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M Takiguchi

Publications and source records attributed to M Takiguchi.

At least 217 records · Page 12Linked to original sources
PubMed1992

Molecular analysis of the association of HLA-B53 and resistance to severe malaria.

The protective association between the human leukocyte antigen HLA-B53 and severe malaria was investigated by sequencing of peptides eluted from this molecule followed by screening of candidate epitopes from pre-erythrocytic-stage antigens of Plasmodium falciparum in biochemical and cellular assays. Among malaria-immune Africans, HLA-B53-restricted cytotoxic T lymphocytes recognized a conserved nonamer peptide from liver-stage-specific antigen-1 (LSA-1), but no HLA-B53-restricted epitopes were identified in other antigens. These findings indicate a possible molecular basis for this HLA-disease association and support the candidacy of liver-stage-specific antigen-1 as a malaria vaccine component.

Amino Acid Sequence↗
PubMed1992

Trehalase from male accessory gland of an insect, Tenebrio molitor. cDNA sequencing and developmental profile of the gene expression.

A cDNA of alpha alpha-trehalase (EC 3.2.1.28) from a cDNA library of male bean-shaped accessory gland of the mealworm beetle, Tenebrio molitor, has been isolated by the homology screening approach. Sequence analysis of the cDNA (1830 bp) revealed that the cDNA encoded a protein of 555 amino acids with a calculated M(r) of 64457. The deduced amino acid sequence had significant similarities to rabbit small intestine and Escherichia coli trehalases. Northern blotting and semi-quantitative PCR analyses revealed that a trehalase transcript with about 2.0 kb was abundant in bean-shaped accessory glands. In the glands, the amount of trehalase transcript increased from 1 to 2 days after adult ecdysis. These tissue- and stage-specific gene expressions of trehalase corresponded to the tissue- and stage-specificity of trehalase activity.

Amino Acid Sequence↗
PubMed1992

Beta-chain broadens range of CD8 recognition for MHC class I molecule.

It is known that the alpha-chain of CD8 binds to a negatively charged loop composed of residues 223 to 229 on MHC class I Ag and that binding of CD8 alpha enhances Ag recognition of T cells. We have recently shown that the mouse CD8 alpha homodimer does not bind to either the HLA class I alpha 3 domain or a mutant of H-2Kb Ag containing a substitution of glutamine for methionine at residue 224, which brings this residue toward the human consensus. Here we report a complementary study of the CD8 beta-chain. The functional role of the CD8 beta-chain was analyzed by using four T cell hybridoma lines expressing mouse CD8 alpha and transfected with the mouse CD8 beta gene. As compared with the lines expressing only CD8 alpha, allorecognition of the chimeric H-2Kb Ag that contains the HLA class I alpha 3 domain was enhanced in lines expressing both CD8 alpha and -beta. This enhancement was blocked by either anti-CD8 mAb or anti-HLA class I alpha 3 domain mAb. In addition, we show that CD8 alpha beta binds the H-2Kb mutant Ag at residue 224. These results suggest that the beta-chain allows the CD8 alpha beta heterodimer to recognize the chimeric H-2Kb Ag. A model for the role of the beta-chain is presented.

Animals↗
PubMed1992

Structural and functional analysis of monomorphic determinants recognized by monoclonal antibodies reacting with the HLA class I alpha 3 domain.

To identify mAb reacting with the HLA class I alpha 3 domain, 14 mAb recognizing monomorphic determinants expressed on HLA-A, B, and C Ag or restricted to HLA-B Ag were screened in indirect immunofluorescence with mouse L cells expressing HLA-B7/H-2Kb chimeric Ag. mAb CR1S63, CR10-215, CR11-115, and W6/32 were found to react with the HLA class I alpha 3 domain in addition to the alpha 2 domain. mAb Q1/28 and TP25.99 were found to react only with the HLA class I alpha 3 domain. The determinants recognized by the six mAb were mapped on the HLA class I alpha 3 domain by indirect immunofluorescence staining of L cells expressing H-2Kb Ag containing different segments of the HLA-B7 alpha 3 domain chimerized with the H-2Kb alpha 3 domain. mAb TP25.99 reacts with chimeric Ag containing the HLA-B7 184 to 199 stretch, mAb CR10-215 and CR11-115 react with chimeric Ag containing the HLA-B7 184 to 246 stretch, mAb CR1S63 and Q1/28 react with chimeric Ag containing the HLA-B7 184 to 256 stretch, and mAb W6/32 reacts with chimeric Ag containing the whole HLA-B7 alpha 3 domain. Functional analysis using human CD8 alpha-bearing mouse H-2Kb-specific T cell hybridoma cells (HTB-Leu2) showed that only mAb TP25.99 inhibited IL-2 production by HTB-Leu2 cells stimulated with L cells expressing KbKbB7 Ag. This inhibition may occur because of the spatial proximity of the determinant defined by mAb TP25.99 to the CD8 alpha binding loop and/or because of change(s) in the conformation of the CD8 alpha binding loop induced by the binding of mAb TP25.99 to the HLA class I molecule. Furthermore, mAb TP25.99 inhibited the cytotoxicity of CD8-dependent and CD8-independent CTL clones. These results indicate that mAb TP25.99 has unique specificity and functional characteristics. Therefore it represents a valuable probe to characterize the role of the HLA class I alpha 3 domain in immunologic phenomena.

Amino Acid Sequence↗
PubMed1992

Conservation of genes encoding HLA-B5 and B35 cross-reactive group antigens in various races.

HLA-B5 and B35 CREG antigens include HLA-B35, B51, B52, B53, and B78. Recent studies suggest that the genes encoding the HLA-B5, B35 CREG, and HLA-B58 antigens share a common ancestor. We sequenced the exons of the genes encoding HLA-B51, B53, and B58 from American black individuals and the gene HLA-B52 encoding from an Arabic individual, and compared them with previously reported sequences of HLA-B51 (B*5101) and HLA-B52 (B*5201) from Japanese, HLA-B53 (B*5301) from an Algerian, and HLA-B58 (B*5801) from a Sardinian. The sequences of the genes from the American black and Arabic individuals were identical to those from the other races. These findings support the hypothesis that these antigens have evolved prior to divergence of the major ethnic groups.

Base Sequence↗
PubMed1992

Effect of the substitutions in the alpha helix and the beta sheet of HLA class I molecule on allorecognition of T cells specific for HLA-B51 and HLA-Bw53.

HLA-B51 and HLA-Bw53 differ by eight amino acids on the alpha 2 domain. Of these eight amino acid substitutions, two are in the alpha helix and six are in the beta sheet. The effect of these substitutions on allorecognition of HLA-B51-specific cytotoxic T lymphocyte (CTL) clones and HLA-Bw53-specific CTL clones was investigated using chimeric antigen (Ag) between HLA-B51 and HLA-Bw53. Of 12 HLA-B51-specific CTL clones, recognition of one clone was abolished by the substitutions on the beta sheet alone, that of two clones by the substitutions on the alpha helix alone, and that of nine clones not only by the substitutions on the alpha helix but also by those on the beta sheets. On the other hand, of 17 HLA-Bw53-specific CTL clones, recognition of 10 clones was affected by the substitutions on the alpha helix alone and that of 7 clones not only by the substitutions on the alpha helix but also by those on the beta sheet. The present study demonstrated that the substitutions (residues 152 and 171) on the alpha helix critically affect recognition of HLA-B51-specific CTL clones and HLA-Bw53-specific CTL clones and that the substitutions on the beta sheet affect also recognition of the majority of HLA-B51-specific CTL clones and 40% of HLA-Bw53-specific CTL clones. These results indicate that the substitutions at the floor of the peptide binding groove affect recognition of allogeneic CTL.

Amino Acid Sequence↗
PubMed1992

Antigen recognition by the T cell receptor is enhanced by CD8 alpha-chain binding to the alpha 3 domain of MHC class I molecules, not by signaling via the cytoplasmic domain of CD8 alpha.

The binding specificities and function of mouse CD8 were studied using a CD4-CD8- allospecific T cell hybridoma, chimeric class I MHC molecules, and a CD8 alpha deletion mutant. By transfecting the mouse CD8 alpha gene into a IL-2 producing, H-2Kb specific hybridoma, IL-2 production was increased when L cells expressing Kb were used as stimulators. However, no increase in IL-2 was observed when a KbKbB7 hybrid molecule, composed of the alpha 1 and alpha 2 domains of H-2Kb, and the alpha 3 domain of HLA-B7, was used as a stimulator. Comparison between T cell hybridomas that expressed full-length CD8 alpha and a deletion mutant lacking part of the cytoplasmic domain revealed identical responsiveness for H-2Kb. The data suggest that the mouse CD8 alpha homodimer does not bind to the alpha 3 domain of HLA class I molecules and that CD8 alpha acts as a co-receptor with the TCR by binding the same MHC molecule for alloantigen recognition. Our data also provide evidence that CD8 alpha signal transduction through its cytoplasmic tail by association with p56lck is not an absolute requirement for antigen recognition by T cells.

Animals↗
PubMed1992

Isolation of human minor histocompatibility peptides.

Incompatibility of human minor histocompatibility (hmH) antigens induces rejection of grafts in organ transplantation and graft versus host disease in bone marrow transplantation if donor and recipient are matched for human leukocyte antigen (HLA) genes. These antigens are recognized only by T cells. We describe here the isolation of hmH peptides recognized by a hmH antigen specific, HLA-B35 restricted CTL clone which was derived from a patient who rejected the kidneys from two HLA-identical sisters. Naturally occurring hmH peptides were isolated from a donor derived B cell line and an HLA-B35 transfected human B cell line by acid elution. Analysis of various HLA class I transfectant cells demonstrated that MHC class I molecules themselves determine the peptides which are naturally processed and presented to T cells.

B-Lymphocytes↗
PubMed1991

Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia.

Carbamyl phosphate synthetase I (CPSI) is the first enzyme involved in urea synthesis. CPSI deficiency is an autosomal recessive disorder characterized by hyperammonemic coma in the neonatal period. To analyze the enzyme and gene structures, and to elucidate the nature of mutations in CPSI deficiency, we isolated cDNA clones encoding human liver CPSI. Oligo(dT)-primed and random primer human liver cDNA libraries in lambda gt11 were screened using 5', middle, and 3' fragments of the rat CPSI cDNA as probes. Seven positive clones covered the full-length cDNA sequence with an open reading frame encoding a precursor polypeptide of 1500 amino acids (aa) (deduced Mr, 164,828) with a putative N-terminal presequence of 38 or 39 aa, a 5'-untranslated sequence of 118 bp and a 3'-untranslated sequence of 597 bp. Comparison with the rat CPSI cDNA showed that the deduced aa sequence of the human liver CPSI precursor is 94.4% identical to the rat enzyme precursor. A molecular analysis was made of the genomic DNA from three patients with CPSI deficiency. Heterogeneity of hybridized fragments that may or may not be the cause of the deficiency was apparent on the DNA blots from tissues from one patient.

Amino Acid Metabolism, Inborn Errors↗
PubMed1991

Induction of inflammatory arthropathy resembling rheumatoid arthritis in mice transgenic for HTLV-I.

Human T cell leukemia virus type-I (HTLV-I) is the etiologic agent of adult T cell leukemia and has also been suggested to be involved in other diseases such as chronic arthritis or myelopathy. To elucidate pathological roles of the virus in disease, transgenic mice were produced that carry the HTLV-I genome. At 2 to 3 months of age, many of the mice developed chronic arthritis resembling rheumatoid arthritis. Synovial and periarticular inflammation with articular erosion caused by invasion of granulation tissues were marked. These observations suggest a possibility that HTLV-I is one of the etiologic agents of chronic arthritis in humans.

Animals↗
PubMed1991

In vitro analysis of the rat liver-type arginase promoter.

Genes for urea cycle enzymes including liver-type arginase are expressed mainly in the liver and are regulated developmentally, nutritionally, and hormonally in a coordinated manner. The promoter region of the rat arginase gene was investigated with an in vitro transcription system using nuclear extracts prepared from rat tissues. Accurate initiation of the transcription in liver nuclear extracts was confirmed by runoff analysis and S1 nuclease mapping. The arginase promoter was transcribed more efficiently in liver nuclear extracts than in brain extracts, reproducing the in vivo tissue specificity qualitatively. Analysis of deletion mutants of the 5'-flanking region in liver nuclear extracts revealed a positive regulatory region spanning nucleotides -90 to -51 relative to the transcription start site. Overlapping this region, two protected areas were detected by DNase I footprinting. Competition analysis with synthetic oligonucleotides showed that the more downstream protected area was occupied, in a mutually exclusive manner, by two factors each related to CTF/NF-1 and Sp1. The other more upstream protected area was recognized by a factor related to the liver-enriched transcription factor C/EBP, which was recently shown to interact with regulatory regions of two other urea cycle enzyme genes.

Animals↗
PubMed1991

Correction of ornithine transcarbamylase (OTC) deficiency in spf-ash mice by introduction of rat OTC gene.

We introduced rat ornithine transcarbamylase (OTC) gene into OTC-deficient spf-ash mice by mating spf-ash heterozygotes with transgenic mice which carried recombinant DNA composed of 1.3 kb of the 5' flanking region of the gene fused onto rat OTC cDNA. The liver OTC activity of hemizygous spf-ash mice which carried the transgene was about twice that of nontransgenic spf-ash mice, and the small intestinal OTC activity was 6 times higher; the values being 12% and 27% of the control levels, respectively. The transgenic spf-ash mice showed normal hair growth without sparse fur, nearly normalized urinary orotic acid excretion and normalized serum citrulline concentration.

Animals↗
PubMed1991

Changes of plasma thromboxane level in subarachnoid haemorrhage. A study with 11-dehydro-TXB2 as measuring index.

Changes of plasma thromboxane level in subarachnoid haemorrhage (SAH) were studied clinically and experimentally using 11-dehydro-thromboxane B2 (11 DTX) as a measuring index. 11 DTX is a major long-lived metabolite formed from thromboxane (TX) B2, and is said to be a more reliable parameter for detecting TXA2 production in biological systems. In this clinical study, blood was sampled from the cubital vein of 10 SAH patients on the earliest possible day (day 0 or 1), during the vasospasm predilection period (day 7 approximately 11) and in the chronic stage (day 16 approximately 32). Plasma concentrations of 11 DTX and 6-keto-PGF 1 alpha were measured in clinical cases. A canine SAH model was produced by the two haemorrhage methods and blood was sampled from the superior sagittal sinus before and on day 4 of the first cisternal blood injection. 11 DTX, TXB2 and platelet function were examined in each sample. In the clinical studies, plasma 11 DTX levels tended to be higher in the early stage of SAH but decreased thereafter to the normal or lower level. Plasma concentrations of 6-keto-PGF1 alpha tended to decrease mildly during the vasospasm predilection period. In the experimental study, neither definite change of plasma 11 DTX level nor neurological deficit could be induced by the mimic SAH, while an increase in platelet aggregability and narrowing of the basilar artery were observed. 11 DTX was inferred to be a more reliable parameter of TX biosynthesis than TXB2.

Adult↗
PubMed1991

T cell can recognize the allospecificities formed by the substitution of amino acids associated with HLA-Bw4/Bw6 public epitopes.

Our previous studies clearly showed that HLA-B35 and HLA-Bw53 differed only by the amino acids associated with HLA-Bw4/Bw6 epitopes, in that the former possessed Bw6 and the latter Bw4 epitope. It remains to be known whether T cell can discriminate HLA-B35 from HLA-Bw53, although the difference between these HLA antigens is discriminated by monospecific human alloantisera. To investigate allorecognition of these HLA antigens by T cells, anti-HLA-Bw53 cytotoxic T lymphocytes (CTLs) were generated. Anti-HLA-Bw53 cytotoxic T lymphocytes (CTLs) were generated. Anti-HLA-Bw53 bulk CTLs from an individual with HLA-B35 clearly discriminated HLA-Bw53 from HLA-B35. On the other hand, anti-HLA-Bw53 bulk CTLs from an individual without HLA-B35 revealed weak cross-reactivity with HLA-B35 and HLA-B51. The additional studies using HLA-Bw53 or HLA-B35-specific CTL clones showed that some but not all of the CTL clones definitively distinguish the difference between HLA-Bw53 and HLA-B35. Thus, the allospecificities formed by HLA-Bw4/Bw6 epitopes were discriminated by allogeneic T cells. The present study demonstrated that HLA-Bw4/Bw6 public epitopes play an important role in allorecognition of T cells.

Amino Acid Sequence↗
PubMed1991

Progressive deterioration of auditory evoked potentials after excision of an acoustic neurinoma: case report.

The authors report the case of a 17-year-old girl who underwent excision of bilateral neurinomas of the cerebellopontine angle. Although her auditory evoked potentials were well maintained during the operation, they deteriorated gradually and progressively for the following 2 months. This seemed to reflect degeneration of the cochlear nerve fibers initiated by operative manipulation in the cerebellopontine angle in a patient who had no hearing when she awoke from surgery.

Adolescent↗
PubMed1991

Serum C-reactive protein (CRP) in horses: the effect of aging, sex, delivery and inflammations on its concentration.

The serum concentration of C-reactive protein (CRP) in horses was measured by single radial immunodiffusion (SRID) using rabbit anti-equine CRP serum to evaluate the significance of CRP as an acute-phase reactive protein. In serum samples of clinically normal newborn thoroughbred foals before being given colostrum, serum CRP was not detectable (less than or equal to 1 microgram/ml). The serum CRP concentration was found to increase quickly and reach a peak level of approximately 14.1 micrograms/ml in 12-month-old horses. Then, it decreased gradually to reach a low value of 5.4 micrograms/ml in the 4-year-old. In horses over 5-year-old, serum CRP concentration was stable at values of 7 to 8 micrograms/ml. In mares during the peri-natal period, serum CRP concentration decreased at 2 months before delivery, showed moderate changes just before and after delivery, and then increased to relatively high level by 2 months after delivery. The concentration of serum CRP was found to be increased at 24 hours after experimentally inflammatory stimuli in adult horses, and reached peak values of 3 to 6 times as high as the base line values at 3 to 5 days. Serum CRP concentration returned to base line values by 2 to 3 weeks after treatments. It is clear from these data that CRP is one of the acute-phase reactive proteins in horses.

Aging↗