits with subacute bronchitis were prepared by long-term exposure to minute amounts of SO2 gas. The sputum was quantitatively collected from the animal through a tracheal cannula at suitable time intervals according to the Perry and Boyd's method. As a preliminary study, changes in volume, viscosity and amounts of freeze-dried substance of sputa were examined after intraduodenal administration of water instead of mucolytic expectorants, the effects of which will be described in the subsequent paper, but no significant changes occurred with this test.

Animals↗

Histologic architecture of submucosal connective tissues in human eustachian tube with supplemental reference to the effects of aging.

Serial sections of 74 human eustachian tubes from 37 autopsy cases were examined microscopically to determine the histologic architecture of submucosal connective tissues. Abundant elastic fibers ran just beneath the mucosal epithelium of the eustachian tube. Two kinds of layers of collagenous fiber were observed an inner circular layer and an outer longitudinal layer. An "elastic fiber band" perfectly encircled the tubal lumen at the pharyngeal part of the eustachian tube. This band became less sharply defined at the osseous part. The two layers of collagenous fiber were contiguous, especially in the upper part of the tube, and ran from the pharyngeal orifice to the isthmus. Submucosal connective tissues were found to be undeveloped in fetal eustachian tubes. In children as well, elastic fibers were not fully developed, and circular banding of collagenous fibers was less marked. With advancing age, elastic fibers increased in number and became large and brittle. Both layers of collagenous fibers became thicker. The present data indicate that the submucosal connective tissues may play an important role in the elasticity of the eustachian tube itself and in the maintenance of the tubal framework. Gerontologic changes in the eustachian tube stroma have been considered pathophysiologically.

Adolescent↗

Interaction between Serratia protease and human plasma alpha 2 macroglobulin.

Serratia protease (TSP) [EC 3.4.24] was bound stoichiometrically to alpha 2 macroglobulin (alpha 2M), which was purified and crystallized from human plasma, but apo TSP was not bound. On formation of the TSP-alpha 2M complex the enzymatic activity of the bound TSP was affected with respect to substrates; Km values of the bound TSP were unchanged but Vmax values were reduced. alpha 2M was cleft at the mid-region of its subunits chains by TSP, which resulted in a conformational change of the alpha 2M molecule with TSP.

Electrophoresis, Polyacrylamide Gel↗