Disease relevance of PNMA3

• Randomized trial comparing cyclophosphamide, epirubicin, and fluorouracil with cyclophosphamide, methotrexate, and fluorouracil in premenopausal women with node-positive breast cancer: update of National Cancer Institute of Canada Clinical Trials Group Trial MA5 [1].
• Epithelial mucin-1 (MUC1) expression and MA5 anti-MUC1 monoclonal antibody targeting in multiple myeloma [2].
• Neither B72.3 nor MA5 was specific for breast cancer cells: both also reacted with cells from benign and precancerous conditions [3].
• Monoclonal antibodies B72.3 and MA5 were tested by the avidin-biotin immunoperoxidase method in histologic sections of 38 benign, 22 precancerous and 22 cancerous breast lesions, as well as in fine needle aspiration (FNA) smears and cell blocks of 25 breast carcinomas [3].
• B72.3 as a "detector" of malignant cells or their precursors was superior to MA5, however: it was not reactive to cells in most benign breast lesions (mammary duct ectasia, fibroadenoma and ductal hyperplasia, with and without atypia) [3].

High impact information on PNMA3

• A bioinformatics approach to finding new cases of -1 frameshifting in the expression of human genes revealed a classical retrovirus-like heptanucleotide shift site followed by a potential structural stimulator in the paraneoplastic antigen Ma3 and Ma5 genes [4].
• MA5 mAb was strongly reactive with six of eight human MM cell lines by flow cytometry [2].
• The MA5 mAb, as well as other anti-MUC1 mAbs reactive with the MUC1 variable number tandem repeat domain, exhibited moderate to strong reactivity with both MM cell lines and clinical samples [2].
• To explore the biochemical nature and potential of MUC1 as an antigenic target in MM, studies were performed to: (a) compare the mRNA and the MUC1 glycoprotein species between epithelial cancer and MM cell lines; and (b) develop and use a human MM tumor xenograft model system to study the biodistribution of the MA5 mAb [2].
• Here, we report the correction and completion of the previously published prototype member PNMA1, the brain and testis restricted expression of a third member (PNMA3) and the sequences for further partially uncharacterized members of this novel neuronal protein family [5].

Biological context of PNMA3

• MIF4G and MA3 domains serve as binding sites for one or more isoforms of the eIF4A family of ATP-dependent DEAD-box RNA helicases that are required for translation and for nonsense-mediated decay [6].
• Proteins that contain the recently described MIF4G and/or MA3 domains function in translation, cell growth, proliferation, transformation, and apoptosis [6].

Associations of PNMA3 with chemical compounds

• Three major radicals are stabilized in 9-methyladenine at 10 K. These are: MA1, the adenine anion, probably protonated at N3; MA2, the species formed by net hydrogen abstraction from the 9-methyl group; and MA3, the radical formed by net hydrogen addition to C8 of the adenine moiety [7].
• In general, chlorophyll-retaining character was related to high carotenoid content (cultivars DN3, DN5, MA3, Mulato, RN1, and RN2) [8].

Analytical, diagnostic and therapeutic context of PNMA3

• CONCLUSION: The previously demonstrated benefit of CEF compared with CMF adjuvant chemotherapy is maintained with longer follow-up in the MA5 trial [1].
• Finally, biodistribution experiments were carried out with 131I-labeled MA5 versus a nonbinding control 125I-labeled mAb in a s.c. MM xenograft model [2].
• 125I-labeled MA5 whole-cell binding studies showed quantitatively similar amounts of binding between strongly positive MM lines and high-MUC1-expressing breast carcinoma lines. mRNA expression was assessed by Northern blotting and reverse transcription-PCR [2].
• Live human and monkey sperm were agglutinated and immobilized by MA1 but only immobilized by MA2 . With the Western blot technique, human sperm antigens of approximately 84,000, 240,000, 30,000 and 71,000 daltons were identified by antibodies MA1 , MA3 , MA4 and MA5 , respectively [9].

References