Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned mRNA sequences

MacDonald, Raymond J.; Swift, Galvin H.; Quinto, Carmen; Swain, William F.; Pictet, Raymond; Nikovits, William; Rutter, William J.

doi:10.1021/bi00535a053

Cited by 120 publications

(69 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Mammalian coding sequences are generally high in third-codon-position G+C content (average of 65%; 72% with immunoglobulins removed from the sample), suggesting that mammalian tissues other than skeletal muscle will have coding sequences enriched in G+C (14)(15)(16)(17). A preliminary survey of cDNA sequences from mammalian pancreas indicates an intermediate G+C content [68% at the third codon position, an average of five proteins (18)(19)(20)(21)]. More sequence information will be required to determine codon usage patterns in tissues other than liver and muscle.…”

Section: Discussionmentioning

confidence: 99%

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Newgard¹,

Nakano²,

Hwang³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We have cloned the cD)NA encoding glycogen phosphorylase (1,4-a-D-glucan:orthophosphate a-D-glucosyltransferase, EC 2.4.1.1) from human liver. Blot-hybridization analysis using a large fragment of the cDNA to probe mRNA from rabbit brain, muscle, and liver tissues shows preferential hybridization to liver RNA. Determination of the entire qucleotide sequence of the liver message has allowed a comparison with the previously determined rabbit muscle phosphorylase sequence. Despite an amino acid identity of 80%, the two cDNAs exhibit a remarkable divergence in G+C content. In the muscle phosphorylase sequence, 86% of the nucleotides at the third codon position are either deoxyguanosine or deoxycytidine residues, while in the liver homolog the figure is only 60%, resulting in a strikingly different pattern of codon usage throughout most of the sequence. The liver phosphorylase cDNA appears to represent an evolutionary mosaic; the segment encoding the N-terminal 80 amino acids contains >90% G+C at the third codon position. A survey of other published mammalian cDNA sequences reveals that the data for liver and muscle phosphorylases reflects a bias in codon usage patterns in liver and muscle coding sequences in general.Glycogen phosphorylase (1,4-a-D-glucan:orthophosphate a-D-glucosyltransferase, EC 2.4.1.1) isozymes play a vital role in mobilization of stored sugar in a variety of mammalian tissues. Three forms of the enzyme have been described that are distinguished by their electrophoretic mobilities on gels and their immunological properties (1-3). The three isozymes are tissue-specific; the brain type (also known as the fetal type) is predominant in adult brain and embryonic tissues, while the liver and muscle types are predominant in adult liver and skeletal muscle tissues, respectively (reviewed in ref. 4). The muscle form is the best characterized; both the primary sequence and the x-ray structure of rabbit muscle phosphorylase are known (5-8). The enzyme functions in muscle to provide glucose required for the energy of contraction. Its physiological role is distinct from the liver isozyme, which is centrally involved in the maintenance of blood glucose homeostasis, and from the brain form, which is associated primarily with provision of an emergency glucose supply during brief periods of anoxia or hypoglycemia (4, 9).Comparisons of the protein and DNA sequences of the phosphorylase isozymes are required to understand the evolutionary and functional relationships among them. Further, such comparisons could ultimately provide insight into how the phosphorylase genes, and perhaps other multigene families, are regulated in a developmental and tissue-specific manner. We have described the cloning and sequencing ofthe rabbit muscle glycogen phosphorylase cDNA and portions of the C-terminal domain from human and rat muscle (6, 7). We report here the cDNA sequence and the deduced amino acid sequence for human liver glycogen phosphorylase. Comparison of liver and muscle phosphorylase sequences reveals extensive...

show abstract

Section: Discussionmentioning

confidence: 99%

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Newgard¹,

Nakano²,

Hwang³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Dr. R. MacDonald kindly gave us cDNAs encoding rat elastase and carboxypeptidase. These cDNAs cross-hybridize to X. laevis RNAs of about the same size as their respective rat mRNAs [1.1 kb for elastase I (MacDonald et al 1982b); 1.5 kb for carboxypeptidase B (Clauser et al 1988)]. The developmental pattern of gene expression (Fig.…”

Section: Developmental Profile Of the Expression Of Pancreatic-specifmentioning

confidence: 99%

Developmental and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis.

Shi

Brown²

1990

Genes Dev.

View full text Add to dashboard Cite

We have isolated and sequenced a cDNA encoding Xenopus laevis pancreatic trypsin, which has -70% amino acid sequence identity to mammalian trypsinogen. Northern blotting analysis shows that the trypsin gene is activated just before the tadpole starts to feed, reaches peak activity in the swimming tadpole (premetamorphosis), and is then repressed during prometamorphosis, attaining its lowest activity at the climax of metamorphosis. The same gene is then activated again in frogs but to a much lower level. The pattern of the changes in trypsin gene expression is followed by at least two other pancreas-specific genes and marks the remodeling of the pancreas of the animal at metamorphosis. Thyroid hormone, which is the causative agent of metamorphosis, can down-regulate trypsin gene expression prematurely.

show abstract

“…An 85% structural similarity was recorded between rat and porcine elastase I, but only 60% similarity between these two amino acid sequences and both human and rat elastase I1 (MacDonald et al 1982b;Kawashima et al 1987). The comparison between the rat lipase and colipase amino acid sequences, as deduced from the corresponding nucleotide sequences, and those of other mammalian species also indicated a fairly high degree of structural similarity (75-88 and 60-69% respectively).…”

mentioning

confidence: 89%

Molecular aspects of enzyme synthesis in the exocrine pancreas with emphasis on development and nutritional regulation

Huërou‐Luron¹,

Lhoste

Wicker‐Planquart

et al. 1993

Proc. Nutr. Soc.

View full text Add to dashboard Cite

Primary structure of two distinct rat pancreatic preproelastases determined by sequence analysis of the complete cloned mRNA sequences

Cited by 120 publications

References 52 publications

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Developmental and thyroid hormone-dependent regulation of pancreatic genes in Xenopus laevis.

Molecular aspects of enzyme synthesis in the exocrine pancreas with emphasis on development and nutritional regulation

Contact Info

Product

Resources

About