ArticleProceedings of the National Academy of Sciences of the United States of America1991
Multiple murine alpha 1-protease inhibitor genes show unusual evolutionary divergence.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 63 citations in OpenAlex.
- Multiple reaction monitoring assays for large-scale quantitation of proteins from 20 mouse organs and tissues.Communications biology · 2024Article
- Rosa26-LSL-dCas9-VPR: a versatile mouse model for tissue specific and simultaneous activation of multiple genes for drug discovery.Scientific reports · 2022Article
- Alpha-1 Antitrypsin Investigations Using Animal Models of Emphysema.Annals of the American Thoracic Society · 2016Review
- A novel model and molecular therapy for Z alpha-1 antitrypsin deficiency.Mammalian genome : official journal of the International Mammalian Genome Society · 2012Article
- Neuraminidase 1 is a negative regulator of lysosomal exocytosis.Developmental cell · 2008Article
- Serine protease inhibitors serpina1 and serpina3 are down-regulated in bone marrow during hematopoietic progenitor mobilization.The Journal of experimental medicine · 2005Article
- Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus.Journal of molecular evolution · 2004Article
- Asymmetric mutation rates at enzyme-inhibitor interfaces: implications for the protein-protein docking problem.Protein science : a publication of the Protein Society · 2003Article
- Differential regulation of gene activity and chromatin structure within the human serpin gene cluster at 14q32.1 in macrophage microcell hybrids.Nucleic acids research · 2000Article
- Sustained secretion of human alpha-1-antitrypsin from murine muscle transduced with adeno-associated virus vectors.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Divergent expression of alpha1-protease inhibitor genes in mouse and human.Nucleic acids research · 1998Article
- Synonymous and nonsynonymous substitutions in mammalian genes and the nearly neutral theory.Journal of molecular evolution · 1995Article
- On hypervariability at the reactive center of proteolytic enzymes and their inhibitors.Journal of molecular evolution · 1994Article
- Further examples of evolution by gene duplication revealed through DNA sequence comparisons.Genetics · 1994Article
- Evolution of the proteinase inhibitor I family and apparent lack of hypervariability in the proteinase contact loop.Journal of molecular evolution · 1994Article
- Evolution of murine alpha 1-proteinase inhibitors: gene amplification and reactive center divergence.Journal of molecular evolution · 1994Article
- A poplar tree proteinase inhibitor-like gene promoter is responsive to wounding in transgenic tobacco.Plant molecular biology · 1993Article
- Physical mapping of four serpin genes: alpha 1-antitrypsin, alpha 1-antichymotrypsin, corticosteroid-binding globulin, and protein C inhibitor, within a 280-kb region on chromosome I4q32.1.American journal of human genetics · 1993Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The murine alpha 1-protease inhibitors (alpha 1-PI) are encoded by a small gene family on chromosome 12. Studies of alpha 1-PI and other serine protease inhibitor genes have revealed an unusually high rate of mutation of the reactive centers of the inhibitors. Using a modification of the PCR technique, we have previously identified five distinct alpha 1 PI reactive site sequences present in the genome of C57BL/6 mice. In this report, we use cDNA cloning techniques to demonstrate that all five genes are expressed in the adult mouse liver. DNA sequence analysis shows that three of the five mRNAs expressed have a substitution for methionine-353, which is essential for normal activity of the homologous human protein, alpha 1-antitrypsin (alpha 1-AT). Comparison of the DNA sequences of the five cDNAs indicates a higher degree of polymorphism in the carboxyl-terminal half of the protein and an extraordinarily replacement/silent ratio of nucleotide changes in a narrow region surrounding the reactive site. The clustering of polymorphisms near the reactive site combined with the high replacement/silent ratio suggest an evolutionary mechanism that apparently selects for functional diversity of the alpha 1-PI genes. Finally, modeling of the three-dimensional positions of the alpha 1-PI polymorphic residues into the homologous positions of the crystallographic structure of ovalbumin, a member of the alpha 1-PI supergene family, predicts that many of these amino acids are on the surfaces, which are likely to interact with the protease targets.
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