Origin and diversification of the plasminogen activation system among chordates

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Origin and diversification of the plasminogen activation system among chordates. / Chana-Muñoz, Andrés; Jendroszek, Agnieszka; Sønnichsen, Malene; Wang, Tobias; Ploug, Michael; Jensen, Jan K.; Andreasen, Peter A.; Bendixen, Christian; Panitz, Frank.

In: BMC Evolutionary Biology, Vol. 19, No. 1, 27, 17.01.2019.

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Chana-Muñoz, Andrés ; Jendroszek, Agnieszka ; Sønnichsen, Malene ; Wang, Tobias ; Ploug, Michael ; Jensen, Jan K. ; Andreasen, Peter A. ; Bendixen, Christian ; Panitz, Frank. / Origin and diversification of the plasminogen activation system among chordates. In: BMC Evolutionary Biology. 2019 ; Vol. 19, No. 1.

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@article{9b1c50a02bc442d388bb403e247f38ac,
title = "Origin and diversification of the plasminogen activation system among chordates",
abstract = "Background: The plasminogen (PLG) activation system is composed by a series of serine proteases, inhibitors and several binding proteins, which together control the temporal and spatial generation of the active serine protease plasmin. As this proteolytic system plays a central role in human physiology and pathophysiology it has been extensively studied in mammals. The serine proteases of this system are believed to originate from an ancestral gene by gene duplications followed by domain gains and deletions. However, the identification of ancestral forms in primitive chordates supporting these theories remains elusive. In addition, evolutionary studies of the non-proteolytic members of this system are scarce. Results: Our phylogenetic analyses place lamprey PLG at the root of the vertebrate PLG-group, while lamprey PLG-related growth factors represent the ancestral forms of the jawed-vertebrate orthologues. Furthermore, we find that the earliest putative orthologue of the PLG activator group is the hyaluronan binding protein 2 (HABP2) gene found in lampreys. The prime plasminogen activators (tissue- and urokinase-type plasminogen activator, tPA and uPA) first occur in cartilaginous fish and phylogenetic analyses confirm that all orthologues identified compose monophyletic groups to their mammalian counterparts. Cartilaginous fishes exhibit the most ancient vitronectin of all vertebrates, while plasminogen activator inhibitor 1 (PAI-1) appears for the first time in cartilaginous fishes and is conserved in the rest of jawed vertebrate clades. PAI-2 appears for the first time in the common ancestor of reptiles and mammals, and represents the latest appearing plasminogen activator inhibitor. Finally, we noted that the urokinase-type plasminogen activator receptor (uPAR) - and three-LU domain containing genes in general - occurred later in evolution and was first detectable after coelacanths. Conclusions: This study identifies several primitive orthologues of the mammalian plasminogen activation system. These ancestral forms provide clues to the origin and diversification of this enzyme system. Further, the discovery of several members - hitherto unknown in mammals - provide new perspectives on the evolution of this important enzyme system.",
keywords = "Chordates, Evolution, Phylogenetic analysis, Plasminogen, Plasminogen activation system, Transcriptome analysis, Amino Acid Sequence, Humans, Phylogeny, Transcriptome/genetics, Genetic Variation, Likelihood Functions, Animals, Sequence Analysis, RNA, Databases, Protein, Plasminogen/genetics, Plasminogen Activator Inhibitor 1/chemistry, Protein Domains, Vitronectin/chemistry, Urokinase-Type Plasminogen Activator/chemistry, Chordata/genetics",
author = "Andr{\'e}s Chana-Mu{\~n}oz and Agnieszka Jendroszek and Malene S{\o}nnichsen and Tobias Wang and Michael Ploug and Jensen, {Jan K.} and Andreasen, {Peter A.} and Christian Bendixen and Frank Panitz",
year = "2019",
month = jan,
day = "17",
doi = "10.1186/s12862-019-1353-z",
language = "English",
volume = "19",
journal = "B M C Evolutionary Biology",
issn = "1471-2148",
publisher = "BioMed Central Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Origin and diversification of the plasminogen activation system among chordates

AU - Chana-Muñoz, Andrés

AU - Jendroszek, Agnieszka

AU - Sønnichsen, Malene

AU - Wang, Tobias

AU - Ploug, Michael

AU - Jensen, Jan K.

AU - Andreasen, Peter A.

AU - Bendixen, Christian

AU - Panitz, Frank

PY - 2019/1/17

Y1 - 2019/1/17

N2 - Background: The plasminogen (PLG) activation system is composed by a series of serine proteases, inhibitors and several binding proteins, which together control the temporal and spatial generation of the active serine protease plasmin. As this proteolytic system plays a central role in human physiology and pathophysiology it has been extensively studied in mammals. The serine proteases of this system are believed to originate from an ancestral gene by gene duplications followed by domain gains and deletions. However, the identification of ancestral forms in primitive chordates supporting these theories remains elusive. In addition, evolutionary studies of the non-proteolytic members of this system are scarce. Results: Our phylogenetic analyses place lamprey PLG at the root of the vertebrate PLG-group, while lamprey PLG-related growth factors represent the ancestral forms of the jawed-vertebrate orthologues. Furthermore, we find that the earliest putative orthologue of the PLG activator group is the hyaluronan binding protein 2 (HABP2) gene found in lampreys. The prime plasminogen activators (tissue- and urokinase-type plasminogen activator, tPA and uPA) first occur in cartilaginous fish and phylogenetic analyses confirm that all orthologues identified compose monophyletic groups to their mammalian counterparts. Cartilaginous fishes exhibit the most ancient vitronectin of all vertebrates, while plasminogen activator inhibitor 1 (PAI-1) appears for the first time in cartilaginous fishes and is conserved in the rest of jawed vertebrate clades. PAI-2 appears for the first time in the common ancestor of reptiles and mammals, and represents the latest appearing plasminogen activator inhibitor. Finally, we noted that the urokinase-type plasminogen activator receptor (uPAR) - and three-LU domain containing genes in general - occurred later in evolution and was first detectable after coelacanths. Conclusions: This study identifies several primitive orthologues of the mammalian plasminogen activation system. These ancestral forms provide clues to the origin and diversification of this enzyme system. Further, the discovery of several members - hitherto unknown in mammals - provide new perspectives on the evolution of this important enzyme system.

AB - Background: The plasminogen (PLG) activation system is composed by a series of serine proteases, inhibitors and several binding proteins, which together control the temporal and spatial generation of the active serine protease plasmin. As this proteolytic system plays a central role in human physiology and pathophysiology it has been extensively studied in mammals. The serine proteases of this system are believed to originate from an ancestral gene by gene duplications followed by domain gains and deletions. However, the identification of ancestral forms in primitive chordates supporting these theories remains elusive. In addition, evolutionary studies of the non-proteolytic members of this system are scarce. Results: Our phylogenetic analyses place lamprey PLG at the root of the vertebrate PLG-group, while lamprey PLG-related growth factors represent the ancestral forms of the jawed-vertebrate orthologues. Furthermore, we find that the earliest putative orthologue of the PLG activator group is the hyaluronan binding protein 2 (HABP2) gene found in lampreys. The prime plasminogen activators (tissue- and urokinase-type plasminogen activator, tPA and uPA) first occur in cartilaginous fish and phylogenetic analyses confirm that all orthologues identified compose monophyletic groups to their mammalian counterparts. Cartilaginous fishes exhibit the most ancient vitronectin of all vertebrates, while plasminogen activator inhibitor 1 (PAI-1) appears for the first time in cartilaginous fishes and is conserved in the rest of jawed vertebrate clades. PAI-2 appears for the first time in the common ancestor of reptiles and mammals, and represents the latest appearing plasminogen activator inhibitor. Finally, we noted that the urokinase-type plasminogen activator receptor (uPAR) - and three-LU domain containing genes in general - occurred later in evolution and was first detectable after coelacanths. Conclusions: This study identifies several primitive orthologues of the mammalian plasminogen activation system. These ancestral forms provide clues to the origin and diversification of this enzyme system. Further, the discovery of several members - hitherto unknown in mammals - provide new perspectives on the evolution of this important enzyme system.

KW - Chordates

KW - Evolution

KW - Phylogenetic analysis

KW - Plasminogen

KW - Plasminogen activation system

KW - Transcriptome analysis

KW - Amino Acid Sequence

KW - Humans

KW - Phylogeny

KW - Transcriptome/genetics

KW - Genetic Variation

KW - Likelihood Functions

KW - Animals

KW - Sequence Analysis, RNA

KW - Databases, Protein

KW - Plasminogen/genetics

KW - Plasminogen Activator Inhibitor 1/chemistry

KW - Protein Domains

KW - Vitronectin/chemistry

KW - Urokinase-Type Plasminogen Activator/chemistry

KW - Chordata/genetics

UR - http://www.scopus.com/inward/record.url?scp=85060084730&partnerID=8YFLogxK

U2 - 10.1186/s12862-019-1353-z

DO - 10.1186/s12862-019-1353-z

M3 - Journal article

C2 - 30654737

AN - SCOPUS:85060084730

VL - 19

JO - B M C Evolutionary Biology

JF - B M C Evolutionary Biology

SN - 1471-2148

IS - 1

M1 - 27

ER -