Disease relevance of PITRM1

• The full-length hMP1 was expressed in the baculovirus system and purified to homogeneity using isoelectrofocusing and ion-exchange chromatography [1].
• The MP1-specific CTLs are amenable to subsequent genetic modification to express a CD19-specific CAR, designated CD19R, and acquire HLA-unrestricted reactivity toward CD19(+) leukemia and lymphoma tumor targets while maintaining HLA-restricted MP1 specificity [2].
• Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2 [3].
• We have previously reported the cloning and characterization of the MP1 gene in Penicillium marneffei and the AFMP1 gene in Aspergillus fumigatus and their use for serodiagnosis of penicilliosis and aspergilloma and invasive aspergillosis, respectively [4].
• A bacterial expression vector for the cDNA of Mn peroxidase isozyme H4 (lambda MP1) was constructed (R. E. Whitwam, I. G. Gazarian, and M. Tien, Biochem. Biophys. Res. Commun. 216, 1013-1017, 1995) whose expression in E. coli results in the formation of catalytically inactive polypeptide which can be refolded to active enzyme [5].

High impact information on PITRM1

• When overexpressed in cultured cells, MP1 enhanced activation of ERK1 and activation of a reporter driven by the transcription factor Elk-1 [6].
• A protein called MP1 (MEK Partner 1) was identified that bound specifically to MEK1 and ERK1 and facilitated their activation [6].
• These findings show that endosomal p14-MP1-MEK1 signaling has a specific and essential function in vivo and, therefore, indicate that regulation of late endosomal traffic by extracellular signals is required to maintain tissue homeostasis [7].
• p14-MP1-MEK1 signaling regulates endosomal traffic and cellular proliferation during tissue homeostasis [7].
• Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes [8].

Biological context of PITRM1

• The full-length MP1 codes for a protein with an open reading frame of 1038 amino acids [1].
• However, the enzyme did not exhibit strict monobasic cleavage specificity, as peptide substrates with amino acid substitutions around the monobasic site was cleaved efficiently by hMP1 [1].
• We also demonstrate that the MnP-encoding gene, lambda MP-1, encoding isozyme H4, and lambda MP-2 reside on separate chromosomes from each other and from the LiP-encoding genes [9].
• The genetic map for the MP1 family with 216 markers spanned 1,166 cM of the garlic genome (5.4 cM average), while 143 markers of MP2 spanned 862 cM (6.0 cM average) [10].
• METHODS: Central 10 degrees visual fields in 11 patients with Best's dystrophy (VA: 0.5+/-0.38) were recorded by the Octopus M2 TOP program and by MP (MP1, Nidek Technologies) [11].

Anatomical context of PITRM1

• The hMP1 mRNA is expressed in a number of cell lines and tissues as a single species of about 3.4 kb [1].
• The expression of hMP1 mRNA is higher in muscle and heart than in brain, pancreas, liver, lung, and placenta [1].
• Numerous filopodia from an identified growth cone (MP1) insert deep within another identified growth cone (pCC), inducing the formation of coated pits and vesicles [12].
• Enhanced antilymphoma efficacy of CD19-redirected influenza MP1-specific CTLs by cotransfer of T cells modified to present influenza MP1 [2].
• MP1 encodes an abundant and highly antigenic cell wall mannoprotein in the pathogenic fungus Penicillium marneffei [13].

Associations of PITRM1 with chemical compounds

• Four cell lines (MP1, -4, -5, -7), isolated from baby hamster kidney cells after simultaneous selection with N-(phosphonacetyl)-L-aspartate and methotrexate, have previously been shown to amplify their DNA at an increased rate [14].
• The clone, lambda MP-1, was isolated by screening a lambda gt11 expression library with polyclonal antibodies raised against a purified manganese-dependent peroxidase (isozyme H4, pI 4.5) [15].
• We found that substitutions at phenylalanine 2835, glycine 2839, or glycine 2840 resulted in a reduction in cleavage of MP1 [3].
• We found that the amino-terminal residue of MP1 corresponds to alanine 2841 [3].
• Using the PAP technique, the location of two new membrane-associated placental tissue proteins, MP1 and PP4 was studied in the placenta, its membranes, decidua and umbilical cord of human and cynomolgus monkeys [16].

Physical interactions of PITRM1

• Expression of MP1 in cells increased binding of ERK1 to MEK1 [6].

Other interactions of PITRM1

• Gel filtration of cell lysates revealed two major MP1 peaks: a broad high molecular weight peak and a 28 kDa complex [17].

Analytical, diagnostic and therapeutic context of PITRM1

• Immunodetection by electron microscopy revealed that MP1 and MP3 were structural proteins of the phage head and that MP2 was a constituent of the tail [18].
• Therefore, in order to improve the specificity of detecting Salm. typhi porins-specific antibodies, an inhibition ELISA was developed using enzyme-conjugated MoAbs (MP1 and MPN4) specific to Salm. typhi porins [19].
• In each patient, retinal sensitivity in the macular area was examined with the Micro Perimeter 1 (MP-1); retinal thickness was measured by optical coherence tomography (OCT) [20].
• Using the avidin-biotin binding system, an enzyme immunoassay procedure was developed to measure the membrane-associated placental tissue protein 1 (MP1) in serum [21].
• In standard Earle's solution, the impalement of 198 cells by a glass microelectrode was accompanied by an hyperpolarization (MP1 = -37.6 +/- 0.7 mV) (means +/- S.E.M.) followed by a gradual depolarization to a steady state potential (MP2 = -25.1 +/- 0.6 mV) (Joffre et al. 1984) [22].

References