Disease relevance of Amy2

• Adult mouse liver expressed Amy-1 and Amy-2 at levels comparable to those of fully induced hepatoma cells [1].
• The oligonucleotides were complementary to sequences surrounding the translation initiation codons of the viral PB2 or PA genes (PB2-as or PA-as, respectively) of the influenza A virus RNA polymerases [2].
• These results indicated that PB1, PA, and NP can support the replication of the influenza virus genome as well as the transcription to yield uncapped poly(A)+ RNA and that PB2 is specifically required for the synthesis of capped RNA [3].
• Overall, our data show that secretory FGF-2 is involved in t-PA synthesis by pancreatic cancer cells and facilitates cell spreading [4].
• A murine monoclonal antibody (MAb), PA 8-15, was produced against a newly established human pancreatic adenocarcinoma cell line, SUIT-2 [5].

High impact information on Amy2

• Quantitative Southern blot hybridization using a DNA probe specific for the first exon of Amy-2 reveals the presence of greater than 10 Amy-2 related sequences per haploid CE/J genome [6].
• The number of active Amy-2 genes has been estimated in strain CE/J mice which produce four distinct electrophoretic forms of alpha-amylase in their pancreas. cDNA cloning and DNA sequence analysis discloses five distinct mRNA sequences which differ by approximately 1% of their nucleotides [6].
• The loss of an individual PA seems to be functionally complemented by the remaining PA but this compensation does not appear to involve any compensatory up-regulation [7].
• To investigate whether the reduced fertility of mice lacking PA gene function is due to a reduced ovulation mechanism, we have determined the ovulation efficiency in 25-day-old mice during gonadotropin-induced ovulation [7].
• These studies demonstrate that Amy-2 expression is not limited to the pancreas but also occurs at a low level in liver cells [1].

Chemical compound and disease context of Amy2

• An established cell line, clone 64, in which the expression of the RNA polymerase PB1 and PA subunit genes and the nucleoprotein (NP) gene but not the PB2 subunit gene of influenza virus can be induced by the addition of dexamethasone, was used to analyze the replication and transcription machineries of the influenza virus [3].
• With the avidin-biotin immunoperoxidase technique, PA 8-15 MAb reacted strongly with 27 of 28 formalin-fixed paraffin-embedded pancreatic adenocarcinoma tissues [5].

Biological context of Amy2

• Several members of the Amy-2 alpha-amylase multigene family from the CE/J strain of mouse have been cloned in cosmid vectors [8].
• All the orphons are identical and contain the entire 185 base-pairs of the first exon, 49 base-pairs of the first intron and more than 400 base-pairs of the Amy-2 5' flanking region [8].
• Both these traits are determined by genetic sites in the region of the Amy-2 locus on mouse chromosome 3 [9].
• A new simplified method for determining the Amy-1 and Amy-2 genotype of mice is presented [10].
• We have identified a distinct insulin-responsive element (IRE) located within the pancreatic enhancer of the mouse amylase gene Amy-2 [11].

Anatomical context of Amy2

• The tissue-specific expression of two types of mouse amylase genes does not overlap in vivo; the Amy-1 locus is transcribed in the parotid gland and the liver, while expression of Amy-2 is limited to the pancreas [12].
• However, PA 8-15 MAb was not reactive with inflammatory or benign tumors of the digestive system except for the epithelium, as was seen in normal adults [5].
• PA 8-15 MAb stained only the epithelium of the pancreatic duct, gall bladder and bile duct in normal adult tissues, and some normal fetal glandular epithelial cells [5].
• These results clearly demonstrated that after injury the PA system was rapidly induced in sensory neurons, where it may play an important role in nerve regeneration in vivo [13].
• In this study, the PA system was shown to be specifically activated in sensory neurons after sciatic nerve crush in adult mice [13].

Associations of Amy2 with chemical compounds

• Amy-2 is not detectable constitutively, but can be activated if the cells are cultured in serum-free medium containing dexamethasone [12].
• Intron and flanking-region sequences of the orphons differ by about 20% from their Amy-2 counterparts, and the exon by about 8% [8].
• About forty percent of the hexuronic acid residues in peonan PA exist as methyl esters [14].
• An acidic polysaccharide, called peonan PA, was isolated from the root of Paeonia lactiflora PALLAS [14].
• Peonan PA is composed of L-arabinose: D-galactose: D-galacturonic acid in the molar ratio of 2:1:10, in addition to small amounts of O-acetyl groups and peptide moieties [14].

Analytical, diagnostic and therapeutic context of Amy2

• Gene titration and cloning experiments suggest that at least four of the approximately 15 Amy-2 copies present in the CE/J genome contain 5' orphon elements [8].
• Addition of recombinant 18 kDa FGF-2 (rFGF-2) to cell cultures resulted in increased t-PA and decreased PAI-1 expression [4].
• Immunohistochemistry of human gastrointestinal cancer-associated antigen detected by monoclonal antibody PA 8-15 [5].
• Reactivity of PA 8-15 MAb with tissue specimens largely disappeared after treatment with neuraminidase, while oxidation with periodate or trypsin digestion did not alter the staining intensity, indicating that antigenic determinants may be at least partly of sialylated carbohydrate nature [5].

References