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Pesquisa : D05.750.078.593.450.074 [Categoria DeCS]
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  1 / 68 MEDLINE  
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[PMID]:28101864
[Au] Autor:Fraser RD; Parry DA
[Ad] Endereço:Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, 4442, New Zealand.
[Ti] Título:Filamentous Structure of Hard ß-Keratins in the Epidermal Appendages of Birds and Reptiles.
[So] Source:Subcell Biochem;82:231-252, 2017.
[Is] ISSN:0306-0225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The structures of avian and reptilian epidermal appendages, such as feathers, claws and scales, have been modelled using X-ray diffraction and electron microscopy data, combined with sequence analyses. In most cases, a family of closely related molecules makes up the bulk of the appendage, and each of these molecules contains a central ß-rich 34-residue segment, which has been identified as the principal component of the framework of the 3.4 nm diameter filaments. The N- and C-terminal segments form the matrix component of the filament/matrix complex. The 34-residue ß-rich central domains occur in pairs, related by either a parallel dyad or a perpendicular dyad axis, and form a ß-sandwich stabilized by apolar interactions. They are also twisted in a right-handed manner. In feather, the filaments are packed into small sheets and it is possible to determine their likely orientation within the sheets from the low-angle X-ray diffraction data. The physical properties of the various epidermal appendages can be related to the amino acid sequence and composition of defined molecular segments characteristic of the chains concerned.
[Mh] Termos MeSH primário: Aves
Epiderme/química
Répteis
beta-Queratinas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Epiderme/ultraestrutura
Plumas/química
Plumas/ultraestrutura
Casco e Garras/química
Casco e Garras/ultraestrutura
Conformação Proteica
Homologia de Sequência de Aminoácidos
Difração de Raios X
beta-Queratinas/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (beta-Keratins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-49674-0_8


  2 / 68 MEDLINE  
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[PMID]:27506161
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Department of Bigea, University of Bologna, Italy. lorenzo.alibardi@unibo.it.
[Ti] Título:Sauropsids Cornification is Based on Corneous Beta-Proteins, a Special Type of Keratin-Associated Corneous Proteins of the Epidermis.
[So] Source:J Exp Zool B Mol Dev Evol;326(6):338-351, 2016 Sep.
[Is] ISSN:1552-5015
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The evolution of the process of cornification in amniote epidermis from the general process of keratinization present in simple epithelia of anamniotes took place through the evolution of specialized intermediate filament (α) keratins, keratin-associated proteins (KAPs) and corneous proteins (CPs). The scanty information on the three-dimensional conformation of known KAPs and CPs indicate these proteins contain α-helix, random coiled, or beta sheets with different lengths and organizations. CP genes originated in a chromosome locus indicated as epidermal differentiation complex (EDC), and transformed the epidermal keratinization of anamniotes into the cornified epidermis and skin appendages of amniotes (claws, beaks, and feathers). In particular, peculiar genes encoding for small proteins with a central region of 34 amino acids conformed as beta sheets were originated in the EDC of sauropsids (reptiles and birds). These proteins were traditionally indicated as beta-keratins because they form filaments of 3-4 nm in diameter and show an X-ray beta pattern. Different from other proteins of the EDC, dimers of these corneous beta-proteins associate into long polymers of filamentous proteins utilized in sauropsids skin appendages, such as scales and feathers. Future challenges in this area of research will be the study on gene regulation and expression for these proteins, their origin and evolution in different lineages of sauropsids, and their role in determining the material properties of sauropsid scales and other skin appendages.
[Mh] Termos MeSH primário: Aves/metabolismo
Epiderme/metabolismo
Répteis/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas Aviárias/metabolismo
Evolução Biológica
Aves/anatomia & histologia
Epiderme/anatomia & histologia
Tegumento Comum
Queratinas/metabolismo
Répteis/anatomia & histologia
Proteínas de Répteis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Reptilian Proteins); 0 (beta-Keratins); 68238-35-7 (Keratins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160811
[St] Status:MEDLINE
[do] DOI:10.1002/jez.b.22689


  3 / 68 MEDLINE  
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[PMID]:27501942
[Au] Autor:Bhattacharjee MJ; Yu CP; Lin JJ; Ng CS; Wang TY; Lin HH; Li WH
[Ad] Endereço:Biodiversity Research Center, Academia Sinica, Taipei, Taiwan.
[Ti] Título:Regulatory Divergence among Beta-Keratin Genes during Bird Evolution.
[So] Source:Mol Biol Evol;33(11):2769-2780, 2016 Nov.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Feathers, which are mainly composed of α- and ß-keratins, are highly diversified, largely owing to duplication and diversification of ß-keratin genes during bird evolution. However, little is known about the regulatory changes that contributed to the expressional diversification of ß-keratin genes. To address this issue, we studied transcriptomes from five different parts of chicken contour and flight feathers. From these transcriptomes we inferred ß-keratin enriched co-expression modules of genes and predicted transcription factors (TFs) of ß-keratin genes. In total, we predicted 262 TF-target gene relationships in which 56 TFs regulate 91 ß-keratin genes; we validated 14 of them by in vitro tests. A dual criterion of TF enrichment and "TF-target gene" expression correlation identified 26 TFs as the major regulators of ß-keratin genes. According to our predictions, the ancestral scale and claw ß-keratin genes have common and unique regulators, whereas most feather ß-keratin genes show chromosome-wise regulation, distinct from scale and claw ß-keratin genes. Thus, after expansion from the ß-keratin gene on Chr7 to other chromosomes, which still shares a TF with scale and claw ß-keratin genes, most feather ß-keratin genes have recruited distinct or chromosome-specific regulators. Moreover, our data showed correlated gene expression profiles, positive or negative, between predicted TFs and their target genes over the five studied feather regions. Therefore, regulatory divergences among feather ß-keratin genes have contributed to structural differences among different parts of feathers. Our study sheds light on how feather ß-keratin genes have diverged in regulation from scale and claw ß-keratin genes and among themselves.
[Mh] Termos MeSH primário: Galinhas/genética
Plumas/fisiologia
Regulação da Expressão Gênica/genética
beta-Queratinas/genética
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Evolução Molecular
Plumas/metabolismo
Variação Genética
Família Multigênica
Análise de Sequência de DNA/métodos
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Transcriptoma
beta-Queratinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transcription Factors); 0 (beta-Keratins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE


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[PMID]:26597267
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Department of Biology, Geology and Environmental Sciences, University of Bologna, via Selmi 3, 40126, Bologna, Italy. lorenzo.alibardi@unibo.it.
[Ti] Título:Review: mapping epidermal beta-protein distribution in the lizard Anolis carolinensis shows a specific localization for the formation of scales, pads, and claws.
[So] Source:Protoplasma;253(6):1405-1420, 2016 Nov.
[Is] ISSN:1615-6102
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The epidermis of lizards is made of multiple alpha- and beta-layers with different characteristics comprising alpha-keratins and corneous beta-proteins (formerly beta-keratins). Three main modifications of body scales are present in the lizard Anolis carolinensis: gular scales, adhesive pad lamellae, and claws. The 40 corneous beta-proteins present in this specie comprise glycine-rich and glycine-cysteine-rich subfamilies, while the 41 alpha-keratins comprise cysteine-poor and cysteine-rich subfamilies, the latter showing homology to hair keratins. Other genes for corneous proteins are present in the epidermal differentiation complex, the locus where corneous protein genes are located. The review summarizes the main sites of immunolocalization of beta-proteins in different scales and their derivatives producing a unique map of body distribution for these structural proteins. Small glycine-rich beta-proteins participate in the formation of the mechanically resistant beta-layer of most scales. Small glycine-cysteine beta-proteins have a more varied localization in different scales and are also present in the pliable alpha-layer. In claws, cysteine-rich alpha-keratins prevail over cysteine-poor alpha-keratins and mix to glycine-cysteine-rich beta-proteins. The larger beta-proteins with a molecular mass similar to that of alpha-keratins participate in the formation of the fibrous meshwork present in differentiating beta-cells and likely interact with alpha-keratins. The diverse localization of alpha-keratins, beta-proteins, and other proteins of the epidermal differentiation complex gives rise to variably pliable, elastic, or hard corneous layers in different body scales. The corneous layers formed in the softer or harder scales, in the elastic pad lamellae, or in the resistant claws possess peculiar properties depending on the ratio of specific corneous proteins.
[Mh] Termos MeSH primário: Estruturas Animais/metabolismo
Epiderme/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Epiderme/ultraestrutura
Lagartos
Transporte Proteico
Proteoma/metabolismo
beta-Queratinas/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteome); 0 (beta-Keratins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE


  5 / 68 MEDLINE  
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[PMID]:26598683
[Au] Autor:Wu P; Ng CS; Yan J; Lai YC; Chen CK; Lai YT; Wu SM; Chen JJ; Luo W; Widelitz RB; Li WH; Chuong CM
[Ad] Endereço:Department of Pathology, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033;
[Ti] Título:Topographical mapping of α- and ß-keratins on developing chicken skin integuments: Functional interaction and evolutionary perspectives.
[So] Source:Proc Natl Acad Sci U S A;112(49):E6770-9, 2015 Dec 08.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Avian integumentary organs include feathers, scales, claws, and beaks. They cover the body surface and play various functions to help adapt birds to diverse environments. These keratinized structures are mainly composed of corneous materials made of α-keratins, which exist in all vertebrates, and ß-keratins, which only exist in birds and reptiles. Here, members of the keratin gene families were used to study how gene family evolution contributes to novelty and adaptation, focusing on tissue morphogenesis. Using chicken as a model, we applied RNA-seq and in situ hybridization to map α- and ß-keratin genes in various skin appendages at embryonic developmental stages. The data demonstrate that temporal and spatial α- and ß-keratin expression is involved in establishing the diversity of skin appendage phenotypes. Embryonic feathers express a higher proportion of ß-keratin genes than other skin regions. In feather filament morphogenesis, ß-keratins show intricate complexity in diverse substructures of feather branches. To explore functional interactions, we used a retrovirus transgenic system to ectopically express mutant α- or antisense ß-keratin forms. α- and ß-keratins show mutual dependence and mutations in either keratin type results in disrupted keratin networks and failure to form proper feather branches. Our data suggest that combinations of α- and ß-keratin genes contribute to the morphological and structural diversity of different avian skin appendages, with feather-ß-keratins conferring more possible composites in building intrafeather architecture complexity, setting up a platform of morphological evolution of functional forms in feathers.
[Mh] Termos MeSH primário: Evolução Biológica
Mapeamento Cromossômico
Queratinas/genética
Pele/embriologia
beta-Queratinas/genética
[Mh] Termos MeSH secundário: Animais
Embrião de Galinha
Hibridização In Situ
Queratina-13/genética
RNA Antissenso/farmacologia
Pele/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (KRT13 protein, human); 0 (Keratin-13); 0 (RNA, Antisense); 0 (beta-Keratins); 68238-35-7 (Keratins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151125
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1520566112


  6 / 68 MEDLINE  
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[PMID]:26220876
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Department of Bigea, University of Bologna, Bologna, Italy.
[Ti] Título:Immunolocalization of large corneous beta-proteins in the green anole lizard (Anolis carolinensis) suggests that they form filaments that associate to the smaller beta-proteins in the beta-layer of the epidermis.
[So] Source:J Morphol;276(10):1244-57, 2015 Oct.
[Is] ISSN:1097-4687
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The distribution of large corneous beta-proteins of 18-43 kDa (Ac37, 39, and 40) in the epidermis of the lizard Anolis carolinensis is unknown. This study analyses the localization of these beta-proteins in different body scales during regeneration. Western blot analysis indicates most protein bands at 40-50 kDa suggesting they mix with alpha-keratin of intermediate filament keratin proteins. Ac37 is present in mature alpha-layers of most scales and in beta-cells of the outer scale surface in some scales but is absent in the Oberhäutchen, in the setae and beta-layer of adhesive pads and in mesos cells. In differentiating beta-keratinocytes Ac37 is present over 3-4 nm thick filaments located around the amorphous beta-packets and in alpha-cells, but is scarce in precorneous and corneous layers of the claw. Ac37 forms long filaments and, therefore, resembles alpha-keratins to which it probably associates. Ac39 is seen in the beta-layer of tail and digital scales, in beta-cells of regenerating scales but not in the Oberhäutchen (and adhesive setae) or in beta- and alpha-layers of the other scales. Ac40 is present in the mature beta-layer of most scales and dewlap, in differentiating beta-cells of regenerating scales, but is absent in all the other epidermal layers. The large beta-proteins are accumulated among forming beta-packets of beta-cells and are packed in the beta-corneous material of mature beta-layer. Together alpha-keratins, large beta-proteins form the denser areas of mature beta-layer that may have a different consistence that the electron-paler areas.
[Mh] Termos MeSH primário: Citoesqueleto/metabolismo
Epiderme/metabolismo
Lagartos/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Epiderme/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (beta-Keratins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150910
[Lr] Data última revisão:
150910
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150730
[St] Status:MEDLINE
[do] DOI:10.1002/jmor.20415


  7 / 68 MEDLINE  
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[PMID]:26134080
[Au] Autor:Liu ZQ; Jiao D; Zhang ZF
[Ad] Endereço:Shenyang National Laboratory for Materials Science, Institute of Metal Research, Chinese Academy of Sciences, Shenyang 110016, China. Electronic address: liuzq@imr.ac.cn.
[Ti] Título:Remarkable shape memory effect of a natural biopolymer in aqueous environment.
[So] Source:Biomaterials;65:13-21, 2015 Oct.
[Is] ISSN:1878-5905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Remarkable water-stimulated shape memory effect was revealed in a natural biopolymer of peacock's tail covert feathers of which the innate shape can almost be fully recovered after severe deformation by a short hydration step. The shape memory effect manifests a good stability of high recovery rate and ratio during cycles of deformation and subsequent recovery. Both strength and energy absorption efficiency of medullary foam can be recovered despite the apparent decrease in the first deformation stroke caused by structural damage. A kinetic model developed from non-equilibrium thermodynamic fluctuation theory was adopted to describe the shape recovery process by considering the viscoelastic relaxation. The effects of hydration on mechanical properties, recovery kinetics, activation process and dynamic mechanical behaviors were also evaluated. Mechanisms were explored based on the lubrication, swelling effect and structural changes of macromolecular chains or segments in terms of their mobility. This study is expected to aid in understanding the responses of natural biological materials to environmental stimuli and to provide useful information for synthetic shape memory materials from the bio-inspiration perspective.
[Mh] Termos MeSH primário: Proteínas Aviárias/química
Plumas/química
Galliformes
Substâncias Viscoelásticas/química
Água/química
beta-Queratinas/química
[Mh] Termos MeSH secundário: Animais
Materiais Biomiméticos/química
Biopolímeros/química
Plumas/anatomia & histologia
Galliformes/anatomia & histologia
Cinética
Estresse Mecânico
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Biopolymers); 0 (Viscoelastic Substances); 0 (beta-Keratins); 059QF0KO0R (Water)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150720
[Lr] Data última revisão:
150720
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150703
[St] Status:MEDLINE


  8 / 68 MEDLINE  
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[PMID]:25740419
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Department of Bigea, University of Bologna, Bologna, Italy. lorenzo.alibardi@unibo.it.
[Ti] Título:Immunolocalization of sulfhydryl oxidase in reptilian epidermis indicates that the enzyme participates mainly to the hardening process of the beta-corneous layer.
[So] Source:Protoplasma;252(6):1529-36, 2015 Nov.
[Is] ISSN:1615-6102
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Reptilian skin is tough and scaled representing an evolutionary adaptation to the terrestrial environment. The presence of sulfhydryl oxidase during the process of hardening of the corneous layer in reptilian epidermis has been analyzed by immunocytochemistry and immunoblotting. Sulfhydryl oxidase-like immunoreactivity of proteins in the 50-65 kDa range of molecular weight is mainly observed in the transitional and pre-corneous layers of crocodilians, chelonian, and in the forming beta-layer of lepidosaurians. The ultrastructural localization of the enzyme by immunogold in lizard epidermis during renewal and resting stages shows that the labeling is mainly distributed in the cytoplasm and along the accumulating beta-packets of differentiating beta-cells while it appears very low to undetectable in differentiating alpha-cells of the lacunar, clear, mesos, and alpha-layers. The labeling however becomes absent or undetectable also in the fully mature beta-layer. The study shows that an oxidative enzyme is likely responsible of the cross-linking of the numerous cysteines present in the main proteins accumulated in corneocytes of reptilian epidermis, known as corneous beta-proteins (beta-keratins). This process of disulphide bond formation is probably largely responsible for the formation of hard beta-corneous layers in reptilian scales, a difference with alpha-corneous layers where substrate proteins of transglutaminase appear predominant.
[Mh] Termos MeSH primário: Epiderme/enzimologia
Imuno-Histoquímica
Lagartos/metabolismo
Oxirredutases/metabolismo
Proteínas de Répteis/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Cisteína
Epiderme/ultraestrutura
Dureza
Microscopia Eletrônica de Transmissão
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Reptilian Proteins); 0 (beta-Keratins); EC 1.- (Oxidoreductases); EC 1.8.3.- (sulfhydryl oxidase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150306
[St] Status:MEDLINE
[do] DOI:10.1007/s00709-015-0782-9


  9 / 68 MEDLINE  
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[PMID]:26154324
[Au] Autor:Alibardi L
[Ad] Endereço:Comparative Histolab and Dipartimento Bigea, University of Bologna, Italy. lorenzo.alibardi@unibo.it.
[Ti] Título:Transition from embryonic to adult epidermis in reptiles occurs by the production of corneous beta-proteins.
[So] Source:Int J Dev Biol;58(10-12):829-39, 2014.
[Is] ISSN:1696-3547
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:The adaptation of the epidermis in amniote vertebrates to life on land took place by a drastic change from an embryonic epidermis made of two-four periderm layers to a terrestrial-proof epidermis. This transition occurred by the increase in types and number of specialized corneous proteins coded by genes of the Epidermal Differentiation Complex. The prevalent types of corneous proteins produced in the reptilian epidermis contain a beta-sheet region of high amino acid homology which allows their polymerization into a meshwork of filaments forming the hard corneous material of scales and claws. The present immunogold ultrastructural study shows that this transition occurs with the synthesis of glycine-rich corneous beta-proteins (formerly indicated as beta-keratins) that are added to the initial framework of acidic intermediate filaments produced in the embryonic epidermis of lizards, snake, alligator and turtle. These corneous beta-proteins are accumulated in the transitional and definitive layers of reptilian epidermis formed underneath the transitory two-four layered embryonic epidermis. In the more specialized reptiles capable of shedding the epidermis as a single unit, such as lizards and snakes, special glycine-cysteine rich beta-proteins are initially produced in a single layer immediately formed beneath the embryonic epidermis, the oberhautchen. The latter layer allows the in ovo shedding of the embryonic epidermis in preparation for hatching, and in the following shedding cycles of the adult epidermis. The production of specialized corneous-specific beta-proteins in addition to intermediate filament keratins was probably an essential addition for terrestrial life during the evolution of reptiles into different lineages, including birds. The increase of glycine and cysteine in epidermal proteins enhanced the hydrophobicity, insolubility and mechanical strength of the stratum corneum in these amniotes.
[Mh] Termos MeSH primário: Epiderme/embriologia
Queratinas Tipo I/metabolismo
Répteis/embriologia
Proteínas de Répteis/genética
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Evolução Biológica
Diferenciação Celular/genética
Embrião não Mamífero/embriologia
Epiderme/crescimento & desenvolvimento
Interações Hidrofóbicas e Hidrofílicas
Proteínas de Répteis/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Keratins, Type I); 0 (Reptilian Proteins); 0 (beta-Keratins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150709
[Lr] Data última revisão:
150709
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150709
[St] Status:MEDLINE
[do] DOI:10.1387/ijdb.140325la


  10 / 68 MEDLINE  
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[PMID]:25941724
[Au] Autor:Bidzhieva SKh; Derbikova KS; Kublanov IV; Bonch-Osmolovskaya EA
[Ti] Título:[Capacity of hyperthermophilic Crenarchaeota for decomposition of refractory protiens (α- and ß-keratins)].
[So] Source:Mikrobiologiia;83(6):743-51, 2014 Nov-Dec.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Anaerobic thermophilic archaea of the genera Thermogladius and Desulfurococcus capable of a- and P3-keratin decomposition were isolated from hot springs of Kamchatka and Kunashir Island. For two of them (strains 2355k and 3008g), the presence of high-molecular mass, cell-bound endopeptidases active against nonhydrolyzed and partially hydrolyzed proteins at high values of temperature and pH was shown. Capacity for ß-keratin decomposition was also found in collection strains (type strains of Desulfurococcus amylolyticus subsp. amylolyticus, D. mucosus subsp. mobilis, and D. fermentans).
[Mh] Termos MeSH primário: Crenarchaeota/metabolismo
Queratinas/metabolismo
beta-Queratinas/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Crenarchaeota/crescimento & desenvolvimento
Crenarchaeota/isolamento & purificação
Desulfurococcaceae/isolamento & purificação
Desulfurococcaceae/metabolismo
Endopeptidases/metabolismo
Fontes Termais/microbiologia
Concentração de Íons de Hidrogênio
Hidrólise
Temperatura Ambiente
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Keratins); 68238-35-7 (Keratins); EC 3.4.- (Endopeptidases)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:150504
[Lr] Data última revisão:
150504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150506
[St] Status:MEDLINE



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