Disease relevance of Mnat1

• Several RadLV-induced lymphoma cell lines also produce p36, while it was not detectable in the radiation-induced lines tested [1].
• We conclude that p36 may represent a previously unrecognized transformation-related protein induced directly or indirectly by infection with RadLV [1].
• Caspase inhibition by Z-VAD-fmk or transfection with the baculovirus inhibitor p35 did not inhibit doxorubicin (DX)-induced cell death, yet suppressed the immunogenicity of dying tumor cells in several rodent models of neoplasia [2].
• Proteins of molecular mass 46,000 (p46) and 34,000-39,000 (p36) daltons are phosphorylated at tyrosine in Rous sarcoma virus-transformed chicken and mouse fibroblasts. p46 has recently been identified as an isozyme of enolase but the function of p36 is unknown [3].
• Constitutive activities of the P3 ADV and P36 ADV promoters were weaker than those of the corresponding promoters from the prototypic parvovirus minute virus of mice (MVM) and canine parvovirus (CPV) [4].

High impact information on Mnat1

• Stabilization and activation of CAK by p36 is independent of the phosphorylation state of T170, the conserved activating residue of CDK7 [5].
• In addition, p36 was not produced by mouse or mink fibroblasts or cultured thymocyte cell lines infected with virus passaged from the RadLV-induced lymphomas [1].
• We were unable to detect p36 in skeletal or smooth muscle cells, erythrocytes, nerve cells, or lymphocytes in any of the examined tissues. p36 appears to be concentrated in the terminal web region of intestinal columnar epithelial cells [3].
• By SDS gel electrophoresis and immunoblotting, high levels of p36 (60-120% of its relative abundance in fibroblasts) were found in small intestine, lung, and thymus, and intermediate levels (20-50%) were found in spleen, lymph nodes, and testes [3].
• Genetically attenuated, P36p-deficient malarial sporozoites induce protective immunity and apoptosis of infected liver cells [6].

Biological context of Mnat1

• Taken together, these data indicated that cis-acting sequences in the P36 ADV promoter play a major role in determining the low level of transactivation observed [4].
• To study the gene regulation of ADV, we have cloned the P3 ADV and P36 ADV promoters in front of a reporter gene, the chloramphenicol acetyltransferase (CAT) gene, and analyzed these constructs by transient transfection in a feline kidney cell line and mouse NIH 3T3 cells [4].
• This finding may indicate a different mechanism of transactivation of the early promoters (P3 ADV and P4 MVM) compared with the late (P36 ADV and P38 MVM) promoters [4].
• In the present work, we sought to optimize a mucosal vaccine by using the intranasal route for delivery of different antigen preparations, including (i) LaAg, (ii) soluble recombinant p36/LACK leishmanial antigen (LACK), and (iii) plasmid DNA encoding LACK (LACK DNA) [7].
• Listeria monocytogenes as a short-lived delivery system for the induction of type 1 cell-mediated immunity against the p36/LACK antigen of Leishmania major [8].

Anatomical context of Mnat1

• Although p35 was constitutively expressed and not affected by hapten application, p40 transcripts were found to be enhanced in lymph nodes obtained between 12 and 24 h after sensitization [9].
• The results of immunohistochemical staining also confirmed that MAT-1 reacts specifically with epidermal melanocytes in human skin sections [10].
• Thrombopenic purpura induced by a monoclonal antibody directed to a 35-kilodalton surface protein (p35) expressed on murine platelets and endothelial cells [11].
• Transcript levels peaked at P7 in hippocampus, increased linearly from P1 to P36 in cerebellum, and showed minimal developmental regulation in cerebral cortex [12].
• Using real-time RT-PCR, epsilon-SG was detected in both neural (cerebellar cortex, striatum, cerebral cortex, thalamus, hippocampus) and non-neural (muscle, liver, kidney, heart) tissues at each developmental time point tested [Embryonic Day 20 (E20), Postnatal Day 1 (P1), P7, P14, P36, 6 months, 1.5 years) [13].

Associations of Mnat1 with chemical compounds

• We report here the solution structure of the human MAT1 RING finger domain (Met(1)-Asp(65)) as determined by (1)H NMR spectroscopy [14].
• P36 phosphorylation also decreased when mice were given multiple BHT injections over a period of 5 weeks [15].
• Previously we have identified a cell surface-associated glycoprotein (p36) in N. caninum tachyzoites [16].
• Intracellular calcium mobilization was induced in splenic B and T lymphocytes after incubation of total spleen cells with LPS, p43 or p36 [17].
• The whole-cell voltage-clamp technique was used to examine developmental changes of inward rectifier currents in fibres of the flexor digitorum brevis muscle acutely isolated from mice on postnatal day 0 (P0) to P36 [18].

Analytical, diagnostic and therapeutic context of Mnat1

• The cell types within each tissue expressing p36 were identified by immunofluorescence and immunoperoxidase staining [3].
• RNA was extracted, and PCR analysis was performed using primers specific for the IL-12 subunits p35 and p40 [9].
• In Western blots, several CAP proteins (p80, p72-68, p36, p32, p18-12) were reactive with polyclonal antibodies raised against three separate LTR ORF synthetic peptides [19].
• Post-natal day 23 (P23) and P36 mutant and congenic control wild-type mice were kept in darkness overnight and eyes were examined by light and transmission electron microscopy 0.5 hr before, 1.5 hr after and 10.5 hr after lights turned on at 0700 hr [20].
• With a multiple time-point Northern blot, the same three transcripts were present in cerebellum at Embryonic Day (E15), Postnatal Day 1 (P1), P7, P14, P36 and 8 months [12].

References