Disease relevance of MOAP1

• Similarly, homologues of MAP-1 in other phylogenetically and antigenically related ehrlichial agents such as Anaplasma marginale and Ehrlichia chaffeensis are also targets of protective responses [1].
• Expression of microtubule-associated proteins, MAP-1 and MAP-2, in human neuroblastomas and differential diagnosis of immature neuroblasts [2].
• Other types of round-cell tumors examined, including several cases of Ewing's sarcoma, undifferentiated rhabdomyosarcoma, and malignant lymphoma, showed no reaction with antibodies to MAP-1 and MAP-2 [2].
• The map1 gene of Cowdria ruminantium is a member of a multigene family containing both conserved and variable genes [3].
• The fact that aromatic amino acids have been found to be the most representative of A-signal [Kuspa, A., Plamann, L. & Kaiser, D. (1992) J. Bacteriol. 174, 3319-3326] is consistent with the hypothesis that, regarding its specificity, MAP1 is likely to play a role in development of myxobacteria [4].

Psychiatry related information on MOAP1

• However, the amount of tau protein or MAP1 from the brains of Alzheimer's disease patients was about half of that present in their control counterparts [5].
• The hyperphosphorylated tau sequesters normal tau, MAP1 and MAP2, which results in breakdown of the microtubule network and, consequently, a progressive retrograde degeneration of the affected neurons and, ultimately, dementia [6].

High impact information on MOAP1

• RASSF1A/MAP-1 binding relieved this inhibitory interaction, resulting in MAP-1 association with Bax [7].
• The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death [7].
• Taken together the data suggested that estramustine binds to a 330-kD MAP-1-like protein to disrupt microtubules in tumor cells [8].
• Estramustine binds a MAP-1-like protein to inhibit microtubule assembly in vitro and disrupt microtubule organization in DU 145 cells [8].
• These surprising results contrast sharply with reported dramatic developmental increases in the amount of MAP1 in brain and in nerve growth factor-induced PC12 cells [9].

Chemical compound and disease context of MOAP1

• A DNA vaccine (VCL1010/MAP1) containing the major antigenic protein 1 (MAP1) gene of Cowdria ruminantium, driven by the human cytomegalovirus (HCMV) enhancer-promoter, was injected intramuscularly into 8-10 week-old female DBA/2 mice after treating them with 50 microliters/muscle of 0.5% bupivacaine three days previously [10].
• METHODS: Patients with refractory or recurrent acute lymphoblastic leukemia (ALL) were treated with a combination of methotrexate (MTX), vincristine, PEG-asparaginase, and prednisone (MOAP) [11].

Biological context of MOAP1

• We now identify a novel pathway connecting RASSF1A to Bax via the Bax binding protein MOAP-1 [12].
• A 280-kDa protein (p280) confined to the nucleus of interphase cells becomes associated with the mitotic spindle during cell division. p280 is immunologically related to the microtubule-associated protein MAP1, as shown by cross-reactivity with monoclonal (8D12) and polyclonal antibodies raised against MAP1 [13].
• Results of yeast two-hybrid analysis suggested that Map1 may physically interact with Mat1-Pc, the product of the h(+)-specific mating-type gene mat1-Pc [14].
• PolyQ72, but not polyQ11, stimulated Atg5-Atg12-Atg16 complex-dependent microtubule-associated protein 1 (MAP1) light chain 3 (LC3) conversion from LC3-I to -II, which plays a key role in autophagy [15].
• We have examined the post-translational modification of high molecular weight microtubule-associated proteins (MAPs) have shown that MAP1, MAP2, and MAP4 are glycosylated [16].

Anatomical context of MOAP1

• As one of the downstream modulaters of GR activation, Bax can be up regulated and translocated to the mitochondria, where it binds to modulator of apoptosis-1 (MAP-1), a mitochondrial effector of BAX to cause change Deltapsi [17].
• The MAP1-specific cDNA probes were used in blot transfer experiments with RNA prepared from brain, liver, kidney, stomach, spleen, and thymus [9].
• The occurrence and cellular localization of polypeptides related to hog brain microtubule-associated proteins 1 and 2 (MAP-1 and MAP-2) in non-neuronal cell lines of various species and types, and in several tissues from rat was studied [18].
• Immunoblotting of preparations from 3T6, CHO, HeLa and N2A cells, as well as pituitary, heart, testis and liver revealed immuno-reactivity with antibodies to neuronal MAP-1 for polypeptides co-migrating with MAP-1 in all cases, except for HeLa cells and liver [18].
• As shown by double immunofluorescence microscopy of various cultured cell lines using affinity-purified antibodies to MAPs, and monoclonal antibodies to tubulin, MAP-1-as well as MAP-2-related antigens were generally, but not exclusively, associated with typical microtubule structures of the cytoplasm, spindle, midbody and primary cilia [18].

Associations of MOAP1 with chemical compounds

• The MAP 1 minute and 10 minutes after ECT (101.25 [7.5] mm Hg and 100.16 [11.0] mm Hg, respectively) was significantly increased compared with before ECT (94.56 [6.9] mm Hg) in sevoflurane group (P < 0.05) [19].
• Three different conditions for preserving fresh sausages were tested: MAP1 (20% CO2, 70% O2, and 10% N2), MAP2 (40% CO2 and 60% O2), and MAP3 (40% CO2, 30% O2, and 30% N2) [20].

Regulatory relationships of MOAP1

• RASSF1A can activate Bax via MOAP-1 [12].

Other interactions of MOAP1

• Our findings identify RASSF1A and MAP-1 as important components between death receptors and the apoptotic machinery and reveal a potential link between tumor suppression and death receptor signaling [7].
• Late in infection (24-36 h) the anti-apoptotic genes largely shut down and the pro-apoptotic genes, including Nip3, Hrk, Bak, Bik, Bok, Bax, Bad, Bim and Moap-1, were activated [21].

Analytical, diagnostic and therapeutic context of MOAP1

• Genetic immunizations with the gene encoding MAP-1 induce protective T helper cell type 1 responses against lethal challenge in a mouse model [1].
• Immunocytochemistry shows that after 3 days in culture with CT beta, DEV cells develop processes which stain positive for neurofilaments and MAP-1 [22].
• We demonstrate, by sequence analysis, that map1 encoding the major outer membrane protein of C. ruminantium is also encoded by a polymorphic multigene family [3].
• An extracellular elastase, termed Myxococcus xanthus alkaline protease 1 (MAP1), has been purified from M. xanthus DK1622 culture supernatants by a combination of ion-exchange and affinity chromatographies [4].
• Two major antigenic proteins (MAPs), MAP1 and MAP2, have been examined for their use as antigens in the serodiagnosis of heartwater [23].

References