Evolution of tissue-specific keratins as deduced from novel cDNA sequences of the lungfish Protopterus aethiopicus.
ABSTRACT Lungfishes are possibly the closest extant relatives of the land vertebrates (tetrapods). We report here the cDNA and predicted amino acid sequences of 13 different keratins (ten type I and three type II) of the lungfish Protopterus aethiopicus. These keratins include the orthologs of human K8 and K18. The lungfish keratins were also identified in tissue extracts using two-dimensional polyacrylamide gel electrophoresis, keratin blot binding assays and immunoblotting. The identified keratin spots were analyzed by peptide mass fingerprinting which assigned seven sequences (inclusively Protopterus K8 and K18) to their respective protein spot. The peptide mass fingerprints also revealed the fact that the major epidermal type I and type II keratins of this lungfish have not yet been sequenced. Nevertheless, phylogenetic trees constructed from multiple sequence alignments of keratins from lungfish and distantly related vertebrates such as lamprey, shark, trout, frog, and human reveal new insights into the evolution of K8 and K18, and unravel a variety of independent keratin radiation events.
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ABSTRACT: This study was undertaken to identify the normal morphologic, immunohistochemical and ultrastructural features of skin of the turbot (Psetta maxima L.). In the turbot skin, three morphologically distinct layers were identified: epidermis, dermis and hypodermis. The epidermis was non-keratinizing, stratified squamous epithelium that varies in thickness from 5 to 14 cells and 60 to 100 μm in size. Goblet cells were seen randomly distributed between malpighian cells in the epidermal layer. These mucous cells were mainly located in the upper third of the epidermis and displayed a spherical to elongated morphology. Dermis was divided in two well-differentiated layers, the superficial stratum laxum and the deeper stratum compactum. Hypodermis was a loose layer mainly composed by adipocytes but we could observe variable amounts of fibroblast, collagen and blood vessels. In turbot two pigmentary layers could be identified: the pigmentary layer of dermis was located between basement membrane and dermis and the pigmentary layer of hypodermis immediately above the muscular layer. Three different types of chromatophores were present: melanophores, iridophores and xanthophores. The main differences observed between groups of fish with different coloration were in the amount of melanophores and xanthophores. The purpose of this article is to provide an overview of normal cutaneous biology prior to consideration of specific cutaneous alterations and diseases in turbot.Tissue and Cell 10/2014; 46(5). DOI:10.1016/j.tice.2014.06.004 · 1.05 Impact Factor
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ABSTRACT: Intermediate filament (IF) proteins, together with tubulins and actins, constitute the majority of cytoskeletal proteins in metazoans. Proteins of the IF family fulfil increasingly diverse functions but share common structural features. Phylogenetic analysis within the metazoan lineage traces back their origin to a common lamin-like ancestor. Major steps in lamin evolution occurred at the base of the vertebrate radiation, while cytoplasmic IF protein subfamilies evolved independently in the major metazoan lineages. Copyright © 2014 Elsevier Ltd. All rights reserved.Current Opinion in Cell Biology 01/2015; 32C:48-55. DOI:10.1016/j.ceb.2014.12.009 · 8.74 Impact Factor
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ABSTRACT: We have examined cytokeratin distribution and their nature in toe pads of the Himalayan tree-frog Philautus annandalii. Toe pads are expanded tips of digits and show modifications of their ventral epidermis for adhesion. The toe pad epidermal cells, being organized into 3-4 rows, possess keratin bundles, especially in surface nanostructures that are involved in adhesion. Immunohistochemical localization using a pan-cytokeratin antibody revealed that cytokeratin immunoreactivity is the strongest in the mid- to basal cell rows of the epidermis, which parallels our previous ultrastructural observation of dense keratin bundles present in this part of the epidermis. The remainder of the epidermis (i.e., the superficial cell layer) showed little immunoreactivity. Immunoblot analysis revealed that toe-pads possessed keratins prominently in the molecular mass of 50kDa. Possible presence of keratin 5 in toe pad epidermis has been correlated with its usual distribution pattern in mammalian epidermis.Tissue and Cell 03/2014; DOI:10.1016/j.tice.2014.03.001 · 1.05 Impact Factor