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H Inouye

Publications and source records attributed to H Inouye.

At least 37 records · Page 2Linked to original sources
PubMed1995

[Epidemiological studies on enteric adenovirus gastroenteritis in children].

Enteric adenoviruses (EAd), adenovirus (Ad) types 40 and 41, have been established as causative agents of gastroenteritis. By electron microscopic (EM) survey of acute gastroenteritis in children in the Matsuyama area, Ad were detected in 275 of 6476 fecal samples obtained from 1980 to 1993. Two-hundred-thirteen Ad-positive samples were tested for serotyping by the enzyme-linked immunosorbent assay (ELISA) using three monoclonal antibodies, Ad group-specific, Ad 40 type-specific and Ad41 type-specific antibody. Of 199 samples serotyped by ELISA, 65 were identified as Ad40, 73 as Ad41, 1 as double infection with Ad40 and Ad41, and 60 as Non-EAd. About 70% of Adenovirus detected by EM were suggested to be EAd. Other epidemiological feature was as follows: EAd were detected throughout the year. The predominant serotype was Ad40 during 1980-1985, while Ad41 were observed after 1986. EAd were detected most frequently from the children aged 0-3 years. The incidence of fever in EAd positive group was lower (30%) than that (67%) in the Non-EAd positive group. The incidence of vomiting, nausea and respiratory symptoms was higher in Ad41 associated infections than Ad40.

Adenoviridae↗
PubMed1994

X-ray scattering from a discrete helix with cumulative angular and translational disorders.

X-ray scattering from a discrete helix possessing cumulative angular and translational disorders is studied by the Barakat model [Barakat (1987). Acta Cryst. A43, 45-49] assuming Gaussian distributions for random rotations and translations between subunits. This model is found to be identical to the paracrystalline model of the second kind. The intensity function shows that the intensity maximum decreases with increase in the Bessel order, whereas the peak breadth in the fiber direction and the intensity minimum increase.

Mathematical Computing↗
PubMed1994

Thrombin-induced platelet aggregation, phosphoinositide metabolism and protein phosphorylation in NIDDM patients treated by diet, sulphonylurea or insulin.

We studied thrombin-induced metabolism of phosphoinositide, protein phosphorylation and platelet aggregation in platelets from 32 NIDDM patients and 12 control subjects. To clarify the effect of diet, sulphonylureas, or insulin treatment, the subjects were divided into three groups based on the type of treatment. Thrombin-induced platelet aggregation was measured with an aggregometer. Low-dose thrombin (0.25 U/ml)-stimulated platelet aggregation in diabetic patients was significantly increased compared with the control subjects. Platelet aggregation in the sulphonylurea and insulin groups was significantly lower than in the diet group. On the other hand, in platelets incubated with [32P]orthophosphate, thrombin-induced incorporation of 32P radioactivity into phosphatidic acid (PA) was significantly lower in the sulphonylurea and insulin groups than in the diet group. Thrombin-induced incorporation of [32P] radioactivity into phosphatidylinositol (PIP) for 10 s was significantly higher in the sulphonylurea group than in the diet group. There were no differences in thrombin-induced 47 kDa protein phosphorylation between platelets from the diet, sulphonylurea, or insulin groups. These results suggest that sulphonylureas and insulin induce suppression of thrombin-induced activation of phospholipase C, which mediates hydrolysis of PIP and PIP2 and production of PA, which leads to inhibition of platelet aggregation.

Adult↗
PubMed1994

Membrane topology of PLP in CNS myelin: evaluation of models.

Three new models for proteolipid protein (PLP) topology in the myelin membrane have been proposed--the 4-helix N(in) and N(out) models of Popot (J. Membr. Biol. 120:233-246), and the model of Weimbs and Stoffel (Biochemistry 31:12289-12296). Unlike the earlier models proposed by Laursen (Proc. Natl. Acad. Sci. USA 81:2912-2916), Stoffel (Proc. Natl. Acad. Sci. USA. 81:5012-5016) and Hudson (J. Cell Biol. 109:717-727), the four hydrophobic clusters are all assigned as membrane-spanning domains. The Popot-N(in) and Weimbs models, which are similar to the Laursen model, both assign the positively-charged domain, which is deleted from the DM20 transcript of PLP, to the cytoplasmic surface, while the Popot-N(out) model, similar to the Stoffel and Hudson models, assigns this sequence to the extracellular surface. Our calculations of membrane surface charge shows that the disposition of this basic domain greatly influences membrane interactions, by shifting the equilibrium myelin period to alkaline pH due to the electrostatic repulsion force at the extracellular apposition. In the Laursen, Popot-N(in) and Weimbs models, the onset of swelling was calculated to be at lower pH than in the Stoffel, Hudson and Popot-N(out) models, and lower than that observed experimentally with mouse optic nerve myelin. The absolute electron density profile of the myelin membrane that is derived from the x-ray diffraction patterns shows similar density levels at its cytoplasmic and extracellular surfaces. By contrast, the electron density profile calculated from a chemical model that includes lipids plus myelin basic protein (but not PLP) shows a higher density at the cytoplasmic than at the extracellular side.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Increased insulin sensitivity in patients with aldosterone producing adenoma.

OBJECTIVE: Primary aldosteronism is a recognized endocrine cause of glucose intolerance. A blunted insulin response to glucose in patients with primary aldosteronism is well known, but insulin sensitivity has not been thoroughly determined. We investigated insulin sensitivity and insulin secretion in patients with aldosterone producing adenoma. DESIGN: Glucose tolerance and insulin responses to glucose were evaluated using a standard 75 g oral glucose tolerance test in patients with aldosterone producing adenoma before and after surgery, and in control subjects. Parameters for insulin resistance (HOMA-R) and pancreatic beta-cell function (HOMA-beta F) were derived from a homeostasis model assessment. PATIENTS: Fifteen patients with aldosterone producing adenoma and 41 control subjects with normal glucose tolerance matched for age and body mass index, were studied. Eight patients were re-evaluated after surgical removal of the adenoma. In 5 patients 125I-insulin binding to erythrocytes was also measured. MEASUREMENTS: Plasma glucose was measured by a glucose oxidase method. Plasma insulin, aldosterone and renin activity were measured by radioimmunoassay. RESULTS: Both fasting plasma glucose and insulin were lower in the patients than in the controls. Although the areas under the curve for plasma glucose during the oral glucose tolerance test did not differ, that for plasma insulin was less in the patients with hyperaldosteronism. Insulin sensitivity was increased in the patients, as evidenced by decreased HOMA-R compared with controls, while HOMA-beta F was comparable between the groups. 125I-insulin binding to erythrocytes was higher in 5 patients than in 19 normal controls. After surgical removal of adenoma, neither fasting plasma glucose nor the glucose area under the curve during the oral glucose tolerance test changed. However, fasting plasma insulin and the insulin area under the curve increased significantly. HOMA-R increased and HOMA-beta F remained unaltered. CONCLUSION: Insulin sensitivity was increased in untreated patients with aldosterone producing adenoma. Enhanced insulin receptor binding may contribute to this increased insulin sensitivity.

Adenoma↗
PubMed1994

1H-NMR analysis of nerve edema in the streptozotocin-induced diabetic rat.

To define the existence of intracellular hydration caused by metabolic derangements in the excised sciatic nerves of diabetic rats quantitatively, relaxation times (T1, T2) and fraction of intracellular water content were measured with 1H-nuclear magnetic resonance (NMR) spectroscopy in normal rats (control group, n = 10), streptozotocin (STZ)-induced (50 mg/kg, i.v.) diabetic rats (DM group, n = 10), STZ-induced diabetic rats treated with an aldose reductase inhibitor (ARI, Epalrestat, 100 mg/kg) (ARI group, n = 8), and STZ-induced diabetic rats treated with insulin (insulin group, n = 4). For selective measurement of intracellular relaxation times, the inversion recovery (IR) method for conventional T1 and Carr-Purcell-Meiboom-Gill method for T2 were used with an aqueous chemical shift reagent, 10 mmol/L dysprosium triethylenetetramine-N,N,N',N",N"',N"'-hexaacetic acid, resulting in distinct separation of intracellular (Schwann cell, axon, endothelial cell, and pericyte) and extracellular waters under the isotonic condition of the rat sciatic nerves. Furthermore, a new method of driven-equilibrium single-pulse observation of T1 (DESPOT) was used for rapid measurement of T1 for the purpose of clinical application on magnetic resonance imaging (MRI). T1 values measured by the DESPOT and IR methods were significantly correlated (p < 0.001). Total and intracellular water contents, sorbitol contents, and relaxation times of the sciatic nerve taken from the DM group were significantly elevated (p < 0.01), while myoinositol (p < 0.01) and extracellular water (p < 0.05) contents were significantly decreased as compared with the control group. Both insulin and ARI treatments significantly improved relaxation times as compared with those in the DM group (p < 0.05-0.01). Relaxation times correlated positively with total water (T1, p < 0.05-0.01; T2, p < 0.01), intracellular water (T1, p < 0.001; T2, p < 0.001), and sorbitol (T1, p < 0.001; T2, p < 0.001) contents of the excised nerve. Sorbitol content correlated positively with total and intracellular water contents (p < 0.01) but negatively with extracellular water content (p < 0.05). These findings indicated that sorbitol itself and/or secondary sodium accumulation caused by an increase in sorbitol may be a major contributor to the increase in intracellular hydration and prolonged relaxation times associated with hyperglycemia, which are reversible with insulin or ARI treatment. It was also suggested that rapid T1 measurement would provide new insights into the pathogenesis of human diabetic neuropathy as a non-invasive evaluation method on MRI.

Aldehyde Reductase↗
PubMed1993

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

To elucidate the relation between amyloid fibril formation in Alzheimer disease and the primary structure of the beta/A4 protein, which is the major component of the amyloid, we have been investigating the ability of peptides sharing sequences with beta/A4 to form fibrils in vitro. In previous studies we focused on the macroscopic morphology of the assemblies formed by synthetic peptides corresponding in sequence to different regions of this protein. In the present study we analyze the x-ray diffraction patterns obtained from these assemblies. All specimens showed wide angle reflections that could be indexed by an orthogonal lattice of beta-crystallites having unit cell dimensions a = 9.4 A, b = 7 A, and c = 10 A, where a refers to hydrogen bonding direction, b to polypeptide chain direction, and c to intersheet direction. Given the amino acid sequence of beta/A4 as NH2-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIAT-COOH, we found that, based on their orientation and assembly, the analogues could be classified into three groups: Group A, residues 19-28, 13-28, 12-28, 11-28, 9-28, 1-28, 1-38, 1-40, 6-25, 11-25 and 34-42; Group B, residues 18-28, 17-28, and 15-28; and Group C, residues 22-35 and 26-33. For Groups A and C, the sharpest reflections were (h00), indicating that the assemblies were fibrillar, i.e., elongated in a single direction. Lateral alignment of the crystallites in Group A account for its cross-beta pattern, in which the hydrogen bonding (H-bonding) direction is the fiber (rotation) axis. By comparison, the beta-crystallites of Group C had no preferential orientation, thus giving circular scattering. For Group B, the sharpest reflections were (h0l) on the meridian, indicating that the assemblies were plate-like, i.e., extended in two directions. A series of equatorial Bragg reflections having a 40 A period indicated regular stacking of the plates, and the rotation axis was normal to the surface of the plates. Of the Group A peptides, the analogues 11-28 and 6-25 showed intensity maxima on the equator as well as on higher layer lines, indicating that the beta-crystallites are highly ordered relative to one another in the axial, H-bonding direction. This sampling of the layer lines by a larger period (60 A) suggests that the beta-crystallites are arrayed either in cylindrical or small restricted crystalline lattices. Consistent with its electron microscopic images, we modeled the structure as a tube with five or six f,-crystallites constituting the wall and with the individual crystallite, which either rotates freely or is restricted, made of five or fewer beta-pleated sheets. For the Group B peptides, the electron density projection along the b-axis was calculated from the observed intensities using phase combinations from fl-keratin.Amino acid side-chain positions were apparent and, when refined as 4-A-diameter spheres, led to a substantial decrease in the R-factors.For peptide 18-28 the electron density peaks, which are thought to correspond to side chains, were centered 3.3 A from the peptide backbone, whereas for peptides 17-28 and 15-28, these peaks were centered 1 A or more further from the backbone. Peaks having high electron density faced peaks having lower density, suggesting a favorable stereochemical arrangement of the residues. Thus, our analysis of the fiber x-ray patterns from beta/A4 peptides shows the organization of the beta-crystallites that form the wall of the amyloid fibrils as well as possible side-chain interactions.

Amino Acid Sequence↗
PubMed1993

Myelin P0-glycoprotein: predicted structure and interactions of extracellular domain.

Protein zero (P0), a transmembrane glycoprotein, accounts for over 50% of the total protein in PNS myelin. The extracellular domain of P0 (P0-ED) is similar to the immunoglobulin variable domain, carrying one acceptor sequence for N-linked glycosylation. The x-ray diffraction analysis of PNS myelin has demonstrated reversible transitions that depend on pH and ionic strength, resulting in three distinct structures characterized by widths of about 36 A, 50 A (native), and 90 A between the extracellular surfaces of the membranes. In the current work, we considered the constraints imposed by these x-ray diffraction data on the orientation of P0-ED, and we propose how this immunoglobulin-like domain could be accommodated in the variable widths of the extracellular space between myelin membranes. The modeling made use of the finding that beta-strand predictions for P0-ED are virtually superimposable with those of the VH domain of the phosphocholine-binding immunoglobulin M603 of mouse, which has a similar number of residues as P0-ED and a structure that has been solved crystallographically. The dimensions of P0-ED from the space-filling model, developed using PC-based molecular modeling software, were found to be 44 A x 25 A x 23 A. On the assumption that neither the shape nor the orientation of P0-ED changes appreciably, then the different widths at the extracellular apposition would easily accommodate P0-ED from apposed membranes if the molecules were oriented so that the beta-strands were approximately perpendicular to the membrane surface.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1992

Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein.

Deposition of extraneuronal fibrils that assemble from the 39-43 residue beta/A4 amyloid protein is one of the earliest histopathological features of Alzheimer's disease. We have used negative-stain electron microscopy, Fourier-transform infrared (FT-IR) spectroscopy, and fiber X-ray diffraction to examine the structure and properties of synthetic peptides corresponding to residues 1-40 of the beta/A4 protein of primate [Pm(1-40); human and monkey], rodent [Ro(1-40); with Arg5-->Gly, Tyr10-->Phe, and His13-->Arg], and hereditary cerebral hemorrhage with amyloidosis of the Dutch type (HCHWA-D) [Du(1-40); with Glu22-->Gln]. As controls, we examined a reverse primate sequence [Pm*(40-1)] and an extensively substituted primate peptide [C(1-40); with Glu3-->Arg, Arg5-->Glu, Asp7-->Val, His13-->Lys, Lys16-->His, Val18-->Asp, Phe19-->Ser, Phe20-->Tyr, Ser26-->Pro, Ala30-->Val, Ile31-->Ala, Met35-->norLeu, Gly38-->Ile, Val39-->Ala, and Val40-->Gly]. The assembly of these peptides was studied to understand the relationship between species-dependent amyloid formation and beta/A4 sequence and the effect of a naturally occurring point mutation of fibrillogenesis. The three N-terminal amino acid differences between Pm(1-40) and Ro(1-40) had virtually no effect on the morphology or organization of the fibrils formed by these peptides, indicating that the lack of amyloid deposits in rodent brain is not due directly to specific changes in its beta/A4 sequence. beta-Sheet and fibril formation, judged by FT-IR, was maximal within the pH range 5-8 for Pm(1-40), pH 5-10.5 for Du(1-40), and pH 2.5-8 for Ro(1-40).(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1991

Role of adrenal and gonadal androgens in insulin action and metabolism.

In a previous report we found extreme hyperinsulinemia associated with high testosterone levels in patients with polycystic ovarian syndrome (PCO) and normal insulin levels in a small group of patients with elevated dehydroepiandrosterone (DHEA). From these observations, we hypothesized that DHEA and testosterone may have opposing actions on insulin sensitivity. To test this hypothesis, we studied insulin sensitivity in vivo and in vitro in a) obese PCO women with elevated testosterone, b) obese patients with adult-onset adrenal hyperplasia (AH) and high levels of DHEA, c) weight-matched obese controls, and d) lean controls. Insulin sensitivity was determined by insulin responses to a standard OGTT, hypoglycemic responses to an IV insulin tolerance test (ITT), red blood cell (RBC) insulin binding and receptor kinase activity, and phytohemagglutinin (PHA)-activated T-lymphocyte (T-cell) insulin binding and PDH insulin sensitivity. In PCO patients, we found that basal and glucose-challenged insulin levels were significantly greater than, and hypoglycemic responses to IV insulin, significantly lower than, weight-matched control values. However, AH patients had insulin values significantly below, and hypoglycemic responses significantly above, those of the weight-matched controls. Their values were, in fact, comparable to those observed for the lean control subjects. Similar findings were observed with insulin binding and PDH insulin sensitivity. Insulin sensitivity in all study subjects was found to be negatively correlated to testosterone and positively correlated to DHEA and, more significantly, to the ratio of DHEA/testosterone. These data would suggest that, in females, DHEA and T may have opposing actions on insulin sensitivity. We conclude that in females insulin sensitivity in vivo and in vitro is modulated, at least in part, by the ratios of DHEA to testosterone.

Adrenal Glands↗
PubMed1991

Folding and function of the myelin proteins from primary sequence data.

To explain how the myelin proteins are involved in the organization and function of the myelin sheath requires knowing their molecular structures. Except for P2 basic protein of PNS myelin, however, their structures are not yet known. As an aid to predicting their molecular folding and possible functions, we have developed a FORTRAN program to analyze the primary sequence data for proteins, and have applied this to the myelin proteins in particular. In this program, propensities for the secondary structure conformations as well as physical-chemical parameters are assigned to the amino acids and the pattern of these parameters is examined by calculating their average values, autocorrelation functions and Fourier transforms. To compare two proteins, their sequences are aligned using a unitary scoring matrix, and homologies are searched by plotting a two-dimensional map of the correlation coefficients. Comparison of the corresponding myelin basic proteins (MBP) and P0 glycoproteins (P0) for rodent and shark showed that the conserved residues included most of the amino acids which were predicted to form the alpha or beta conformations, while the altered residues were mainly in the hydrophilic and turn or coil regions. In both rodent and shark the putative extracellular domain of P0 glycoprotein displayed consecutive peaks of beta propensity similar to that for the immunoglobulins, while the cytoplasmic domain showed alpha-beta-alpha folding. To trace the immunoglobulin fold along the P0 sequence, we compared the beta propensity curve of P0 with that of the immunoglobulin M603, whose three-dimensional structure has been determined. We propose that the flat beta-sheets of P0 are orientated parallel to the membrane surface to facilitate their homotypic interaction in the extracellular space. An extra beta-fold in the extracellular domain of shark P0 compared with rodent P0 was found, and this may result in a greater attraction between the apposed extracellular surfaces and may account for a smaller extracellular space as measured by x-ray diffraction. A computer search of the myelin protein sequences for functional motifs revealed sites for N-glycosylation, phosphorylation, nucleotide binding, and certain enzyme activities. We note especially that there are potential nucleotide binding sites in proteolipid protein (PLP), MBP and 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP). This is consistent with the experimental observations that PLP acts like an ionophore or proton channel when reconstituted into planar lipid bilayers, MBP binds GTP, and CNP catalyzes in vitro the hydrolysis of 2',3'-nucleotides into corresponding 2'-nucleotides.

2',3'-Cyclic Nucleotide 3'-Phosphodiesterase↗
PubMed1991

Morphology and antibody recognition of synthetic beta-amyloid peptides.

To elucidate the relationship between amyloid fibril formation in Alzheimer disease (AD) and the primary structure of the beta-amyloid protein (beta-AP), we investigated the ability of peptides sharing sequences with beta-AP to form fibrils in vitro and to recognize anti-beta-amyloid antisera. The peptides, which were synthesized using a FMOC solid phase procedure and purified by HPLC, consisted of residues 6-25 from the putative aqueous domain, residues 22-35, which overlaps the putative aqueous and transmembrane domains, and residues 1-38 and 1-40 representing nearly the full length of beta-AP. Electron microscopy of negative-stained or thin-sectioned preparations revealed that the peptides assembled into fibrils having different morphologies, some of which resembled in situ AD amyloid. Peptide 6-25 fibrils had diameters of 50-80 A and occasionally showed a central groove suggestive of constituent filaments. Cross sections of the fibril showed a penta- or hexameric arrangement of globular subunits with diameters of 25-30 A. Peptide 22-35 fibrils were helical, with a pitch of 1,100 A and a width of 120 A at its greatest and 50-60 A at its narrowest. The fibrils formed by peptides 1-38 and 1-40 were 70-90 A in diameter. When the peptide assemblies were singly oriented by sedimentation or doubly oriented in a magnetic field, their X-ray diffraction patterns all showed reflections typical of a cross-beta pleated sheet conformation. The patterns differed mainly in their small-angle equatorial intensity, which arises from the packing of fibrils having different widths. Antiserum raised to either native amyloid or to synthetic peptide beta-(1-28) was highly reactive in an inhibition-ELISA assay to beta-(6-25) and beta-(1-38), but not to beta-(22-35), and immunostained beta-(1-40) on Western blots. These studies show that the beta-(6-25), beta-(1-38) and beta-(1-40) peptides can assemble into cross-beta fibrils that retain epitopes characteristic of AD amyloid.

Amino Acid Sequence↗
PubMed1991

[Enzyme-linked immunosorbent assay using monoclonal antibodies for direct serotyping of enteric adenoviruses in feces].

We were prepared three monoclonal antibodies in which the monoclone 12D was type specific for Adenovirus 40 (Ad40), 1F was type specific for Ad41 and 15D was group specific for Ads. For identification of enteric adenoviruses (EAd) in stool specimens, enzyme-linked immunosorbent assay (ELISA) test using monoclonal antibodies was developed. Results of identification by the ELISA tests using monoclonal antibodies to EAd on 15 fecal samples in which Ad particles were found by electron microscopy showed complete coincidence to those of Sma 1 restriction endonuclease cleavage. From these results, the ELISA tests employing EAds type specific monoclonal antibodies proved to be specific and this was a rapid technique for laboratory diagnosis of EAd in fecal specimens of viral gastroenteritis. Fifty-eight fecal samples with Ad particles positive by EM were serotyped by the ELISA using monoclonal antibodies. Eleven fecal samples were identified as Ad40, 25 as Ad41, 1 as double infection with Ad40 and Ad41, and 4 as non-EAd. These results indicated that Ad41 was more dominant than Ad40 during April, 1986 to January, 1989 in Matsuyama city.

Adenoviruses, Human↗
PubMed1991

Helicobacter pylori is not a co-carcinogen in N-methyl-N'-nitro-N-nitrosoguanidine-induced rat gastric carcinogenesis.

Helicobacter pylori was implicated in gastric carcinogenesis through the induction of metaplasia of the gastric mucosa. In this experiment a co-carcinogenic effect of H. pylori on chemically induced gastric carcinogenesis was examined. Wistar WKY male rats received drinking water containing 50 mg/l of N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), and intragastric administration of 10(6) to 10(8) colony forming unit of H. pylori thrice a week for 40 weeks. Thus, 3 groups were assigned as Group I; MNNG alone, Group II; MNNG + vehicle, and Group III; MNNG + H. pylori (n = 30, each). At autopsy, 9 rats (30%) had 7 glandular stomach and 3 duodenal tumors in Group I, and 10 rats (33%) had 8 glandular stomach and 2 duodenal tumors in Group II, whereas in Group III 4 rats (13%) had 2 glandular stomach and 2 duodenal tumors (chi 2 = 4.257, P < 0.15 for the incidences of glandular stomach tumors among 3 groups). The finding seems to suggest that H. pylori has an ambitendency in the gastritis-metaplasia-carcinogenesis sequence as a promoter for the induction of the predisposing mucosa and as an inhibitor against certain carcinogens.

Animals↗
PubMed1990

The primary structure and analysis of the squid kinesin heavy chain.

We report the cDNA sequence of the squid kinesin heavy chain and compared the predicted amino acid sequence with that of the Drosophila heavy chain as reported by Yang, J.T., Laymon, R.A., and Goldstein, L.S. B. (1989) Cell 56, 879-889). We compared the two kinesin sequences with regard to the predicted physicochemical parameters of hydrophobicity, charge, and propensities of the secondary conformations. A comparison of the sequences from the two species reveals the head, stalk, and tail domains because a reduced degree of conservation demarcates the stalk. The charge profile indicates that the head region is nearly neutral, the stalk region acidic, and the tail is basic. The Fourier transform analysis of the hydrophobic profile of the stalk shows predominant peaks at 1/3.5 and 1/2.3, which are indexed as the second and third orders of the period 7 residue. As in the Drosophila sequence, the rod domain is divided into an amino and a carboxyl subdomain by a predicted hinge region. We show that the disposition of hydrophobic residues is distinct in these two subdomains. In particular, the heptad repeat is more regular in the amino-terminal rod domain than in the carboxyl-terminal rod domain. The tail region is positively charged, a feature that is consistent with the known electrostatic interaction between the heavy chain and negatively charged surfaces such as glass coverslips and latex beads. Three monoclonal antibodies to the kinesin heavy chain have been mapped to a region within the carboxyl terminus of the stalk.

Adenosine Triphosphatases↗
PubMed1990

Risk assessment of drinking water in a reservoir contaminated by PAH's originated from road traffic.

The loads of Polycyclic Aromatic Hydrocarbons (PAHs) originating from road traffic were measured and in units of per vehicle per meter was estimated as follows: 0.07 ng/veh.m for Benzo[a]pyrene, and 0.83 ng/veh.m for Dibenzanthracene and so on, and 5.77 ng/veh.m for total PAHs. This unit is applied to risk estimation of drinking water in a reservoir where it is planned to construct a new high way the near future, and the concentration in the reservoir water is estimated to be 3.3-101 ng/l for individual PAH's. Assuming standard oral exposure to PAHs in raw water for drinking water supply, the estimated lifetime risk of carcinogenesis was less than 1 in 10(6), which is not considered significant.

Benz(a)Anthracenes↗
PubMed1989

Immunogenetic heterogeneity in type 1 (insulin-dependent) diabetes among Japanese HLA antigens and organ-specific autoantibodies.

HLA phenotypes and haplotypes in relation to organ-specific autoantibody responses were studied in 82 Japanese patients with Type 1 (insulin-dependent) diabetes. HLA-DRw9 antigen and HLA phenotype of DRw9/X (X:not DR4) were increased in patients with organ-specific autoantibodies other than islet cell antibody (CP less than 0.02, RR = 4.02 and p less than 0.05 RR = 2.30, respectively); whereas HLA-DR4 antigen and HLA phenotype of DR4/X (X: not DRw9) were increased in those without the autoantibodies (CP less than 0.001, RR = 3.95 and p less than 0.01, RR = 2.46, respectively). HLA haplotype of Bw61-DRw9 was increased in patients with the autoantibodies (p less than 0.005, RR = 4.94), and HLA haplotype of Bw54-DR4 was increased in those without the autoantibodies (p less than 0.001, RR = 5.52). The relative risk of HLA-DR4/DRw9 was the highest among all HLA-DR phenotypes or genotypes in patients either with or without the autoantibodies. No association was, however, found between the incidence of islet cell antibody and HLA-DR phenotypes. These findings suggest that Type 1 diabetes among Japanese is immunogenetically heterogeneous as is Type 1 diabetes among Caucasians; and the differences in HLA-association of Type 1 diabetes among ethnic groups might give a clue to understanding of a role of HLA-antigens in the development of Type 1 diabetes.

Autoantibodies↗