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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A partial EcoRI fragment of Bacillus coagulans DNA cloned in an Escherichia coli K12 bacteriophage lambda host-vector system was shown to direct the synthesis of a thermostable alpha-amylase whose activity could be detected in situ on petri plates using the iodine staining method. A 3.31 kb EcoRI fragment containing the active gene with its own promoter was subcloned in pBR322; in the new clone, called pAMY2, the amylase was shown to accumulate in the periplasmic space. The molecular weight of the enzyme, confirmed by in vivo labelling of plasmid products in minicells, was estimated to be 60000. The restriction map of the plasmid was determined for five restriction enzymes and two new plasmids with smaller DNA inserts were constructed, both directing the synthesis of amylase; one of them with a 2.2 kb PstI insert was shown to be responsible for the synthesis of a fused beta-lactamase-alpha-amylase protein with amylase activity.
Mol Gen Genet 1982
PMID:Cloning and expression of a Bacillus coagulans amylase gene in Escherichia coli. 618 47

The degree of activation of rat parotid gland cyclic AMP-dependent protein kinase (EC 2.7.1.37) was measured in tissue minces in vitro in order to assess the involvement of this enzyme in the parotid stimulus-secretion coupling mechanism. Kinase activation, determined by the activity ratio method, was measurably increased by isoproterenol, a beta-adrenergic agonist and a potent stimulator of alpha-amylase (EC 3.2.1.1) secretion. Muscarinic cholinergic and alpha-adrenergic stimulation, less effective in releasing amylase, did not affect protein kinase activation. Kinase activation closely paralleled the cyclic AMP concentration when the concentration of isoproterenol was varied. Amylase release exhibited a similar isoproterenol dose-dependence, except that amylase release was measurably increased at an isoproterenol concentration slightly lower than that required to increase detectably the cyclic AMP concentration or kinase activation. Partial dissociation between cyclic AMP levels, kinase activation, and secretion was seen when submaximal beta-adrenergic stimulation was combined with submaximal and supramaximal cholinergic stimulation. These results suggest an involvement of cyclic AMP-dependent protein kinase in beta-adrenergic-stimulated amylase release, but show that the extent of secretion is not rigidly coupled to the extent of kinase activation as determined by the activity ratio method. Protein kinase activation may function in concert with other factors in the regulation of exocytosis in this tissue.
Mol Pharmacol 1982 Jan
PMID:Rat parotid gland protein kinase activation. Relationship to enzyme secretion. 618 52

With appropriate measures to protect 3H-substance P (3H-SP) from proteolytic degradation and from nonspecific adsorption to glass-fiber filters, we have been able to demonstrate reliably a high-affinity specific binding of 3H-SP to rat submaxillary/sublingual gland membranes with a KD of 1 nM and Bmax of 6 pmoles/g of tissue. The relative potencies of various SP fragments and related analogues in reducing 3H-SP binding parallel their potencies in stimulating phosphatidylinositol turnover, amylase release, and salivation, thus supporting an association of the observed 3H-SP binding site with the physiological SP receptors in this tissue. This binding is selectively stimulated by some divalent cations (Mn2+ greater than Mg2+ greater than Ca2+) but inhibited by several guanyl nucleotides, suggesting a possible linkage to adenylate cyclase. However, no effect of SP on either the basal or the norepinephrine-stimulated adenylate cyclase activity could be demonstrated in salivary gland homogenates.
Mol Pharmacol 1983 May
PMID:3h-substance P binding to salivary gland membranes. Regulation by guanyl nucleotides and divalent cations. 619 Nov 91

The human protooncogene NRAS and the genes for the beta-subunit of nerve growth factor (NGFB) and for amylase (AMY) have previously been assigned to the proximal short arm of chromosome 1, but their precise positions have not been unequivocally established. By in situ hybridization of DNA probes for the three genes, we have ascertained the location of complementary sequences in mouse-human somatic cell hybrids that contained translocations of chromosome 1. The results agreed with the presence or absence of the human sequences as determined by Southern blotting of hybrid cell DNA. The in situ data confirmed that the genes were present on the cytologically recognized rearranged chromosome. Compared to the autoradiographic silver grain distribution on normal human chromosome 1, our in situ results obtained with the translocation chromosomes allowed much greater precision of mapping. Both NRAS and NGFB map to band 1p22, and AMY was confirmed in band 1p21.
Somat Cell Mol Genet 1984 Nov
PMID:Comparative analysis of mouse-human hybrids with rearranged chromosomes 1 by in situ hybridization and Southern blotting: high-resolution mapping of NRAS, NGFB, and AMY on human chromosome 1. 620 8

We report the nucleotide sequence of mRNA for the common electrophoretic isozyme of human pancreatic alpha-amylase, Amy2 A. The sequence was derived from a nearly full-length complementary DNA (cDNA) isolated from a cloned cDNA library. The relatively short 5' untranslated region (15 nucleotides) was determined by primer-extension sequencing. The human Amy2 messenger codes for a 511-residue preamylase polypeptide. An amino-terminal signal peptide of 15 amino acids with an Ala X Gln cleavage site is proposed based on homology to mouse, dog and hog amylases. The Amy2 A mRNA sequence differs from a recently reported human Amy2 sequence. Differences were found at 31 nucleotide positions. The alpha-amylase proteins predicted by the two mRNAs differ at 17 amino acid positions. Relative to the known sequences of other mammalian amylases, most of the differences between the two human Amy2 sequences appear to have occurred as substitutions in the sequence reported by Nakamura et al. (1984). These substitutions predict a protein with a substantially greater net negative charge than that of Amy2 A. We suggest that the two sequences may represent either divergent Amy2 alleles or the expression of non-allelic pancreatic amylase genes.
Mol Biol Med 1984 Oct
PMID:A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A. 633 37

Antibodies directed against centromeric chromatin characteristically occur in the sera of patients with the CREST variant of scleroderma. We have studied the in situ enzymatic sensitivity and solubility of the centromeric antigen and have isolated an antigenic moiety that reacts with anticentromere antibodies. The centromeric antigen in the human epithelial cell line, HEp-2, was sensitive to DNAase I and micrococcal nuclease but not affected by RNAase A, trypsin or amylase. It was insoluble in 0.15-4 M NaCl but was extracted from the HEp-2 cells by 4 M urea/2 M NaCl. Antigenic activity in a 4 M urea/2 M NaCl extract of rabbit thymus was demonstrated by immunoabsorption. Indirect immunofluorescence of the extract separated by polyacrylamide gel electrophoresis revealed a fluorescent band with a mol. wt of 33,000. Calf thymus and trout testis histone preparations were fractionated by gel electrophoresis and transferred by blotting techniques to diazobenzyloxymethyl cellulose paper for autoradiography. Anticentromere antibodies bound to and were absorbed by trout testis histone 1. We propose that the centromeric antigen may be a variant of histone 1 that is associated with condensed chromatin.
Mol Immunol 1984 Sep
PMID:Anticentromere antibodies bind to trout testis histone 1 and a low molecular weight protein from rabbit thymus. 638 63

A human genomic DNA segment (lambda hal) which hybridizes with rat pancreatic amylase cDNA was used to regionally assign amylase genes in human-mouse somatic cell hybrids. The assignment of amylase genes to chromosome 1 was confirmed and regionally mapped to the short arm region p22.1----p21 using a cell hybrid retaining a translocation involving chromosome 1 [46,XX,t(1;2)(p21;q37)]. Restriction length polymorphisms at the amylase loci are reported for gene linkage studies.
Somat Cell Mol Genet 1984 Mar
PMID:Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1. 660 95

During the last 60 years, the inversion polymorphism on the third chromosome of Drosophila pseudoobscura has become a case study of the evolution of linked blocks of genes, isolated from each other by the suppression of recombination in heterozygotes for different inversions. Due to its location within inverted regions in most gene arrangements, the amylase (Amy) gene region can be used to elucidate the molecular pattern of evolution in these inversions. We studied this region in the Tree Line phylad of gene arrangements, with regard to both restriction site polymorphisms (RSP) and nucleotide sequences. The analysis of restriction maps, encompassing 26 kb, corroborates the cytogenetic phylogeny established on the basis of inversion breakpoints. However, we found that the 2.7 kb of nucleotide sequences of the AmyI gene are identical in both Estes Park and Hidalgo arrangements, despite the fact that these inversions arose independently from Tree Line. These contrasting results suggest that a homogenizing force, most likely gene conversion, is able to bring about localized exchanges between otherwise isolated gene arrangements.
Mol Biol Evol 1995 Sep
PMID:Interchromosomal exchange of genetic information between gene arrangements on the third chromosome of Drosophila pseudoobscura. 747 40

Several cDNA clones with similarity to alpha-amylases have been characterized from a library made from adult female salivary gland RNA isolated from the vector mosquito, Aedes aegypti. The corresponding gene, designated Amylase I (Amy I), is expressed specifically in the proximal-lateral lobes of the adult female salivary gland, a pattern overlapping that of another gene, Mal I, involved in carbohydrate metabolism. The deduced amino acid sequence of Amy I indicates that this gene encodes a protein, approximate M(r) = 81,500, that appears to be a novel member of the amylase gene family. The mosquito protein contains a putative signal peptide for secretion and several consensus sites for asparagine-linked glycosylation. The Amy I protein shows significant similarity to invertebrate and vertebrate amylases including the conservation of four reactive and substrate binding sites. However, the amino-terminal region of the Amy-I protein is unique to the mosquito. Similarity with the Drosophila melanogaster protein is evident only after the first 260 amino acids in the mosquito sequence. The identification of this gene and its expression pattern adds to the observed relationship between spatial-specific gene expression in the female salivary glands and the specific feeding mode of the adult mosquito.
Insect Mol Biol 1993
PMID:The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family. 750 1

Effects of pertussis toxin (PT) treatment on atrial natriuretic peptide (ANP)-mediated inhibition of adenylate cyclase and amylase release were investigated in rat parotid gland. Adenylate cyclase activity stimulated by GTP gamma S in PT-treated membranes was much larger than that in normal membranes. ANP dose-dependently inhibited adenylate cyclase stimulated by GTP gamma S in control rat parotid membranes, however in membranes prepared from PT-injected (in vivo) rat parotid gland, ANP did not inhibit adenylate cyclase. ANP(10(-7)M) inhibited cAMP accumulation stimulated by forskolin (10(-6)M) in control rat parotid acinar cells by about 34%, however, in PT-treated cells, the inhibitory effect of ANP was attenuated completely. In control cells amylase release stimulated by isoproterenol (10(-6)M) and forskolin (10(-6)M) were also depressed by ANP (10(-7)M) by 27 and 30% respectively. The inhibitory response of ANP on amylase release was completely attenuated by PT-treatment. Gi was detected as a ADP-ribosylated 41-KDa protein by incubation of parotid membranes with PT and [alpha-32P]NAD. In rat parotid gland, these results suggested that ANP mediates adenylate cyclase/cAMP system and consequently reduces amylase release through ANP-C receptor coupled to Gi.
Mol Cell Biochem 1994 Oct 12
PMID:Effect of PT-treatment on ANP-mediated inhibition of adenylate cyclase and amylase release in rat parotid gland. 753 19


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