Three types of Amy-2-related DNA sequences, Amy-2a I, Amy-2a II and Amy-X, exist in the genome of mice of the inbred strain A/J. Amy-2a I and Amy-X are single copy sequences. Amy-2a II occurs as three copies per haploid genome. DNA sequence analysis reveals that both classes of Amy-2a genes specify the same unique pancreatic alpha-amylase mRNA species, since they share common exon sequences. Four independently cloned Amy-2a II isolates were found to be identical in all regions sequenced. This suggests that most, if not all, chromosomal Amy-2a II copies are identical. Amy-X is presumably a pseudogene, since its exon sequences, which are distinct from those of Amy-2a, are not detected in pancreatic alpha-amylase mRNA. We have determined the transcriptional activities of the Amy-2a genes by mapping in vitro elongated nascent transcripts to Amy-2a restriction fragments. Transcription initiation occurs at or close to the cap site. The expression of Amy-2a in vivo is under control of strong promoters, which are active exclusively in the pancreas. The accumulation of alpha-amylase mRNA in cells of the exocrine pancreas is regulated mainly at the transcriptional level. We have searched for pancreatic transcripts of Amy-1a, which specifies both parotid gland and liver-type alpha-amylase mRNAs. Surprisingly, the weak Amy-1a promoter, which directs the synthesis of the mRNA containing the liver-type leader sequence, also is active in the pancreas and, hence, in all alpha-amylase-producing tissues.
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http://dx.doi.org/10.1016/0022-2836(85)90404-8 | DOI Listing |
Mol Pharmacol
May 2005
School of Biological Sciences, University of Auckland, New Zealand.
Calcitonin (CT) receptors dimerize with receptor activity-modifying proteins (RAMPs) to create high-affinity amylin (AMY) receptors, but there is no reliable means of pharmacologically distinguishing these receptors. We used agonists and antagonists to define their pharmacology, expressing the CT(a) receptor alone or with RAMPs in COS-7 cells and measuring cAMP accumulation. Intermedin short, otherwise known as adrenomedullin 2, mirrored the action of alpha CGRP, being a weak agonist at CT(a), AMY(2a), and AMY(3a) receptors but considerably more potent at AMY(1a) receptors.
View Article and Find Full Text PDFClin Chim Acta
August 2002
Department of Biochemistry, Saitama Medical School, 38 Morohongo, Moroyama-machi, Iruma, Saitama 350-0495, Japan.
Background: The alpha-amylase isozymes can be detected separately by electrophoresis; however, sometimes the identification is difficult because of their microheterogeneity. In the present study, we tried to establish a convenient method for the detection of alpha-amylase isozyme expression.
Methods: The procedure is based on three different restriction sites presented in those genes; a PstI site in both AMY 2A and 2B genes, a HaeII site in both AMY 1 and 2A genes, and a BamHI site in AMY 2B gene.
Nucleic Acids Res
November 1986
Elastase II and trypsin mRNAs were cloned in form of their cDNAs from pancreas of strain A/J mice, and their complete nucleotide sequences were determined. The elastase II mRNA is 912 nucleotides long and encodes a protein of 271 amino acids. The cloned trypsin mRNA species is 814 nucleotides long and encodes a protein of 246 amino acids.
View Article and Find Full Text PDFThe two isozymes of pancreatic amylase in mouse strain YBR/Ki are encoded by closely linked genes which are independently regulated. We have isolated these two pancreatic amylase genes, Amy-2.1 and Amy-2.
View Article and Find Full Text PDFThree types of Amy-2-related DNA sequences, Amy-2a I, Amy-2a II and Amy-X, exist in the genome of mice of the inbred strain A/J. Amy-2a I and Amy-X are single copy sequences. Amy-2a II occurs as three copies per haploid genome.
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