Isolation and amino-terminal sequence analysis of a new pancreatic trypsinogen of the African lungfish Protopterus aethiopicus

C, de Haën; Ka, Walsh; Neurath, Hans

doi:10.1021/bi00639a015

Cited by 16 publications

(1 citation statement)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The unusual four aspartyl residues (Asp 4 ) preceding the cleavage bond Lys23-Ile24 (human trypsinogen numbering is used throughout the text) were found to be strictly conserved in trypsinogen activation peptides of pig (Charles et al 1963), sheep (Schyns, Bricteux-Gregoire, and Florkin 1969), and other mammals (e.g., Bricteux-Gregoire, Schyns, and Flokin 1972), including the human (Guy et al 1976(Guy et al , 1978. However, this is not always the case in nonmammalian vertebrates (e.g., de Haen, Walsh, and Neurath 1977). More recently, a comparative analysis of trypsinogen activation peptides suggested that there might be a progressive increase in selective pressure for such acidic residues during the course of vertebrate evolution (Roach et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Evolution of Trypsinogen Activation Peptides

Chen

Kukor

Maréchal³

et al. 2003

Molecular Biology and Evolution

103

View full text Add to dashboard Cite

The activation peptide of mammalian trypsinogens contains a highly conserved tetra-aspartate sequence (D19-D20-D21-D22) preceding the K23-I24 scissile peptide bond, which is hydrolyzed as the first step in the activation process. Here, we examined the evolution and function of trypsinogen activation peptides through integrating functional characterization of disease-associated mutations with comparative genomic analysis. Activation properties of three chronic pancreatitis-associated activation peptide mutants (the novel D19A and the previously reported D22G and K23R) were simultaneously analyzed, for the first time, in the context of recombinant human cationic trypsinogen. A dramatic increase in autoactivation of cationic trypsinogen was observed in all three mutants, with D22G and K23R exhibiting the most marked increases. The physiological activator enteropeptidase activated the D19A mutant normally, activated the D22G mutant very poorly, and stimulated activation of the K23R mutant. The biochemical and structural data, taken together with a comprehensive sequence comparison, indicates that the tetra-aspartate sequence in mammalian trypsinogen activation peptides has evolved not only for optimal enteropeptidase recognition in the duodenum but also for efficient inhibition of trypsinogen autoactivation within the pancreas. Moreover, the use of lysine instead of arginine at the P1 position of activation peptides also has an advantageous effect against trypsinogen autoactivation. Finally, fixed substitutions in the key residues of the trypsinogen activation peptide may suggest the evolution of new functions unrelated to digestion, as found in the group III trypsinogens of cold-adapted fishes.

show abstract

Section: Introductionmentioning

confidence: 99%

Evolution of Trypsinogen Activation Peptides

Chen

Kukor

Maréchal³

et al. 2003

Molecular Biology and Evolution

103

View full text Add to dashboard Cite

show abstract

An historical overview of the literature of dipnoi: Introduction to the bibliography of lungfishes

Conant

1986

J. Morphol.

View full text Add to dashboard Cite

The 2,200 citations of a bibliography of literature on the dipnoan fishes provide an overview of 150 years of work on lungfishes. Starting with Agassiz's volumes on fossil fishes in the 1830s and extending to papers from 1985, one can document the debate on the systematic position of dipnoans, the successive areas of research interest, and the continuing use of lungfish for comparative and evolutionary studies. The papers from 1837–1860 trace the misidentification and confusion surrounding the early discovery and description of Ceratodus, Lepidosiren, and Protopterus, centering on the uncertainty about whether to place the living genera among the fishes or the amphibians. The papers of the latter half of the 19th century show the influence of evolutionary theory, of the discovery of Neoceratodus, and of interest in embyrology. The trends in the 20th century reflect those of the larger scientific community. The listing will thus be useful both to the historian and to the active research scientist.

show abstract

A clade of trypsins found in cold‐adapted fish

Roach

2002

Proteins

View full text Add to dashboard Cite

A clade of trypsins, known as group III, is identified by phylogenetic analysis. These trypsins occur in fish that spend all or part of their lives at temperatures near 0 degrees C and may represent extreme psychrophilic enzymes. A principal component analysis of amino acid compositions distinguishes group III from mesophilic trypsins, as do molecular trees and multidimensional scaling of molecular sequence distances. The primary sequences of group III trypsins, in conjunction with the known structures of mesophilic trypsins, permit insight into function and mechanisms of cold adaption. The techniques employed are broadly applicable to phylogenies characterized by a markedly different, or "fast-evolving," clade. An updated lactate dehydrogenase molecular tree illustrates an additional fast-evolving clade.

show abstract

Isolation and amino-terminal sequence analysis of a new pancreatic trypsinogen of the African lungfish Protopterus aethiopicus

Cited by 16 publications

References 22 publications

Evolution of Trypsinogen Activation Peptides

Evolution of Trypsinogen Activation Peptides

An historical overview of the literature of dipnoi: Introduction to the bibliography of lungfishes

A clade of trypsins found in cold‐adapted fish

Contact Info

Product

Resources

About