Disease relevance of AMY2A

• The nucleotide sequence homologies of cDNAs between this carcinoid amylase and amy1, amy2 are 97.5% and 98.2%, respectively [1].
• The findings reveal that newly synthesized NP and PA proteins are required for influenza virus transcription and replication and provide a basis for the development of siRNAs as prophylaxis and therapy for influenza infection in humans [2].
• Mutation in NS2, a nonstructural protein of influenza A virus, extragenically causes aberrant replication and expression of the PA gene and leads to generation of defective interfering particles [3].
• However, siRNA specific for nucleocapsid (NP) or a component of the RNA transcriptase (PA) abolished the accumulation of not only the corresponding mRNA but also virion RNA and its complementary RNA [2].
• One patient (PA field) has died from seminoma [4].

High impact information on AMY2A

• In contrast to the observations of A549 cells, TGF beta caused a decrease in the expression of both urokinase and the tissue-type PA mRNA in human embryonic WI-38 lung fibroblasts indicating opposite regulation of the expression of PAs in these cells [5].
• Analysis of nucleotide sequence demonstrated that the NS gene of Wa-182 contained three point mutations relative to the wild-type NS gene that resulted in two amino acid substitutions in the nonstructural protein NS2, suggesting that the mutation in NS2 protein affected the normal replication of the PA gene of Wa-182 [3].
• The only other marker whose lod score exceeded 1.0 under any model was pancreatic amylase (AMY2) [6].
• The asparagine buffered sheet gel now allows the differentiation of the genotypes AMY2B/AMY2B,AMY2B/AMY2A, and AMY2B/AMY2C, thus classifying these three alleles as codominants [7].
• 1 chromosome since the AMY2 locus has been placed on the short arm of 1 [8].

Chemical compound and disease context of AMY2A

• Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses [9].
• RESULTS: PA protein was highly purified from insect cells infected with the recombinant baculovirus carrying PA cDNA, and a novel chymotrypsin-type serine protease activity was identified with the synthetic peptide, Suc-LLVY-MCA, in the PA protein [10].
• The observed down-regulation of transcription by C4 nucleotide is consistent with its potential role in segment-specific regulation of influenza virus gene expression, especially PB1, PB2 and PA proteins, during virus infection [11].
• The ascites PA activated plasminogen and showed amidolytic activity for S-2444 [12].
• Five factors were associated with a decrement in CrCl greater than the average decrease (17.6%): presence of hydronephrosis, age <50, no history of cisplatin treatment, a BED to gross adenopathy exceeding mean BED, and salvage treatment of PA node recurrence [13].

Biological context of AMY2A

• These findings can be explained by unequal homologous crossovers between AMY2A and AMY1A, resulting in haplotypes with one gene less or one gene more than the haplotypes described thus far [14].
• Nucleotide sequence analysis showed that the amylase expressed in this carcinoid tumor has 13 and 6 amino acid substitutions when compared with salivary amylase (Amy1) and pancreatic amylase (Amy2), respectively [1].
• It consists of ten major exons whose sequences are highly homologous to those of AMY1 and AMY2 [15].
• Only AMY2 has a second secondary binding site corresponding to an ESI2 complex [16].
• The hydrolysis of DP 4900-amylose, reduced (r) DP18-maltodextrin and maltoheptaose (catalysed by AMY1 and AMY2) was followed in the absence and in the presence of inhibitor [16].

Anatomical context of AMY2A

• Malaysians of Malay, Chinese, and Indian ancestries were electrophoretically phenotyped for Amy1 and saliva esterase region 1 (Set-1) from saliva, Amy2 from plasma, soluble and mitochondrial GOT and PGM3 from leukocyte and placenta [17].
• A starch-coated slide assay was used to quantitate amylase activity in amniotic fluids, and samples with activity were studied by electrophoresis to determine the presence of salivary amylase (Amy1) and pancreatic amylase (Amy2) isozymes [18].
• One of the pancreatic genes, AMY2B, is also transcribed at a low level in liver, but not from the promoter used in pancreas [19].
• CONCLUSION: In patients with testicular seminoma stage I (T1 to T3) and with undisturbed lymphatic drainage, adjuvant radiotherapy confined to the PA lymph nodes is associated with reduced hematologic, gastrointestinal, and gonadal toxicity, but with a higher risk of pelvic recurrence, compared with DL radiotherapy [4].
• Upon stimulation, alkyl-[32P]PC-labeled neutrophils do not produce [32P]phosphocholine, suggesting that PC is not hydrolyzed by phospholipase C. In addition, PA is formed in amounts sufficient to account for all of the DG formed during stimulation [20].

Associations of AMY2A with chemical compounds

• To distinguish AMY1 transcripts from a mixture of AMY1 and AMY2, use was made of the differences in the ethidium bromide-stained agarose gel patterns obtained after digestion of the amplified exon 3-4 fragments with TaqI [21].
• Consequently, in the presence of this oligosaccharide substrate, acarbose bound both to the active site and to a secondary binding site. alpha-CD inhibited the AMY1 and AMY2 catalysed hydrolysis of amylose, but was a very weak inhibitor compared to acarbose.beta- and gamma-CD are not inhibitors [16].
• The pleiotropic effects of retinoic acid (PA) in the developing and adult animal are mediated by ligand-inducible transcription factors (RA receptors [RARs] and retinoid X receptors [RXRs]) that belong to the superfamily of nuclear receptors [22].
• Following stimulation with fMLP, neutrophils double-labeled in alkyl-PC by incubation with [3H]alkyl-lysoPC and alkyl-[32P]lysoPC generate [3H]alkyl-DG and [32P]orthophosphate [( 32P]PO4) with superimposable kinetics, indicating degradation of PA by a phosphohydrolase [20].
• For purification of P protein complexes, the PA protein was expressed as a fusion with a histidine tag added at its N terminus [23].

Other interactions of AMY2A

• The short haplotype contains two pancreatic genes (AMY2A and AMY2B) and one salivary amylase gene (AMY1C), arranged in the order 2B-2A-1C, encompassing a total length of approximately 100 kb [24].
• We constructed a high resolution genetic map of the region flanking the polymorphic HSD3B1 and HSD3B2 genes including ten Généthon markers and the two NIH/CEPH markers AMY2B and D1Z5 [25].

Analytical, diagnostic and therapeutic context of AMY2A

• We studied the distribution of alpha-amylase mRNA in normal dog tissues by northern blotting (NB) and reverse transcription-polymerase chain reaction (RT-PCR) with human pancreatic (AMY2) and salivary (AMY1) alpha-amylase cDNA-specific primers [26].
• The genetically determined polymorphism of human pancreatic amylase (E.C. 3.2.1.1), AMY2, is demonstrated in serum specimens by agarose gel electrophoresis [27].
• PA activity was quantitated by caseinolysis assays, and characterized by urokinase mRNA analysis, immunoprecipitation, and zymography assays [5].
• Survival at 3 years was 99.3% for PA and 100% for DL radiotherapy [4].
• Within the first 18 months of follow-up, the sperm counts were significantly higher after PA than after DL irradiation [4].

References