[A case of lymphangioma of the pancreas].
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Cholangiopancreatography, Endoscopic Retrograde↗
Biomedical subjects
S Kunita
Publications and source records attributed to S Kunita.
Establishment of a new murine-phenotypic angiosarcoma cell line (ISOS-1).
A cell line, designated ISOS-1, was established from a tumor formed by transplantation of a human angiosarcoma into mice with severe combined immunodeficiency (SCID). The cells showed endothelial properties, based on the uptake of Dil-Ac-LDL and binding of UEA-I/GSA-I lectins, but were negative for CD11b and Pan Cytokeratin. However, the cells lost differentiated characteristics such as expression of von Willebrand factor, contact inhibition growth and tube formation activity. These findings indicate that ISOS-1 is a poorly-differentiated endothelial cell line. At the 81st passage, all of the cells were positive for H-2Dd in various intensity, but not HLA-ABC. The metaphase chromosomes consistently showed a characteristic mouse, but not human, telocentric form. Furthermore, this cell line produced fatal tumor growth in SCID mice and also in BALB/c mice. These results suggest that ISOS-1 is a murine-phenotypic angiosarcoma cell line.
Animals↗
Characterization of the S protein of enterotropic murine coronavirus strain-Y.
The pathogenesis of enterotropic murine coronavirus strain MHV-Y differs extensively from that of prototypic respiratory strains of murine coronaviruses. The S protein of MHV-Y was characterized as a first step towards identifying viral determinants of enterotropism. Immunoblots of MHV-Y virions using anti-S protein specific antiserum revealed that the MHV-Y S protein was inefficiently cleaved. The MHV-Y S gene was cloned and sequenced. It encodes a protein predicted to be 1361 amino acids long. The presence of several amino acids changes within and surrounding the predicted cleavage site of the MHV-Y S protein may contribute to its inefficient cleavage.
Amino Acid Sequence↗
Molecular characterization of the S proteins of two enterotropic murine coronavirus strains.
Enterotropic strains of murine coronaviruses (MHV-Y and MHV-RI) differ extensively in their pathogenesis from the prototypic respiratory strains of murine coronaviruses. In an effort to determine which viral proteins might be determinants of enterotropism, immunoblots of MHV-Y and MHV-RI virions using anti-S, -N and -M protein-specific antisera were performed. The uncleaved MHV-Y and MHV-RI S proteins migrated slightly faster than the MHV-A59 S protein. The MHV-Y S protein was inefficiently cleaved. The MHV-Y, MHV-RI and MHV-A59 N and M proteins showed only minor differences in their migration. The S genes of MHV-Y and MHV-RI were cloned, sequenced and found to encode 1361 and 1376 amino acid long proteins, respectively. The presence of several amino acids changes upstream from the predicted cleavage site of the MHV-Y S protein may contribute its inefficient cleavage. A high degree of homology was found between the MHV-RI and MHV-4 S proteins, whereas the homology between the MHV-Y S protein and the S proteins of other MHV strains was much lower. These results indicate that the enterotropism of MHV-RI and MHV-Y may be determined by different amino acid changes in the S protein and/or by changes in other viral proteins.
Amino Acid Sequence↗
Genotyping of mouse hepatitis virus strains by restriction endonuclease analysis of amplified nucleocapsid protein genes.
Restriction endonuclease analysis of amplified nucleocapsid protein genes from mouse hepatitis virus (MHV) was used to differentiate 12 strains isolated from mouse liver or transplantable tumors from five facilities, and the restriction patterns of the isolates were compared with those of five well-defined MHV strains, A59, JHM, 2, S and Nu-67. The patterns of 10 isolates from three facilities were the same as that of Nu-67. The remaining two isolates revealed different patterns from the five reference strains. This study showed that reverse transcription and the polymerase chain reaction assay based restriction analysis are feasible for the detection and genotyping of MHV, and the Nu-67 related strain was the most prevalent type found in the clinical samples.
Animals↗
Comparison of polymerase chain reaction and culture methods for detection of Mycoplasma pulmonis from nasal, tracheal and oral swab samples of rats.
The polymerase chain reaction (PCR) and culture methods were used to detect Mycoplasma pulmonis in nasal, tracheal and oral swab samples of rats derived from 5 mycoplasma-contaminated and 2 mycoplasma-free facilities, and the results of both methods were compared. Thirty-four/54 and 30/54 in nasal samples, 31/54 and 28/54 in tracheal samples, and 12/39 and 30/39 in oral samples were positive in PCR and cultures, respectively. Agreements in the results of both tests were 48/54 (88.9%) in nasal samples and 49/54 (90.7%) in tracheal samples. This indicates that nasal and tracheal samples are useful for detecting M. pulmonis by PCR. The detection number for M. pulmonis from the oral cavity by PCR was remarkably lower than those of nasal and tracheal sites. These results show that the PCR method has significant potential as a rapid and sensitive method for detecting M. pulmonis in clinical samples collected from the nasal cavity and trachea.
Animals↗
Sequence analysis of the nucleocapsid protein gene of rat coronavirus SDAV-681.
The nucleotide sequence of the 3'-end of the genomic RNA of sialodacryoadenitis virus strain 681 (SDAV-681) was determined. A large open reading frame encoding a 454-amino-acid protein was identified as the nucleocapsid protein (N) gene, since the predicted protein is similar in size, chemical properties, and amino acid sequence to the N proteins of other coronaviruses. The amino acid variance of the N proteins between SDAV and mouse hepatitis virus (MHV) is not markedly different from that among MHV strains. A high degree of genetic relatedness between SDAV and MHV was revealed in the intergenic and 3'-noncoding sequences as well as in the N gene.
Amino Acid Sequence↗
Sequence analysis and molecular detection of mouse hepatitis virus using the polymerase chain reaction.
Sequence analysis of the nucleocapsid protein genes of five strains of mouse hepatitis virus (MHV) disclosed that the 3' region of the nucleocapsid protein gene contains highly conserved sequences unique to MHV. We designed a pair of primers to amplify cDNA from such sequences of MHV by using the polymerase chain reaction (PCR). Six isolates of wild-type MHV, as well as prototype viruses, were amplified successfully and detected in ethidium bromide-stained agarose gels. The sequence identity of PCR products was readily verified by confirming target size and a MflI site within the target. The sensitivity of our PCR assay was estimated to be sufficient to detect a single cell infected with MHV. This new approach may permit more sensitive and rapid detection of MHV in biologic materials than current methods such as virus isolation, the infant mouse bioassay, and the mouse antibody production test.
Base Sequence↗
A serological survey on Bacillus piliformis infection in laboratory rabbits in Japan.
A total of 544 rabbit sera obtained from 6 commercial breeding facilities and 9 research institutions during 1985-1990 were tested for Bacillus piliformis antibody by an enzyme-linked immunosorbent assay (ELISA) and indirect immunofluorescent antibody test (IFAT). The antibody was detected in 53 (14.2%) rabbits from 3 breeding facilities and 30 (17.4%) rabbits from 6 research institutions, indicating the prevalence of B. piliformis infection among laboratory rabbits in Japan. The overall agreement with ELISA for immune status was 96.9% (527/544) with IFAT. In tests of the ability of ELISA and IFAT to quantitate antibody, a correlation coefficient (r) of 0.86 (P less than 0.01) was obtained by plotting the measured average log of the ELISA titer against the corresponding log of the IFAT titer.
Animals↗
A monoclonal antibody specific for bovine T cell surface antigen associated with the E-rosette receptor.
From mice immunized with T lymphocyte-enriched bovine peripheral blood mononuclear cells (PBMC), a monoclonal antibody termed BLMo-12 was obtained. BLMo-12 reacted with the antigen of Mr 56,000 in lysate of T lymphocytes. This mAb was found to inhibit spontaneous rosette formation by T-bovine lymphocytes with sheep red blood cells but it did not react with B lymphocytes, monocytes, neutrophils or eosinophils. In frozen section of the thymus, BLMo-12 showed a positive staining both the cortex and the medulla. In lymph nodes, the mAb stained the T-dependent paracortex. BLMo-12 reacted with 49.9% of PBMC and 82.5% of thymocytes. Recognition of the bovine homologue of CD2 on the T lymphocyte surface by this mAb was discussed.
Animals↗
Sensitive detection of Mycoplasma pulmonis by using the polymerase chain reaction.
Detection of Mycoplasma pulmonis was examined by using the polymerase chain reaction (PCR) for amplifying a specific DNA sequence. In gel electrophoresis which was conducted to detect the amplified products, only 1 pg of M. pulmonis DNA could be detected following 30 cycles of amplification, while no amplified product was detected even from 1 microgram of M. arthritidis or M. neurolyticum DNA. Furthermore, 10 colony-forming units of M. pulmonis could be detected by direct amplification from the mycoplasma suspension. These results suggest the usefulness of the PCR as a highly sensitive, specific, and rapid method for direct detection of M. pulmonis.
Base Sequence↗
Genomic DNA analysis of rodent mycoplasmas.
Genomic DNA was compared between three typical species of rodent mycoplasmas, Mycoplasma pulmonis, M. arthritidis and M. neurolyticum, and between strains of these species. Each of the three species showed a distinct restriction endonuclease cleavage pattern of genomic DNA. The genetic heterogeneity of these species was revealed by total DNA hybridization as well. In addition, the restriction endonuclease cleavage pattern of genomic DNA was almost identical in three strains of M. pulmonis and in two strains of M. neurolyticum. The genetic hemogeneity among strains of the same species was revealed by total DNA hybridization as well. These data suggest that the genomic DNA sequence of each rodent mycoplasma species has a high degree of species specificity.
Animals↗
Expression of Mycoplasma pulmonis antigens in Escherichia coli.
The expression of Mycoplasma pulmonis antigen in Escherichia coli was investigated by cloning genomic DNA derived from M. pulmonis m 53, and the DNA fragment participating in antigen expression was identified. When the DNA library of M. pulmonis was screened by colony immunoassay using anti-M. pulmonis serum, 10 recombinant clones expressing seroreactive antigens were obtained. The recombinant plasmids isolated from these clones included 3.7-6.5 kilobase pair (kbp) DNA inserts, while all clones contained a common 2.3-kbp DNA fragment. Subcloning of initial DNA inserts showed that the common 2.3-kbp fragment is essential for antigen expression. Moreover, antiserum against the recombinant antigen generated from the 2.3-kbp DNA fragment recognized a native M. pulmonis antigen. The reactivity of this antiserum was absorbed specifically with M. pulmonis. These results suggest that the cloned 2.3-kbp DNA fragment codes an antigen specific to M. pulmonis.
Antigens, Bacterial↗
A DNA probe for specific detection of Mycoplasma pulmonis.
Mycoplasma pulmonis was specifically detected by using a 2.3 kilobase pair (kbp) cloned DNA fragment derived from M. pulmonis m 53 as a probe. This probe recognized 2.3-kbp DNA fragments of three M. pulmonis strains in Southern hybridization, while it did not hybridize with the DNA of M. arthritidis or M. neurolyticum. Determination of the sensitivity of the probe by dot hybridization revealed that 10 ng of M. pulmonis DNA was detected by a biotinylated probe and 1 ng of M. pulmonis DNA was detected by a radioactive probe.
DNA Probes↗
Cross reactivity of Mycoplasma pulmonis and Mycoplasma arthritidis antigen strains to anti-Mycoplasma pulmonis antibody in the sera of Mycoplasma pulmonis infected rats.
Reactivity of Mycoplasma pulmonis (Mp) antigen strains to anti-Mp antibody in the sera of Mp infected rats was examined by enzyme linked immunosorbent assay (ELISA). Antibody titers to 7 kinds of Mp antigens were measured in the sera of 20 Mp isolated rats and 20 Mp free rats by ELISA and complement fixation test (CF test). ELISA showed that there was no difference in the antibody titer of the same serum among 7 Mp antigen strains employed, and the main cross reaction to anti-Mp antibody took place on the common recognition site (common antigen) in all the Mp antigens. The CF test suggested that the antibody titers largely differed due to the kind of Mp antigen strains, and the detection rate was between 0 and 60%, presumably due to the difference in the reactivity or binding ability of complements but not due to the difference in the cross reactivity of Mp antigen to anti-Mp antibody. When the cross reactivity of anti-Mp antibody to Mycoplasma arthritidis (Ma) antigen was examined in the sera of 33 Mp isolated rats, the CF test exhibited the negative results, but ELISA showed 4 positive cases to support the cross reactivity of anti-Mp antibody to Ma antigen.
Animals↗
Preparation and characterization of monoclonal antibodies against bovine B lymphocyte surface antigens.
Two monoclonal antibodies (MoAbs; BLMo-4 and BLMo-10) were prepared by immunizing with a cell line established from peripheral blood mononuclear cells (PBMC) of enzootic bovine leukosis (EBL) cattle. The specificities of these MoAbs were assayed using bovine PBMC. BLMo-4 reacted with all surface immunoglobulin-positive cells (SIg+ cells; B lymphocytes) and also recognized monocytes, but did not react with T lymphocytes. BLMo-10 recognized a majority, although not all, B lymphocytes, but did not react with either T lymphocytes or monocytes. The antigens recognized by BLMo-4 and BLMo-10 were not Ig, Fc or C3 receptors on the surface of B lymphocytes. The reactivity of the MoAbs with mononuclear cells from the lymphoid organs of adult cattle was studied. BLMo-4 and BLMo-10 did not react with any bone marrow cells. BLMo-10 reacted with 7.4% of thymocytes, and stained the medulla of the thymus in the immunoperoxidase assay. In the case of PBMC, spleen and lymph node cells, the percentage of cells positive for BLMo-4 was slightly higher than that of SIg+ cells, but BLMo-10 showed a slightly lower value.
Animals↗
Preparation of monoclonal antibodies reacting with bovine cortical thymocytes.
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Animals↗
[A new simplified colorimetric assay of colipase in duodenal juice using BALB as substrate and its clinical application].
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Colipases↗