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Article: Variation in the Evolution and Sequences of Proglucagon and the Receptors for Proglucagon-Derived Peptides in Mammals.

Irwin, David M

2021 Volume 12, Page(s) 700066

Abstract: The mammalian proglucagon gene ( ...

Abstract	The mammalian proglucagon gene (
MeSH term(s)	Amino Acid Sequence ; Animals ; Evolution, Molecular ; Genetic Variation ; Genome ; Glucagon/genetics ; Glucagon-Like Peptide 1 ; Glucagon-Like Peptide 2 ; Glucagon-Like Peptide-1 Receptor/genetics ; Glucagon-Like Peptide-2 Receptor/genetics ; Mammals ; Phylogeny ; Proglucagon/genetics ; Receptors, Glucagon/genetics
Chemical Substances	Glucagon-Like Peptide 2 ; Glucagon-Like Peptide-1 Receptor ; Glucagon-Like Peptide-2 Receptor ; Receptors, Glucagon ; Proglucagon (55963-74-1) ; Glucagon-Like Peptide 1 (89750-14-1) ; Glucagon (9007-92-5)
Language	English
Publishing date	2021-07-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2021.700066
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Article: Evolution of the Insulin Gene: Changes in Gene Number, Sequence, and Processing.

Irwin, David M

Frontiers in endocrinology

2021 Volume 12, Page(s) 649255

Abstract: Insulin has not only made major contributions to the field of clinical medicine but has also played central roles in the advancement of fundamental molecular biology, including evolution. Insulin is essential for the health of vertebrate species, yet its ...

Abstract	Insulin has not only made major contributions to the field of clinical medicine but has also played central roles in the advancement of fundamental molecular biology, including evolution. Insulin is essential for the health of vertebrate species, yet its function has been modified in species-specific manners. With the advent of genome sequencing, large numbers of insulin coding sequences have been identified in genomes of diverse vertebrates and have revealed unexpected changes in the numbers of genes within genomes and in their sequence that likely impact biological function. The presence of multiple insulin genes within a genome potentially allows specialization of an insulin gene. Discovery of changes in proteolytic processing suggests that the typical two-chain hormone structure is not necessary for all of inulin's biological activities.
MeSH term(s)	Algorithms ; Animals ; Computational Biology/methods ; Evolution, Molecular ; Gene Duplication ; Genome ; Humans ; Insulin/genetics ; Insulin/metabolism ; Inulin/chemistry ; Mice ; Microbiota ; Phylogeny ; Rats ; Signal Transduction ; Species Specificity
Chemical Substances	Insulin ; Inulin (9005-80-5)
Language	English
Publishing date	2021-04-02
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2021.649255
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Article ; Online: Evolution of the mammalian insulin (Ins) gene; Changes in proteolytic processing.

Irwin, David M

Peptides

2020 Volume 135, Page(s) 170435

Abstract: Disruption of insulin signaling in humans leads to diabetes yet changes in insulin function is tolerated in some species. Taking advantage of the large number of publicly available mammalian genome sequences I identified insulin gene (Ins) in the genomes ...

Abstract	Disruption of insulin signaling in humans leads to diabetes yet changes in insulin function is tolerated in some species. Taking advantage of the large number of publicly available mammalian genome sequences I identified insulin gene (Ins) in the genomes of 151 of 156 mammalian species with well-annotated genomes, of which 141 had complete Ins coding sequences. Complete Ins coding sequences were identified from 8 additional species that lack complete genomes. Duplicated Ins genes were found in 12 rodents (9 with complete genomes) resulting in the identification of a total of 161 complete mammalian Ins coding sequences. While all 161 proinsulin protein sequences were predicted to have functional signal peptides, which should allow secretion of the hormone, unexpectedly, substitutions were found at prohormone convertase processing sites in sequences from 6 species, 2 from Chiroptera (Myotis brandtii and M. lucifugus) and 4 from Afrotheria (Chrysochloris asiatica, Echinops telfairi, Elephantulus edwardii, and Orycteropus afer). Both basic residues at the C-peptide-A-chain junction in the bats M. brandtii and M. lucifugas are replaced, which should prevent processing. Replacements of a single basic residue are found at the B-chain-C-peptide junction, in the two bats, and at the C-peptide-A-chain junction, in 4 species of Afrotheria, processing sites that suggest impaired processing. In addition, a large number of substitutions at sites that interact with the insulin receptor were found in the insulin sequences from M. brandtii and M. lucifugas suggesting a change in biological function.
MeSH term(s)	Amino Acid Sequence ; Animals ; Chiroptera/genetics ; Evolution, Molecular ; Genome/genetics ; Humans ; Insulin/genetics ; Mammals/genetics ; Phylogeny ; Proinsulin/genetics ; Protein Processing, Post-Translational ; Receptor, Insulin/genetics
Chemical Substances	Insulin ; Proinsulin (9035-68-1) ; Receptor, Insulin (EC 2.7.10.1)
Language	English
Publishing date	2020-11-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2020.170435
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Article ; Online: Viral Hormones: Do They Impact Human Endocrinology?

Irwin, David M

Endocrinology

2019 Volume 160, Issue 10, Page(s) 2326–2327

MeSH term(s)	Endocrinology ; Hormones ; Humans
Chemical Substances	Hormones
Language	English
Publishing date	2019-08-15
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	427856-2
ISSN	1945-7170 ; 0013-7227
ISSN (online)	1945-7170
ISSN	0013-7227
DOI	10.1210/en.2019-00541
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Article ; Online: Variation in the rates of evolution of the insulin and glucagon hormone and receptor genes in rodents.

Irwin, David M

Gene

2019 Volume 728, Page(s) 144296

Abstract: Insulin and glucagon are important hormones for regulating blood glucose levels. Rodents are useful models for understanding human physiology, however, differences exist between rodents and humans. Here I examined the evolution of the genes encoding ... ...

Abstract	Insulin and glucagon are important hormones for regulating blood glucose levels. Rodents are useful models for understanding human physiology, however, differences exist between rodents and humans. Here I examined the evolution of the genes encoding insulin (Ins) and glucagon (Gcg, which also encodes GLP-1 and GLP-2) and the receptors for these hormones (Insr, Gcgr, Glp1r, and Glp2r). Our results show that the insulin 1 gene (Ins1) that originated by retroposition in some rodents such as mice, experienced selective constraints that are as strong as those acting upon the Ins2 gene found in the locus-of-origin. Previous studies had shown that the insulin hormones and genes in hystricomorph rodents, such as the guinea pig, have altered function and selective constraints, respectively. Here I show that the insulin receptor genes in hystricomorph rodents also experienced changes in evolutionary rates, but that these changes did not alter sites involved in hormone binding. While glucagon, but not GLP-1 and GLP-2, in hystricomorph rodents also show increased rates of sequence evolution, no changes in the evolution of the glucagon receptor gene (Gcgr) was seen. Intriguingly, the GLP2 receptor gene (Glp2r) in mice-like rodents evolved more rapidly than those in hystricomorph rodents. When the rates of evolution of the genes encoding the receptors for proglucagon-derived peptides, which are all G-protein coupled receptors, were compared, the GLP-1 receptor gene (Glp1r) was found to display increased levels of sequence constraint compared to the Gcgr and Glp2r genes.
MeSH term(s)	Animals ; Evolution, Molecular ; Genome ; Glucagon/genetics ; Insulin/genetics ; Phylogeny ; Receptor, Insulin/genetics ; Receptors, Glucagon/genetics ; Rodentia/genetics
Chemical Substances	Insulin ; Receptors, Glucagon ; Glucagon (9007-92-5) ; Receptor, Insulin (EC 2.7.10.1)
Language	English
Publishing date	2019-12-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	391792-7
ISSN	1879-0038 ; 0378-1119
ISSN (online)	1879-0038
ISSN	0378-1119
DOI	10.1016/j.gene.2019.144296
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Article ; Online: Molecular evolution of GIP and Exendin and their receptors.

Irwin, David M

Peptides

2019 Volume 125, Page(s) 170158

Abstract: Glucose-dependent insulinotropic polypeptide (GIP) is a product of the Gip gene and acts as an incretin hormone in mammals. Gip is most closely related to the proglucagon (Gcg) and Exendin genes and diverged from these very early in vertebrate evolution. ...

Abstract	Glucose-dependent insulinotropic polypeptide (GIP) is a product of the Gip gene and acts as an incretin hormone in mammals. Gip is most closely related to the proglucagon (Gcg) and Exendin genes and diverged from these very early in vertebrate evolution. In mammals, GIP acts through its specific receptor, encoded by the Gipr gene, which belongs to a subfamily of 7-transmembrane G-protein coupled receptor (GPCR) genes that also includes those for the proglucagon-derived peptides (Gcgr, Glp1r, and Glp2r), and the receptor for Exendin (Grlr). Gip, Gipr, Exendin, and Grlr genes are found in species from most vertebrate classes. While most species that have a Gip gene also have a Gipr gene, two classes of vertebrates, cartilaginous fish and birds, retain conserved Gip genes but lack Gipr genes. This raises the possibility the GIP signals through other receptors in some vertebrates. Exendin genes and the gene for its receptor, Grlr, are also found in diverse vertebrates, with the notable exception of mammals. Both GIP and Exendin likely have important roles in vertebrate physiology, but their roles are either dispensable or can be replaced by other hormones.
MeSH term(s)	Animals ; Evolution, Molecular ; Gastric Inhibitory Polypeptide/genetics ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Phylogeny ; Receptors, Gastrointestinal Hormone/genetics
Chemical Substances	Intercellular Signaling Peptides and Proteins ; Receptors, Gastrointestinal Hormone ; exendin receptor ; Gastric Inhibitory Polypeptide (59392-49-3) ; helospectin I (93438-37-0) ; gastric inhibitory polypeptide receptor (D6H00MV7K8)
Language	English
Publishing date	2019-09-30
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2019.170158
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Article: Evolution of the mammalian insulin (Ins) gene; Changes in proteolytic processing

Irwin, David M

Peptides. 2021 Jan., v. 135

2021

Abstract	Disruption of insulin signaling in humans leads to diabetes yet changes in insulin function is tolerated in some species. Taking advantage of the large number of publicly available mammalian genome sequences I identified insulin gene (Ins) in the genomes of 151 of 156 mammalian species with well-annotated genomes, of which 141 had complete Ins coding sequences. Complete Ins coding sequences were identified from 8 additional species that lack complete genomes. Duplicated Ins genes were found in 12 rodents (9 with complete genomes) resulting in the identification of a total of 161 complete mammalian Ins coding sequences. While all 161 proinsulin protein sequences were predicted to have functional signal peptides, which should allow secretion of the hormone, unexpectedly, substitutions were found at prohormone convertase processing sites in sequences from 6 species, 2 from Chiroptera (Myotis brandtii and M. lucifugus) and 4 from Afrotheria (Chrysochloris asiatica, Echinops telfairi, Elephantulus edwardii, and Orycteropus afer). Both basic residues at the C-peptide-A-chain junction in the bats M. brandtii and M. lucifugas are replaced, which should prevent processing. Replacements of a single basic residue are found at the B-chain-C-peptide junction, in the two bats, and at the C-peptide-A-chain junction, in 4 species of Afrotheria, processing sites that suggest impaired processing. In addition, a large number of substitutions at sites that interact with the insulin receptor were found in the insulin sequences from M. brandtii and M. lucifugas suggesting a change in biological function.
Keywords	Echinops ; Elephantulus ; Orycteropus afer ; diabetes ; evolution ; genes ; insulin receptors ; peptides ; proinsulin ; proteolysis ; secretion ; signal peptide
Language	English
Dates of publication	2021-01
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	769028-9
ISSN	1873-5169 ; 0196-9781
ISSN (online)	1873-5169
ISSN	0196-9781
DOI	10.1016/j.peptides.2020.170435
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Article: Duplication and diversification of insulin genes in ray-finned fish.

Irwin, David M

Zoological research

2018 Volume 40, Issue 3, Page(s) 185–197

Abstract: Insulin is a key hormone for the regulation of metabolism in vertebrates. Insulin is produced by pancreatic islet cells in response to elevated glucose levels and leads to the uptake of glucose by tissues such as liver and adipose tissue to store energy. ...

Abstract	Insulin is a key hormone for the regulation of metabolism in vertebrates. Insulin is produced by pancreatic islet cells in response to elevated glucose levels and leads to the uptake of glucose by tissues such as liver and adipose tissue to store energy. Insulin also has additional functions in regulating development. Previous work has shown that the proglucagon gene, which encodes hormones counter regulating insulin, is duplicated in teleost fish, and that the peptide hormones encoded by these genes have diversified in function. I sought to determine whether similar processes have occurred to insulin genes in these species. Searches of fish genomes revealed an unexpected diversity of insulin genes. A triplication of the insulin gene occurred at the origin of teleost fish, however one of these three genes, insc, has been lost in most teleost fish lineages. The two other insulin genes, insa and insb, have been retained but show differing levels of selective constraint suggesting that they might have diversified in function. Intriguingly, a duplicate copy of the insa gene, which I named insab, is found in many fish. The coding sequence encoded by insab genes is under weak selective constraint, with its predicted protein sequences losing their potential to be processed into a two-peptide hormone. However, these sequences have retained perfectly conserved cystine residues, suggesting that they maintain insulin's three-dimensional structure and therefore might modulate the processing and secretion of insulin produced by the other genes.
MeSH term(s)	Adaptation, Physiological ; Animals ; Biological Evolution ; Fishes/genetics ; Gene Duplication ; Gene Expression Regulation/physiology ; Genetic Variation ; Insulin/genetics
Chemical Substances	Insulin
Language	English
Publishing date	2018-08-20
Publishing country	China
Document type	Journal Article
ISSN	2095-8137
ISSN	2095-8137
DOI	10.24272/j.issn.2095-8137.2018.052
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Article ; Online: Viral Insulin/IGF-1-Like Peptides: Novel Regulators of Physiology and Pathophysiology?

Irwin, David M

Endocrinology

2018 Volume 159, Issue 11, Page(s) 3659–3660

MeSH term(s)	Humans ; Insulin ; Insulin-Like Growth Factor I ; Peptides ; Receptor, IGF Type 1 ; Signal Transduction ; Somatomedins
Chemical Substances	Insulin ; Peptides ; Somatomedins ; Insulin-Like Growth Factor I (67763-96-6) ; Receptor, IGF Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2018-10-10
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	427856-2
ISSN	1945-7170 ; 0013-7227
ISSN (online)	1945-7170
ISSN	0013-7227
DOI	10.1210/en.2018-00856
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Article: Variation in the rates of evolution of the insulin and glucagon hormone and receptor genes in rodents

Irwin, David M

Gene. 2020 Feb. 20, v. 728

2020

Abstract	Insulin and glucagon are important hormones for regulating blood glucose levels. Rodents are useful models for understanding human physiology, however, differences exist between rodents and humans. Here I examined the evolution of the genes encoding insulin (Ins) and glucagon (Gcg, which also encodes GLP-1 and GLP-2) and the receptors for these hormones (Insr, Gcgr, Glp1r, and Glp2r). Our results show that the insulin 1 gene (Ins1) that originated by retroposition in some rodents such as mice, experienced selective constraints that are as strong as those acting upon the Ins2 gene found in the locus-of-origin. Previous studies had shown that the insulin hormones and genes in hystricomorph rodents, such as the guinea pig, have altered function and selective constraints, respectively. Here I show that the insulin receptor genes in hystricomorph rodents also experienced changes in evolutionary rates, but that these changes did not alter sites involved in hormone binding. While glucagon, but not GLP-1 and GLP-2, in hystricomorph rodents also show increased rates of sequence evolution, no changes in the evolution of the glucagon receptor gene (Gcgr) was seen. Intriguingly, the GLP2 receptor gene (Glp2r) in mice-like rodents evolved more rapidly than those in hystricomorph rodents. When the rates of evolution of the genes encoding the receptors for proglucagon-derived peptides, which are all G-protein coupled receptors, were compared, the GLP-1 receptor gene (Glp1r) was found to display increased levels of sequence constraint compared to the Gcgr and Glp2r genes.
Keywords	G-proteins ; blood glucose ; evolution ; genes ; glucagon ; glucagon receptors ; glucagon-like peptide 1 ; glucagon-like peptide 2 ; guinea pigs ; human physiology ; insulin ; insulin receptors
Language	English
Dates of publication	2020-0220
Publishing place	Elsevier B.V.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	391792-7
ISSN	1879-0038 ; 0378-1119
ISSN (online)	1879-0038
ISSN	0378-1119
DOI	10.1016/j.gene.2019.144296
Database	NAL-Catalogue (AGRICOLA)

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