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1.
Mol Phylogenet Evol ; 114: 261-270, 2017 09.
Article in English | MEDLINE | ID: mdl-28684366

ABSTRACT

Ecological niche models (ENMs) have been used in a wide range of ecological and evolutionary studies. In biogeographic studies these models have, among other things, helped in the discovery of new allopatric populations, and even new species. However, small sample sizes and questionable taxonomic delimitation can challenge models, often decreasing their accuracy. Herein we examine the sensitivity of ENMs to the addition of new, geographically isolated populations, and the impact of applying different taxonomic delimitations. The East African reed frog Hyperolius substriatus Ahl, 1931 was selected as a case study because it has been the subject of previous ENM predictions. Our results suggest that addition of new data and reanalysis of species lineages of H. substriatus improved our understanding of the evolutionary history of this group of frogs. ENMs provided robust predictions, even when some populations were deliberately excluded from the models. Splitting the lineages based on genetic relationships and analysing the ENMs separately provided insights about the biogeographical processes that led to the current distribution of H. substriatus.


Subject(s)
Anura/classification , Africa, Eastern , Animals , Anura/genetics , Biological Evolution , DNA/chemistry , DNA/isolation & purification , DNA/metabolism , Ecology , Gene Flow , Genetic Linkage , Phylogeny , Phylogeography , Proprotein Convertases/classification , Proprotein Convertases/genetics , Proto-Oncogene Proteins c-myc/classification , Proto-Oncogene Proteins c-myc/genetics , RNA, Ribosomal, 16S/classification , RNA, Ribosomal, 16S/genetics , Sequence Analysis, DNA
2.
Methods Mol Biol ; 768: 23-57, 2011.
Article in English | MEDLINE | ID: mdl-21805237

ABSTRACT

The proprotein convertases (PCs) are secretory mammalian serine proteinases related to bacterial subtilisin-like enzymes. The family of PCs comprises nine members, PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9 (Fig. 3.1). While the first seven PCs cleave after single or paired basic residues, the last two cleave at non-basic residues and the last one PCSK9 only cleaves one substrate, itself, for its activation. The targets and substrates of these convertases are very varied covering many aspects of cellular biology and communication. While it took more than 22 years to begin to identify the first member in 1989-1990, in less than 14 years they were all characterized. So where are we 20 years later in 2011? We have now reached a level of maturity needed to begin to unravel the mechanisms behind the complex physiological functions of these PCs both in health and disease states. We are still far away from comprehensively understanding the various ramifications of their roles and to identify their physiological substrates unequivocally. How do these enzymes function in vivo? Are there other partners to be identified that would modulate their activity and/or cellular localization? Would non-toxic inhibitors/silencers of some PCs provide alternative therapies to control some pathologies and improve human health? Are there human SNPs or mutations in these PCs that correlate with disease, and can these help define the finesses of their functions and/or cellular sorting? The more we know about a given field, the more questions will arise, until we are convinced that we have cornered the important angles. And yet the future may well reserve for us many surprises that may allow new leaps in our understanding of the fascinating biology of these phylogenetically ancient eukaryotic proteases (Fig. 3.2) implicated in health and disease, which traffic through the cells via multiple sorting pathways (Fig. 3.3).


Subject(s)
Proprotein Convertases , Amino Acid Sequence , Animals , Dyslipidemias/enzymology , Endocrine System Diseases/enzymology , History, 20th Century , History, 21st Century , Humans , Mice , Mice, Knockout , Neoplasms/enzymology , Proprotein Convertase 9 , Proprotein Convertases/chemistry , Proprotein Convertases/classification , Proprotein Convertases/history , Proprotein Convertases/metabolism , Protease Inhibitors , Rats , Saccharomyces cerevisiae/enzymology , Sequence Homology , Serine Endopeptidases/metabolism , Substrate Specificity/physiology , Virus Diseases/enzymology
3.
Int J Biol Sci ; 2(3): 125-32, 2006.
Article in English | MEDLINE | ID: mdl-16763672

ABSTRACT

The proprotein convertases (PCs) comprise a family of subtilisin-like endoproteases that activate precursor proteins (including, prohormones, growth factors, and adhesion molecules) during their transit through secretory pathways or at the cell surface. To explore the evolution of the PC gene family in chordates, we made a phylogenetic analysis of PC genes found in databases, with special attention to three PC genes of the cephalochordate amphioxus, the closest living invertebrate relative to the vertebrates. Since some vertebrate PC genes are essential for early development, we investigated the expression pattern of the C isoform of the amphioxus PC6 gene (aPC6C). In amphioxus embryos and larvae, aPC6C is expressed at places where epithelia fuse. Several kinds of fusions occur: ectoderm-to-ectoderm during neurulation; mesoderm-to-ectoderm during formation of the preoral ciliated pit; and endoderm-to-ectoderm during formation of the mouth, pharyngeal slits, anus, and external opening of the club-shaped gland. Presumably, at all these sites, aPC6C is activating proteins favoring association between previously disjunct cell populations.


Subject(s)
Chordata/embryology , Chordata/metabolism , Phylogeny , Proprotein Convertases/genetics , Animals , Epithelium/embryology , Epithelium/metabolism , In Situ Hybridization , Proprotein Convertases/classification
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