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PubMed1977

Suppression of production of mouse 28S ribosomal RNA in mouse-human hybrids segregating mouse chromosomes.

Mouse-human somatic cell hybrids that lose (segregate) human chromosomes produce only mouse 28S ribosomal RNA even when they retain copies of the human chromosomes that contain the genes for 28S ribosomal RNA. In contrast, mouse-human hybrid cells that segregate mouse chromosomes produce only human 28S ribosomal RNA even when they have retained copies of mouse chromosomes that contain the 28S ribosomal RNA genes.

Animals↗
PubMed1986

[A comparison of two antigen strains of each of mouse hepatitis virus and mouse adenovirus for detection of complement fixation antibody in mouse and rat sera].

Detection rates of complement fixation antibodies in mice and rats were compared between two antigen strains of each of mouse hepatitis virus (MHV) and mouse adenovirus (MAV). Among 66 and 47 naturally infected MHV-positive sera of mice (18 facilities) and rats (16 facilities) respectively, 17 mouse and 21 rat sera reacted with both Nu-67 and MHV-2 strains, but 49 mouse and 25 rat sera were positive to Nu-67 strain alone. Only one rat serum reacted with MHV-2 strain alone. In comparison with K87 and FL strains of MAV, all 8 positive mouse sera (3 facilities) reacted with K87 strain alone whereas out of 53 positive rat sera (20 facilities), 43, 6 and 4 sera reacted with K87 strain alone, with FL strain alone and with both the two strains, respectively.

Adenoviridae↗
PubMed1979

Detection of proteolytic (C 3-cleaving) activity on mouse mastocytoma (P 815) cells and other mouse cell lines by formation of cell contact with C 3-carrying mouse lymphocytes.

Mouse mastocytoma cells (P 815) formed rosettes with normal mouse spleen lymphocytes which had been coated with uncleaved human C 3; this interaction was clearly dependent on the amount of C 3. Lymphocytes treated with C 3 b or buffer alone were ineffective. Formation of cell contact could be inhibited by the presence of protease inhibitors such as diisopropyl fluorophosphate, phenyl methyl sulfonyl fluoride and tosyllysyl chloromethyl ketone. Seve n out of 13 different cell lines behaved like P 815 cells. The results strongly suggested that a proteolytic activity on mouse tumor cells led to a cooperation with uncleaved C 3 on a carrier cell to connect these two cells. We interpreted these data in analogy to the complement-dependent bridge formation mechanism (M. P. Dierich and B. Landen, J. Exp. Med. 1977. 146: 1484): uncleaved C 3, attached to mouse spleen lymphocytes as carriers, becomes cleaved by enzymes associated with the tumor cells tested; by this cleavage, the labile binding site is released on C 3 (nascent C 3 b) and anchors the C 3-carrying cell to the protease-carrying cell; since this labile binding site is short-lived, this process can be induced by membrane-associated proteases only. The nature of the proteases and the biological implications of this process are as yet uncertain.

Animals↗
PubMed1982

Relationship between choline derivatives and mouse erythrocyte membrane antigens revealed by mouse monoclonal antibodies. I. Anticholine activity of anti-mouse erythrocyte monoclonal antibodies.

Different clones of mouse hybridomas, derived from the fusion of unstimulated mouse peritoneal cells with mouse myeloma cells, producing IgM monoclonal antibodies directed against the membrane of bromelain-treated mouse erythrocytes (MRBC(Br)) have been previously established. We have recently shown that one of these hybridomas produce, in ascites, antibodies cross-reacting with phosphorylcholine derivatives (trimethylammonium (TMA) derivatives). In this work the cross-reactivity for TMA derivatives of the monoclonal antibodies produced by 4 anti-MRBC(Br) hybridomas have been studied at the cell level (plaque-forming cells). Phosphorylcholine, choline bromide and p-aminophenyl-trimethylammonium were found to be potent specific inhibitors of plaque formation (anti MRBC(Br)). The hemolytic activities of ascites and tissue culture supernatants were studied and their inhibition by TMA derivatives was determined. Immunoglobulins from ascites purified on TMA immunoadsorbent column were analyzed by two-dimensional gel electrophoresis, their spectrotype was compared to the spectrotype of immunoglobulins from tissue culture supernatants from the same hybridoma radioactively tagged by internal incorporation of [14C]leucine. It could be shown without ambiguity that the PTMA column retained an IgM with the same characteristics as the IgM secreted in vitro.

Animals↗
PubMed2002

Identification of mouse submaxillary gland protein in mouse saliva and its binding to mouse oral bacteria.

The mouse submaxillary gland protein (mSMGP) is highly expressed in the submandibular gland of the adult mouse and rat. It shares 51% identity at the amino-acid level with a human protein, the prolactin-inducible protein (PIP)/gross cystic disease fluid protein 15 (GCDFP-15), which has been found in saliva, tears, sweat, seminal plasma, submucosal glands of the lung and amniotic fluid. More recently, the human PIP has been reported to bind to bacterial strains normally found in the mouth, ear canal and human skin. Sequence analysis of mSMGP/PIP earlier identified the presence of a signal peptide, suggesting that it is a secreted protein. Here, by Western blotting, mSMGP/PIP has been identified in mouse saliva. To investigate further the role of this secreted protein, its ability to bind specifically to oral bacteria was examined; the hypothesis was that mSMGP/PIP is involved in non-immune host defence by binding to bacteria. Several bacterial strains, found to belong to the genera Streptococcus, Aerococcus, Pseudomonas, Staphylococcus, Sphingomonas, Vibrio and Aeromonas, were isolated from the mouse oral cavity. Following incubation of these bacteria with (35)S-labeled, in vitro-translated mSMGP/PIP, the protein was found to bind specifically and selectively to several but not all strains tested, showing the highest affinity for the streptococci. The protein also bound specifically to an Aerococcus sp., and a low binding interaction with the Pseudomonas and Staphylococcus spp. was observed. The conservation of SMGP sequences among several animal species suggests that this protein may play an important part in the biology of the submandibular gland. As the function of the mSMGP/PIP is still undetermined, these findings provide insight into a possible involvement of this protein in host defence.

Animals↗
PubMed1994

Follicle-stimulating hormone receptor mRNA in the mouse ovary during post-natal development in the normal mouse and in the adult hypogonadal (hpg) mouse: structure of alternate transcripts.

The structure of RNA encoding the mouse ovarian follicle-stimulating hormone (FSH) receptor was studied during post-natal development and in the adult hypogonadal (hpg) mouse which lacks circulating gonadotrophins. Using reverse transcription and the polymerase chain reaction (PCR) four major transcripts of the FSH receptor were found in the normal adult ovary. The largest transcript was the expected size from the position of the PCR primers (on exons 1 and 10) and sequencing confirmed that it was derived from FSH receptor mRNA. The three other transcripts were also derived from FSH receptor mRNA but they contained deletions corresponding to one or more complete exons. Each transcript lacked exon 2 while exons 5 and/or 6 were lacking in the smaller species. All four transcripts were present in ovaries of hpg mice showing that expression of receptor mRNA and development of alternate splicing are not gonadotrophin-dependent. During development in the mouse full-length FSH receptor transcripts were not detected in the ovary until day 5 although shorter transcripts were present at days 1 and 3. Results confirm that the FSH receptor primary transcript undergoes alternate splicing in the ovary and that the pattern of splicing changes as the ovary develops, probably as a result of follicular development.

Alternative Splicing↗
PubMed1999

The Mouse Genome Database (MGD): genetic and genomic information about the laboratory mouse. The Mouse Genome Database Group.

The Mouse Genome Database (MGD) focuses on the integration of mapping, homology, polymorphism and molecular data about the laboratory mouse. Detailed descriptions of genes including their chromosomal location, gene function, disease associations, mutant phenotypes, molecular polymorphisms and links to representative sequences including ESTs are integrated within MGD. The association of information from experiment to gene to genome requires careful coordination and implementation of standardized vocabularies, unique nomenclature constructions, and detailed information derived from multiple sources. This information is linked to other public databases that focus on additional information such as expression patterns, sequences, bibliographic details and large mapping panel data. Scientists participate in the curation of MGD data by generating the Chromosome Committee Reports, consulting on gene family nomenclature revisions, and providing descriptions of mouse strain characteristics and of new mutant phenotypes. MGD is accessible at http://www.informatics.jax.org

Animals↗
PubMed1986

Enhanced casein kinase II activity during mouse embryogenesis. Identification of a 110-kDa phosphoprotein as the major phosphorylation product in mouse embryos and Krebs II mouse ascites tumor cells.

Mouse embryos at various stages of development were used to study the relationship of protein kinase activities with normal embryogenesis. Casein kinase II (CKII) activity in developing mouse embryos shows a 3-4-fold activity increase at day 12 of gestation. Together with the CKII activity, increased phosphorylation of a 110-kDa protein is observed. Treatment of the embryo extracts with heparin, a highly specific inhibitor of CKII activity, results in a drastic reduction of the 110-kDa protein phosphorylation indicating that the protein might be a CKII-specific substrate. Rapidly proliferating mouse tumour cells also show an enhanced CKII activity. Here too, a 110-kDa phosphoprotein was the major phosphoryl acceptor. Partial proteolytic digestion shows that both proteins are identical. Other protein kinases tested (cAMP- and cGMP-dependent protein kinases) only show a basal level of enzyme activity with minor alterations throughout the different stages of embryogenesis investigated.

Animals↗
PubMed1988

Reactivity of mouse antibodies against bromelain-treated mouse erythrocytes with various mouse cells before and after protease treatment.

A mouse monoclonal antibody against bromelain-treated mouse erythrocytes (BrMRBC) was conjugated with fluorescein isothiocyanate. Various cells from the blood and lymphoid tissues of mice were stained before and after protease treatment with the fluorescent antibody. Without protease treatment, only the platelets were specifically, though dully, fluorescent. Protease treatment made all the erythrocytes, the majority of platelets, thymus and bone marrow cells and a small part of the spleen cells brightly fluorescent. The reactivity of the antibody with cells depended on the temperature, being stronger at 0 than at 37 degrees C. The present findings demonstrate that various mouse cells besides erythrocytes bear the epitopes for anti-BrMRBC antibodies in exposed or hidden form.

Animals↗
PubMed1989

Reactivity of mouse antibodies against bromelain-treated mouse erythrocytes with thrombin-treated mouse platelets.

The reactivity of mouse antibodies against bromelain-treated mouse erythrocytes (BrMRBC) with mouse platelets before and after thrombin treatment was assessed by flow cytometry. Anti-BrMRBC antibodies could bind to thrombin-treated platelets, although normal platelets were also weakly reactive with the antibodies. The binding of anti-BrMRBC antibodies to platelets was confirmed by complement-dependent lysis. It is suggested that thrombin-activated platelets may be a real target for anti-BrMRBC antibodies.

Animals↗
PubMed1995

Genomic cloning of mouse MIF (macrophage inhibitory factor) and genetic mapping of the human and mouse expressed gene and nine mouse pseudogenes.

The single functional mouse gene for MIF (macrophage migration inhibitory factor) has been cloned from a P1 library, and its exon/intron structure determined and shown to resemble that of the human gene. The gene was mapped to chromosome 10 using two multilocus crosses between laboratory strains and either Mus musculus musculus or Mus spretus. Nine additional loci containing related sequences, apparently all processed pseudogenes, were also mapped to chromosomes 1, 2, 3, 7, 8, 9, 12, 17, and 19. While most of these pseudogenes were found in inbred mice and M. spretus, some are species specific. This suggests that there have been active phases of pseudogene formation in Mus both before and after the separation of musculus and spretus. The human genome contains no pseudogenes; we assigned the human gene to chromosome 19, consistent with the location of mouse and human functional genes for MIF in a region of conserved linkage.

Amino Acid Sequence↗
PubMed1987

The mouse homolog of the human amyloid beta protein (AD-AP) gene is located on the distal end of mouse chromosome 16: further extension of the homology between human chromosome 21 and mouse chromosome 16.

The human amyloid beta protein is the major constituent of the brain amyloid plaques found in Alzheimer disease. The gene that encodes this protein is located on chromosome 21, and individuals with Down syndrome (trisomy 21) also exhibit an early onset form of Alzheimer disease. We have used the cloned human amyloid beta protein gene and a panel of somatic cell hybrids to map the location of the mouse homolog of this gene. We report here that the mouse gene is located on chromosome 16 within the region 16C3----ter, in common with three other genes which map within the Down syndrome region of human chromosome 21.

Amyloid↗
PubMed1991

One-step double immunolabeling of mouse interdigitating reticular cells: simultaneous application of pre-formed complexes of monoclonal rat antibody M1-8 with horseradish peroxidase-linked anti-rat immunoglobulins and of monoclonal mouse anti-Ia antibody with alkaline phosphatase-coupled anti-mouse immunoglobulins.

A novel one-step double immunolabeling method was elaborated on the basis of the simultaneous application of preformed molecular complexes of two primary antibodies with their specific secondary antibodies labeled with different enzymes. Treatment with a rat monoclonal antibody (MAb), M1-8, pre-coupled with horseradish peroxidase-linked sheep anti-rat immunoglobulins, and enzyme reaction revealed by the 3-amino-9-ethylcarbazole/hydrogen peroxide reaction, resulted in red-brown intracytoplasmic staining of interdigitating reticular cells in the lymph nodes of Balb/c mice. Another molecular complex, made of mouse anti-Ia MAb with alkaline phosphatase-linked rabbit anti-mouse immunoglobulins, applied at the same time and then developed with naphthol AS-BI-phosphate/fast blue BB as substrate, yielded blue surface staining of this cell type in addition to labeling of B-lymphocytes. The method described provides the possibility of relatively rapid double antigen detection where the binding sites of the secondary antibodies are saturated by the specific primary immunoglobulins. This approach seems to avoid nonspecific binding of primary antibodies to Fc receptors, and the unwanted binding of secondary antibodies with cell surface immunoglobulins on B-lymphocytes or with crossreactive primary antibodies used in the other sequence, if the primary antibodies and the tissue are the same or crossreactive animal species.

Alkaline Phosphatase↗
PubMed1987

The lipolytic effects of mouse placental lactogen II, mouse prolactin, and mouse growth hormone on adipose tissue from virgin and pregnant mice.

The lipolytic activities of three structurally related mouse hormones, placental lactogen II (mPL-II), GH (mGH), and PRL (mPRL), and human PL (hPL) were investigated. Adipose tissue was obtained from virgin and day 12 and day 16 pregnant mice. Lipolytic activity was assessed by the ability of the hormones to stimulate glycerol release from fat explants in the presence of dexamethasone and by the ability of the hormones to sensitize adipose tissue to the lipolytic stimulus theophylline. In the first experiment, adipose tissue explants were incubated in Krebs-Ringer buffer with 0.0, 0.1, 0.5, 1.0, 5.0, and 10.0 micrograms/ml hormone for 4 h. mGH was lipolytic at a concentration of 0.5 micrograms/ml or greater in adipose tissue from both virgin and pregnant mice. mPRL was lipolytic at a concentration of 5.0 micrograms/ml or greater in adipose tissue from virgin mice. In adipose tissue from pregnant mice mPRL was not lipolytic in day 12 tissue, but it was lipolytic at a concentration of 5.0 micrograms/ml in day 16 tissue. mPL-II and hPL did not stimulate glycerol release in mouse adipose tissue from virgin or pregnant mice. In the second experiment preincubating adipose tissue from virgin mice in the presence of 0.5 or 5.0 micrograms/ml mGH significantly increased the ability of the tissue to respond to theophylline; however, mGH did not induce this response in adipose tissue from pregnant mice, mPRL, mPL-II, and hPL did not increase theophylline-induced lipolysis in adipose tissue from either virgin or pregnant mice. These results indicate that two lipolytic mechanisms are activated in adipose tissue from mice; mGH can activate both mechanisms, whereas mPRL can activate only one.

Adipose Tissue↗
PubMed1990

A congenic line of the BALB/c mouse strain with the endogenous mouse mammary tumor virus proviral gene Mtv-3: tissue-specific expression and correlation with resistance to mouse mammary tumor virus infection and tumorigenesis.

Mouse mammary tumor virus (MMTV) expression and MMTV-induced tumorigenesis were studied in a congenic line of the BALB/cHeA strain, termed BALB/c-Mtv-3+, that carries the Mtv-3 proviral gene. BALB/c-Mtv-3+ mice were free of milk-transmitted MMTV and did not spontaneously develop mammary tumors. A specific Mtv-3 expression was observed in the mammary gland and spleen, but not in other lymphoid tissues, such as thymus and bone marrow. This expression was hormone dependent, as shown by the increase of MMTV mRNA during pregnancy. At the protein level, large amounts of p28, but only traces of gp52, the main MMTV core and envelope antigens, respectively, were observed, in agreement with the already described "partial" expression of the Mtv-3 gene products. The presence of the 24S (3.8 kilobases) mRNA encoding the MMTV env antigens in the spleen and the low gp52 reactivity in lactating mammary glands showed that this noncoordinate expression was probably due to a defect in translation or posttranslational processing of env proteins. The susceptibility of BALB/c-Mtv-3+ to experimental MMTV infection was studied. The presence of Mtv-3 conferred to BALB/c mice resistance to MMTV infection, as shown by measuring viral antigens released in the milk of infected mice and by recording the incidence of early mammary tumors. The presence of a nontumorigenic endogenous MMTV gene was therefore protective against exogenous MMTV infection.

Animals↗
PubMed2006

Characterization of endotoxin and mouse allergen exposures in mouse facilities and research laboratories.

OBJECTIVES: Researchers and technicians who use mice in research are exposed to complex mixtures containing mouse allergen, endotoxin and particulates from animals, bedding and feed. The particle characteristics of these different exposures, and whether they are encountered together or separately, are important to better understand their adjuvant and allergic effects. Endotoxin and mouse allergen are derived from the same animal source, but have different physicochemical attributes. It is not known if airborne exposures to these agents are correlated in the laboratory animal workplace. METHODS: Side-by-side personal and area samples for airborne endotoxin (52), mouse allergen (46) and total particulates (43) were obtained in the animal facility and laboratories of a medical research institution. Animal handlers and researchers reported time spent on work tasks with mice, symptoms upon exposure to mice and mouse sensitization was determined by skin test or RAST. RESULTS: Mean airborne endotoxin exposure was highest during mouse experiments in the animal facility at 960 pg m(-3), peaked at 3125 pg m(-3), and ranged from 46 to 678 pg m(-3) with work in mouse rooms and research labs. Mouse allergen concentrations were highest during direct mouse work and background in research labs (mean 63-68 ng m(-3), range 41-271 ng m(-3)), but were undetectable during mouse research performed under a hood. Endotoxin and mouse allergen concentrations were correlated during direct research with mice and mouse care activities. Particle counts were low, typically < 1 cm(-3), varied widely, and exhibited peaks and valleys during different work tasks. From 80-90% of particles were < 1 microm in aerodynamic diameter during background measurements. The contribution of respirable particles 1-5 microm in size increased to 25-30% during mouse care and mouse research activities, but we found no association between any particle size and endotoxin or mouse allergen concentrations. Animal handlers and researchers in the mouse facility were exposed to the highest daily endotoxin concentrations, whereas researchers working with mice in the mouse facility and in laboratories were exposed to the highest daily mouse allergen concentrations. CONCLUSIONS: These findings suggest that endotoxin and mouse allergen are co-exposures during mouse handling and research, and that control of exposure peaks may be necessary to limit allergic disease in the laboratory animal workplace.

Air Pollutants, Occupational↗
PubMed1996

An alternative splice variant of the mouse TRH receptor mRNA is the major form expressed in the mouse pituitary gland.

The sequences of the mouse and rat TRH receptors (TRH-Rs) show 94% similarity at the protein level. However, they differ significantly at their carboxy terminals, i.e. the mouse TRH-R ends with an asparagine at position 393 while, in the rat, residue 393 is lysine and an additional 19 amino acids are added before the first stop codon. In the mouse cDNA, the sequence encoding these additional amino acids is located 224 bp downstream in the 3' untranslated region (3'UT). As the mouse TRH-R was cloned from thyrotrope-derived TtT97 tissue and the rat TRH-R from lactotrope-derived GH cell lines, we have investigated whether this difference at the carboxy terminus represents a species-specific or cell type-specific pattern of TRH-R expression. Total RNA was isolated from mouse pituitary and TtT97 tissue, and rat pituitary and GH3 cells. Reverse transcription PCR analysis was performed using primers that would generate DNA fragments including the stop codon in either the mouse or the rat TRH-R and, in the mouse form, the extra 224 bp of 3'UT. This would generate a product of 234 bp from the rat sequence and 441 bp from the mouse sequence. In rat pituitary and GH3 cDNA, PCR generated the expected 234 bp product but not a band representing the mouse sequence. In both mouse pituitary and TtT97 cDNA, neither the expected 441 bp nor the 234 bp fragments were amplified; instead a larger, 829 bp, product was generated. Sequence analysis revealed a 388 bp insertion at position 1663 in the 3'UT compared with the published mouse TRH-R sequence. Ribonuclease protection analysis using this 829 bp fragment as a probe showed that this sequence represented the major TRH-R mRNA species in mouse pituitary and TtT97 RNA. A genomic clone containing this region of the mouse TRH-R gene was isolated and analysis of the sequence in this region revealed that this longer form of the mouse TRH-R could be generated by alternative splicing. In summary, we have shown that the carboxyterminal differences between the mouse and rat TRH-Rs are species-specific rather than cell type-specific, and that the major TRH-R mRNA expressed in mouse pituitary contains an additional 388 bp of 3'UT compared with the published sequence. As a region in the 3'UT of the published mTRH-R sequence has been shown to be important for stability of this mRNA, this additional 3'UT sequence could have major effects on the regulation and stability of the mouse TRH-R mRNA.

Alternative Splicing↗