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PubMedDate not supplied

Cytogenetic effects of the insecticide methamidophos in mouse bone marrow and cultured mouse spleen cells.

The cytogenetic effect of the insecticide methamidophos (0,S-dimethylphosphoroamidothiolate) was studied in mouse bone marrow and mouse spleen cells in culture. In vivo the ability of methamidophos to induce micronuclei and sisterchromatid exchange in mouse bone marrow was investigated. In vitro mouse spleen cells in culture were used to assess the ability of the insecticide to induce chromosomal aberrations and sister chromatid exchange. Three different routes of application for the pure insecticide were tested so as to cover the different possibilities for human exposure to the insecticide. Intraperitoneal, oral and dermal treatment with methamidophos caused toxicity to marrow as indicated by a significant increase in the percentage of polychromatic erythrocytes (PEs) over that of the control. Methamidophos showed mutagenic potential as evidenced by a positive response in the micronucleus and chromosomal aberrations assays. Thus, single and multiple i.p. injections at 6 and 4.5 mg methamidophos/kg body wt., oral administration of the insecticide for 14 consecutive days at a dietary level of 100 ppm and multiple dermal treatments (total 4) with 24 mg/kg body wt. induced a statistically significant increase in the frequency of PEs with micronuclei in mouse bone marrow. Moreover, the tested concentrations of methamidophos as low as 0.25 microgram/ml induced a high percentage of metaphases with chromosomal aberrations in cultured mouse spleen cells. Methamidophos is a weak inducer of SCEs in mouse bone marrow and cultured mouse spleen cells.

Animals↗
PubMed2002

Molecular cloning and expression of mouse Wnt14, and structural comparison between mouse Wnt14-Wnt3a gene cluster and human WNT14-WNT3A gene cluster.

Glycoprotein WNTs play key roles in carcinogenesis and embryogenesis. Human WNT14 and WNT3A genes are clustered in human chromosome 1q42 region with an interval of about 58 kb. Here, mouse Wnt14 was isolated to compare the structure of human WNT14-WNT3A gene cluster with that of mouse Wnt14-Wnt3a gene cluster. Mouse Wnt14 showed 98.1% total-amino-acid identity with human WNT14, and 61.9% total-amino-acid identity with human WNT14B/WNT15. Mouse Wnt14 mRNA was expressed in adult brain, lung, skeletal muscle, heart, and 17-day embryo. Mouse Wnt14 and Wnt3a genes were clustered in head-to-head manner with an interval of about 16 kb. Exon-intron structures were well conserved between human WNT14-WNT3A gene cluster and mouse Wnt14-Wnt3a gene cluster. Capicua-related sequence and AK024248-related sequence were identified in the intergenic region of human Wnt14-Wnt3a gene cluster as well as in other human chromosomal loci, but not in that of mouse Wnt14-Wnt3a gene cluster. Capicua-related sequences were pseudogenes derived from Capicua gene on human chromosome 19q13. Capicua pseudogene and AK024248-related sequence were clustered in tail-to-tail manner with interval ranging from 2.2 to 11.0 kb. AK024248-related sequences in several human genome draft sequences were truncated in the 3'-portion compared with that in the intergenic region of human WNT14-WNT3A gene cluster. This is the first report on structural comparison of WNT gene clusters in human genome and in mouse genome.

Amino Acid Sequence↗
PubMed1989

Complete structure of the mouse mast cell receptor for IgE (Fc epsilon RI) and surface expression of chimeric receptors (rat-mouse-human) on transfected cells.

The high affinity receptor for IgE (Fc epsilon RI) found on mast cells and basophils is a tetrameric complex of a single alpha subunit, a single beta subunit, and two identical gamma subunits. The genes for the three subunits of mouse Fc epsilon RI have now been cloned from the mast cell line, PT18. When compared at the DNA level, the rat and mouse subunits are similarly conserved. However, at the protein level the homology between mouse and rat alpha is surprisingly low (71% identities) especially in the cytoplasmic regions (57% identities) which are of different length (25 and 20 residues, respectively). By contrast the beta and gamma are homogeneously conserved between mouse and rat (83 and 93% identities, respectively). The consensus amino acid sequence of the alpha subunit derived from three species (rat, mouse, and human) shows that the cytoplasmic tail diverges to the same extent as the leader peptide. Conversely, the transmembrane domain of the alpha is highly conserved and contains 10 consecutive residues that are identical. Comparisons between mouse Fc epsilon RI and other mouse proteins reveal regions of high homology between the alpha subunit and Fc gamma RIIa and between the gamma subunit and the zeta chain of the T cell receptor. Cells transfected with the alpha gene express the alpha subunit on their surface very inefficiently. Efficient expression is only achieved after co-transfection of the three rodent genes or of the human alpha gene together with the rodent gamma without apparent need for beta. The subunits are completely interchangeable upon transfection so that various chimeric mouse-rat-human receptors can be expressed.

Amino Acid Sequence↗
PubMed1988

The characterization of four monoclonal antibodies specific for mouse IL-5 and development of mouse and human IL-5 enzyme-linked immunosorbent.

Four rat mAb directed against mouse IL-5 have been characterized by their ability to remove and neutralize mouse IL-5 activity in various bioassays. All four mAb absorbed IL-5 activity from solution. Although all were able to neutralize mouse IL-5 bioactivity, two were significantly more effective. These two were also able to neutralize the activity of mouse IL-5 delivered to B cells during a cognate-linked interaction with a Th cell clone. A two-site sandwich ELISA specific for mouse IL-5 was developed by using pairs of mAb. The mouse IL-5 ELISA is capable of detecting natural or mouse rIL-5 in supernatants, crude bacterial lysates, and high concentrations of mouse serum, and has a detection limit of less than 20 pg. Two of these antibodies cross-reacted with and neutralized human rIL-5, and one of these was used for development of an ELISA for human IL-5.

Animals↗
PubMed1995

Catalytic properties of NAD(P)H:quinone acceptor oxidoreductase: study involving mouse, rat, human, and mouse-rat chimeric enzymes.

NAD(P):quinone acceptor oxidoreductase (quinone reductase) (DT-diaphorase, EC 1.6.99.2) is involved in the process of reductive activation of cytotoxic antitumor quinones and nitrobenzenes. In this study, we initially examined the relative abilities of mouse, rat, and human quinone reductases to reduce two prodrugs, CB 1954 [5-(aziridin-1-yl)-2,4-dinitrobenzamide] and EO9 [5-(1-aziridinyl)-3-(hydroxymethyl)-2-(3-hydroxy-1-propenyl)-1- methyl-1H-indole-4,7-dione]. By using Escherichia coli-expressed quinone reductases and evaluating them under identical conditions, we confirmed previous finding showing that the human enzyme is not as effective as the rat enzyme in reducing CB 1954 and EO9, although the two enzymes have similar NAD(P)H-menadione reductase activities. Interestingly, although the amino acid sequence of mouse quinone reductase is more homologous to that of the rat enzyme, we found that the mouse enzyme behaves similarly to the human enzyme in its ability to reduce these compounds and to generate drug-induced DNA damage. To determine the region of quinone reductase that is responsible for the catalytic differences, two mouse-rat chimeric enzymes were generated. MR-P, a chimeric enzyme that has mouse amino-terminal and rat carboxy-terminal segments of quinone reductase, was shown to have catalytic properties resembling those of rat quinone reductase, and RM-P, a chimeric enzyme that has rat amino-terminal and mouse carboxyl-terminal segments of quinone reductase, was shown to have catalytic properties resembling those of mouse quinone reductase. In addition, MR-P and RM-P were found to be inhibited by flavones with Ki values similar to those for rat and mouse quinone reductases, respectively. Based on these results, we propose that the carboxyl-terminal portion of the enzyme plays an important role in the reduction of cytotoxic drugs and the binding of flavones.

Amino Acid Sequence↗
PubMed1993

A plan for the mouse genome project. Joint NIH/DOE Mouse Working Group.

The National Center for Human Genome Research and the Department of Energy convened a committee of geneticists and biologists who use the laboratory mouse in their research programs. Their responsibility was to identify goals and guidelines for completing the genetic and physical maps of the mouse genome. The motivation for convening this group was to make certain that existing and anticipated research projects together represent a comprehensive program for addressing the Five Year Goals of the Human Genome Project. Three meetings were held: the first addressed the contributions that the mouse can make to the Human Genome Project; the second meeting reviewed the status of the genetic map, gene mapping research, and genome informatics; and the final meeting evaluated the status of the physical map and physical mapping research. The committee then prepared a report that reviewed the status of the mouse genome project and made recommendations concerning areas of research emphasis. The resulting Request For Applications entitled 'Mapping the Mouse Genome with Emphasis on Technology Development' (RFA: HG-92-002) is an important mechanism for coordinating mouse genome research and accomplishing the goals of the mouse genome project. Progress towards complete genetic and physical maps has been impressive. The genetic map should be completed on schedule, and ongoing physical mapping projects are promising. Given rapid progress on these maps, the Working Group proposed expanding the focus of the mouse genome effort to begin planning comprehensive approaches for characterizing the function of the large number of genes that will soon be mapped and eventually sequenced.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1997

Differences in partial agonist action at cholecystokinin receptors of mouse and rat are dependent on parameters extrinsic to receptor structure: molecular cloning, expression and functional characterization of the mouse type A cholecystokinin receptor.

The mouse cholecystokinin (CCK) receptor is functionally distinct from the extensively studied rat receptor on the basis of differences in binding and biological activity of phenethyl ester analogs of CCK. These are partial agonists at the rat receptor and full agonists at the mouse pancreatic receptor. To explore this, we cloned the cDNA for the mouse type A CCK receptor, established a receptor-bearing Chinese hamster ovary (CHO) cell line and characterized its binding and biological characteristics. Despite 25 differences in amino acid sequence from the rat receptor, including a seven-amino acid insertion in the third intracellular loop, mouse and rat receptors were functionally indistinguishable when expressed in CHO cells. Of note, in the mouse pancreatic cell environment, a stable analog of guanosine triphosphate significantly inhibited binding of CCK-OPE, whereas it had no effect on binding to the same receptor on the CHO-CCKM cell line or to the rat receptor in either environment of the acinar cell. This likely reflects a difference in coupling of the mouse receptor to its G protein in the natural environment of the acinar cell. This may relate to differences extrinsic to the receptor, in the stoichiometry or character of G proteins or in the composition or organization of the lipid environment of the mouse acinar cell membrane. Although this may require complementation of the unique sequence of the mouse receptor, that structure alone is insufficient to explain this phenomenon. Receptor microenvironment makes an important, yet often ignored, contribution to receptor function.

Amino Acid Sequence↗
PubMed1995

The chromosomal location of the mouse mammary tumor gene Int6 and related pseudogenes in the mouse genome.

The Int6 gene is a common insertion site for the mouse mammary tumor virus (MMTV) in mouse mammary tumors. We have determined that this gene is located centromeric of the Myc protooncogene on mouse chromosome 15. In the mouse genome there are several other Int6-reactive restriction fragments that are located on mouse chromosomes 6, 11, 14, 17, and 18. Nucleotide sequence analysis of four of six of these additional Int6 fragments showed that they contain processed Int6 pseudogenes. Comparisons between the Int6 genes of the inbred mouse laboratory strains and the wild mouse species Mus spretus and Mus mus musculus indicate that some pseudogenes were present before divergence of these species and others were acquired since their separation.

Animals↗
PubMed2005

The Mouse Genome Database (MGD): from genes to mice--a community resource for mouse biology.

The Mouse Genome Database (MGD) forms the core of the Mouse Genome Informatics (MGI) system (http://www.informatics.jax.org), a model organism database resource for the laboratory mouse. MGD provides essential integration of experimental knowledge for the mouse system with information annotated from both literature and online sources. MGD curates and presents consensus and experimental data representations of genotype (sequence) through phenotype information, including highly detailed reports about genes and gene products. Primary foci of integration are through representations of relationships among genes, sequences and phenotypes. MGD collaborates with other bioinformatics groups to curate a definitive set of information about the laboratory mouse and to build and implement the data and semantic standards that are essential for comparative genome analysis. Recent improvements in MGD discussed here include the enhancement of phenotype resources, the re-development of the International Mouse Strain Resource, IMSR, the update of mammalian orthology datasets and the electronic publication of classic books in mouse genetics.

Animals↗
PubMed1998

Apoptosis in the lens anlage of the heritable lens aplastic mouse (lap mouse).

Adult homozygous lap mice show various eye abnormalities, such as aphakia, retinal disorganization, and dysplasia of the cornea and anterior chamber. In the fetal eye of a homozygous lap mouse, the lens placode seems to develop normally. However, the lens vesicle progresses abnormally to form a mass of cells without a cavity, and the mass vanishes soon afterward. We examined cell death in the lens anlage of this mutant. The lens anlagen of homozygous lap and normal mice from days 10 to 12 of gestation were observed by light microscopy after DNA end-labeling by immunohistochemistry and by transmission electron microscopy. By light microscopy, a slight frequency of cell death was detected in the lens anlage encircling the surface ectoderm and in the anlage or in the anlage of both homozygous lap mice and normal mice at day 10 of gestation. Cell death was seen in the lens anlage encircling the surface ectoderm in the normal mouse and sporadically in the anlage of the homozygous lap mouse at day 10.5 of gestation. Cell death was visible at the area of the lens vesicle attached to the surface ectoderm and encircling the surrounding surface ectoderm in the normal mouse, and in the lens anlage encircling the surface ectoderm and the apex areas of the lens anlage in the homozygous lap mouse at day 11 of gestation. At day 12 of gestation, almost no cell death was observed in the lens anlage of the normal mouse. However, extensive areas of cell death were still seen in the lens anlage at its apex, at the inner region, and encircling the surface ectoderm in the homozygous lap mouse. Electron microscopic observation showed that the dead cells observed in the lens anlagen by light microscopy in normal and lap mice are the result of apoptosis. In lap mice, cells with cytoplasmic condensation were observed mainly at days 10 and 10.5 of gestation. Many apoptotic bodies which had been phagocytosed by adjacent cells were seen predominantly at day 11 of gestation. At day 12 of gestation, apoptotic bodies phagocytosed by adjacent cells, which were seen at day 11, were still predominant, but there were more apoptotic bodies per cell and more digested apoptotic bodies than at day 11. These results indicate that cell death, resulting from apoptosis is involved in the disappearance of the lens anlage of lap mice.

Animals↗
PubMed1998

Characterization of mouse mast cell protease-8, the first member of a novel subfamily of mouse mast cell serine proteases, distinct from both the classical chymases and tryptases.

Using a recently developed PCR-based strategy, a cDNA encoding a novel mouse mast cell (MC) serine protease (MMCP-8) was isolated and characterized. The MMCP-8 mRNA contains an open reading frame of 247 amino acids (aa), divided into a signal sequence of 18 aa followed by a 2-aa activation peptide (Gly-Glu) and a mature protease of 227 aa. The mature protease has an M(r) of 25072, excluding post-translational modifications, a net positive charge of +12 and six potential N-glycosylation sites. MMCP-8 showed a high degree of homology with mouse granzyme B in the critical regions for determining substrate cleavage specificity, indicating that MMCP-8, similar to granzyme B, preferentially cleaves after Asp residues. A comparative analysis of the aa sequence of MMCP-8 with other hematopoietic serine proteases shows that it is more closely related to cathepsin G and T cell granzymes than to the MC chymases. We therefore conclude that MMCP-8 belongs to a novel subfamily of mouse MC proteases distinct from both the classical chymases and tryptases. Southern blot analysis of BALB/c genomic DNA indicated that only one MMCP-8 gene (or MMCP-8 like gene) is present in the mouse genome. Northern blot analysis of rodent hematopoietic cell lines revealed high levels of MMCP-8 mRNA in a mouse connective tissue MC-like tumor line. However, MMCP-8 mRNA could not be detected in mouse liver, intestine, lung or ears, indicating very low expression in normal tissues. Analysis of the expression of different MMCP in the tissues of Schistosoma mansoni-infected BALB/c mice showed a strong increase in MMCP-8 levels in the lungs but not in the intestines of infected animals, suggesting the presence of a novel subpopulation of MC in the lungs that expressed MMCP-8, either alone or in combination with MMCP-5 and carboxypeptidase A. The dramatic increase in MMCP-1 and MMCP-2 levels but not of MMCP-8 in the intestines of parasitized animals also shows that MMCP-8 is not expressed in mucosal MC in the mouse. This latter is in clear contrast to what has been observed in the rat where the MMCP-8 homologues, RMCP-8, -9 and -10, can be considered as true mucosal MC proteases.

Amino Acid Sequence↗
PubMed1991

Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein.

A polypeptide chain for the mouse interleukin 5 receptor (IL5R) was purified from detergent-lysed B13 cells, a mouse IL5-dependent pre-B cell line. Purification was by a single immunoaffinity chromatographic step using an anti-mouse IL5R monoclonal antibody, R52. Internal amino acid sequence was obtained from four trypsin-generated peptides. All peptides were found to be present in the published amino acid sequence of a mouse IL3R and the mouse IL3R-like protein deduced from the cDNA. This indicates that the mouse IL5R and the mouse IL3R have a homologous polypeptide in common and suggests that the specificity of these lymphokine receptors is mainly generated by association with another ligand-specific polypeptide chain.

Amino Acid Sequence↗
PubMed1995

Differences in the interleukin-2 (IL-2) receptor system in human and mouse: alpha chain is required for formation of the functional mouse IL-2 receptor.

Reconstitution with mouse interleukin-2 (IL-2) receptor subunits demonstrated that the mouse IL-2 receptor complex was different from the human complex in the alpha chain requirement for the functional mouse receptor complex. The heterotrimeric complex of the mouse exogenous alpha and beta chains and the endogenous gamma chain on mouse lymphoid BW5147 cells showed the ability to bind IL-2 with high affinity, resulting in IL-2-induced tyrosine phosphorylation of a cytosolic tyrosine kinase, JAK3, which is involved in IL-2-dependent signals. Exogenous introduction of the beta chain with the endogenous gamma chain, however, could neither confer appreciable IL-2 binding nor IL-2-induced signal transduction on BW5147 cells, unlike the human beta gamma heterodimer. Mouse spleen CD8+ cells, not having the alpha chain initially, showed IL-2-dependent cell proliferation only when expression of the alpha chain was induced. Collectively, these results illustrate that the functional mouse IL-2 receptor complex necessarily includes the alpha chain, and that the regulation of CD8+ T cell growth during immune reaction depends upon alpha chain expression.

Animals↗
PubMed1995

Mapping of the mouse homologue of the Wilson disease gene to mouse chromosome 8.

ATP7B, the gene altered in Wilson disease (WD) patients, lies in a block of homology shared between human chromosome 13q14 and the central region of mouse chromosome 14. However, we have mapped the murine homologue of ATP7B (Atp7b) to mouse chromosome 8 by somatic cell hybrid analysis. Analysis of 80 interspecific backcross offspring was used to position Atp7b close to D8Mit3 and another ATPase locus, Atp4b, on mouse chromosome 8. ATP4B lies in 13q34 and is separated from ATP7B by several loci whose mouse homologues map to mouse chromosome 14. The assignment of Atp7b to mouse chromosome 8 identifies a previously unrecognized region of homology between this chromosome and human chromosome 13. This assignment suggests a possible location for the toxic milk mutation in the mouse, which has been proposed as a homologue of WD.

Animals↗
PubMed1995

Human follicular fluid and mouse cumulus cells act synergistically to enhance preimplantation mouse Balb/cJ embryo development.

PROBLEM: The development of preimplantation mammalian embryos in vitro is less than optimal. Follicular fluid and cumulus cells have both been used, independently, to improve preimplantation embryo quality in culture. METHOD: To determine the ability of mouse cumulus cell coculture in the presence of human follicular fluids to support preimplantation mouse Balb/cJ embryo development in vitro. RESULTS: Culture of preimplantation mouse Balb/cJ embryo's independently in human follicular fluid or on mouse cumulus cells had no significant affect on blastocyst. The coculture of mouse Balb/cJ preimplantation-stage embryos on mouse cumulus cells in the presence of human follicular fluid significantly (P < 0.01) improved blastocyst development and the total number of cells per blastocyst. CONCLUSION: Cumulus cells and follicular fluid have a positive synergistic affect on preimplantation mouse Balb/cJ embryo development and formation in vitro.

Animals↗
PubMed2000

Intracerebroventricular infusion of CHO5, a rat monoclonal antibody directed against mouse low-affinity nerve growth factor receptor (p75NTR), specifically labels basal forebrain cholinergic neurons in mouse brain.

The finding that basal forebrain cholinergic cells are specifically endowed with the low-affinity nerve growth factor receptor p75NTR has been employed to develop a cholinergic immunotoxin in rats by covalently linking the monoclonal antibody 192IgG against the rat p75NTR with the cytotoxic protein saporin (192IgG-saporin). Following intracebroventricular application of 192IgG-saporin, the antibody conjugate is taken up into cholinergic cells via the p75NTR, retrogradely transported to the cell body, where saporin exerts cytotoxic action. The lack of an appropriate antibody directed against mouse p75NTR has been hampered the development of a mouse-specific cholinergic immunotoxin, which should be a useful tool to study effects of cortical cholinergic deficits on processing of amyloid precursor protein in transgenic mice with Alzheimer pathology. To develop an appropriate mouse-specific immunotoxin, a variety of antibodies directed against mouse p75NTR were tested. Using double labeling immunocytochemistry, the rat monoclonal antibody CHO5 against mouse p75NTR was found to label mouse basal forebrain neurons, which also demonstrated immunoreactivity for choline acetyltransferase and the high-affinity nerve growth factor receptor, TrkA. Intracerebroventricular infusion of CHO5 in mice resulted in an accumulation of the antibody in cholinergic cells within the basal forebrain, suggesting that CHO5 is a suitable candidate to develop a mouse-specific cholinergic immunotoxin.

Animals↗
PubMed2005

Mouse models in skeletal physiology and osteoporosis: experiences and data on 14,839 cases from the Hamburg Mouse Archives.

Our understanding of the developmental biology of the skeleton, like that of virtually every other subject in biology, has been transformed by recent advances in human and mouse genetics, but we still know very little, in molecular and genetic terms, about skeletal physiology. Thus, among the many questions that are largely unexplained are the following: why is osteoporosis mainly a women's disease? How is bone mass maintained nearly constant between the end of puberty and the arrest of gonadal functions? Molecular genetics has emerged as a powerful tool to study previously unexplored aspects of the physiology of the skeleton. Among mammals, mice are the most promising animals for this experimental work. The input that transgenic animals can offer to our field depends on our means of phenotypic characterization of the mouse skeleton. In fact, full appreciation of the skeletal characteristics of a given mouse model requires the application of standardized protocols for noninvasive imaging, histology, histomorphometry, biomechanics, and individually adapted in vitro and in vivo analysis. Over the past years we have established a mouse archive that consists of 14,839 cases from more than 120 different mouse models that we have phenotypically characterized in Hamburg. Today, this is one of the biggest databases on the mouse skeleton. This review focuses on one aspect of skeletal physiology, namely skeletal aging, and demonstrates that mouse models can be a valuable tool to gain insights in certain facets of skeletal physiology that have been unexplored previously.

Animals↗
PubMed1978

Assessment of plasminogen synthesis in vitro by mouse tumor cells using a competition radioimmunoassay for mouse plasminogen.

A sensitive, specific competition radioimmunoassay for mouse plasmin(ogen) has been developed in order to determine whether mouse tumor cells can synthesize plasminogen in vitro. The rabbit anti-BALB/c mouse plasminogen antibodies used in the assay react with the plasminogen present in serum from BALB/c, C3H, AKR and C57BL/6 mice, and also recognized mouse plasmin. The competition radioimmunoassay can detect as little as 50 ng of mouse plasminogen. No competition was observed with preparations of fetal calf, human and rabbit plasminogens. A variety of virus-transformed and mouse tumor cell lines were all found to contain less than 100 ng mouse plasminogen/mg of cell extract protein. Thus, if the plasminogen activator/plasmin system is important in the growth or movement of this group of tumor cells, the cells will be dependent upon the circulatory system of the host for their plasminogen supply.

Cell Line↗