Avian keratin genes I. A molecular analysis of the structure and expression of a group of feather keratin genes

Presland, Richard B.; Gregg, Keith; Molloy, Peter L.; Morris, C. Phillip; Crocker, Lesley; Rogers, George E.

doi:10.1016/0022-2836(89)90593-7

Cited by 79 publications

(71 citation statements)

References 43 publications

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“…This observation confirms previous biochemical studies where histidine-rich proteins were seen only in embryonic feathers and scales [Dhouailly et al, 1978;Gregg and Rogers, 1986;Presland et al, 1989;Barnes et al, 1995].…”

Section: Proteins Of Scales and Featherssupporting

confidence: 81%

“…It is believed that the small ß-keratins of feathers allow for the formation of long and axial filaments of ß-keratin within the cytoplasm of feather cells, permitting their lengthening (the 'filant capacity' of FBK) [Brush, 1983]. The specific FBK immunolabeling in feathers (but not in scales) further suggests that the large ß-keratins of archosaurian scales were specifically modified when feathers evolved [Presland et al, 1989;Chuong et al, 2000Chuong et al, , 2003Sawyer et al, 2000;Prum, 2002;Sawyer and Knapp, 2003].…”

Section: Proteins Of Scales and Feathersmentioning

confidence: 99%

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Localization and Characterization of Specific Cornification Proteins in Avian Epidermis

Alibardi

Toni

2004

Cells Tissues Organs

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Little is known about proteins involved in the formation of the stratum corneum in the avian apteric epidermis. The present immunocytochemical, autoradiographic and electrophoretic study shows that antibodies against characteristic proteins of mammalian cornification (α-keratins, loricrin, sciellin, filaggrin, transglutaminase) recognize avian epidermal proteins. This suggests the presence of avian protein with epitopes common to related mammalian proteins. These proteins may also be involved in the formation of the cornified core and cell envelope of mature avian corneocytes. The immunoblotting study suggests that protein bands, cross-reactive for antibodies against loricrin (45, 52–57 kDa), sciellin (54, 84 kDa), filaggrin (32, 38, 45–48 kDa), and transglutaminase (40, 50, 58 kDa), are present in the avian epidermis. Immunocytochemistry shows that immunoreactivity for the above proteins is localized in the transitional and lowermost corneous layer of apteric epidermis. Their epitopes are rapidly masked/altered in cornifying cells and are no longer detectable in mature corneocytes. In scaled epidermis a thick layer made of β-keratins of 14–18, 20–22, and 33 kDa is formed. Only in feathered epidermis (not in scale epidermis), an antifeather chicken β-keratin antibody recognized a protein band at 8–12 kDa. This small β-keratin is probably suitable for the formation of long, axial filaments in elongated barb, barbule and calamus cells. Conversely, the larger β-keratins in scales are irregularly deposited forming flat plates. Tritiated histidine coupled to autoradiography show an absence of both keratohyalin and histidine-rich proteins in adult feathered and scaled epidermis. Most of the labeling appears in proteins within the range of β- and α-keratins. These data on apteric epidermis support the hypothesis of an evolution of the apteric and interfollicular epidermis from the expansion of hinge regions of protoavian archosaurians.

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Section: Proteins Of Scales and Featherssupporting

confidence: 81%

Section: Proteins Of Scales and Feathersmentioning

confidence: 99%

Localization and Characterization of Specific Cornification Proteins in Avian Epidermis

Alibardi

Toni

2004

Cells Tissues Organs

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“…The alignment of the other sequences is one of several alternative possibilities. That shown maximizes the alignment of proline residues and is similar to the one used in our earlier studies a O'Donnell (1973) b O'Donnell and Inglis (1974) c Presland et al (1989): the same sequences is present in duck (Anas platyrhynchos) and pigeon (Columba livia)- Arai et al (1986) d Sawyer et al (2003) e Walker and Bridgen (1976) f Inglis et al (1987) g Whitbread et al (1991) h Toni et al (2007a) i Toni et al (2007b) j Dalla β-sheets in mammalian keratin…”

Section: An Additional β-Sheet In Lizard Clawsupporting

confidence: 72%

The role of β-sheets in the structure and assembly of keratins

Fraser

2009

Biophys Rev

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X-ray diffraction, infrared and electron microscope studies of avian and reptilian keratins, and of stretched wool and hair, have played a central role in the development of models for the β-conformation in proteins. Both α-and β-keratins contain sequences that are predicted to adopt a β-conformation and these are believed to play an important part in the assembly of the filaments and in determining their mechanical properties. Interactions between the small β-sheets in keratins provide a simple mechanism through which shape and chemical complementarity can mediate the assembly of molecules into highly specific structures. Interacting β-sheets in crystalline proteins are often related to one another by diad symmetry and the data available on feather keratin suggest that the filament is assembled from dimers in which the β-sheets are related by a perpendicular diad. The most detailed model currently available is for feather and reptilian keratin but the presence of related β-structural forms in mammalian keratins is also noted.

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“…In birds, α-keratins (intermediate filament proteins) produce α-X-ray patterns that are present in various skin appendages (1). In chickens, five β-keratin subfamilies (claw, feather, feather-like, keratinocyte, and scale) have been classified by sequence heterogeneity and tissue-specific expression (14,24,25,(45)(46)(47). Each of these studies only provided rough profiles due to the limitations of older techniques.…”

Section: Discussionmentioning

confidence: 99%

Topographical mapping of α- and β-keratins on developing chicken skin integuments: Functional interaction and evolutionary perspectives

Yan

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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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 β-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 β-keratin genes in various skin appendages at embryonic developmental stages. The data demonstrate that temporal and spatial α-and β-keratin expression is involved in establishing the diversity of skin appendage phenotypes. Embryonic feathers express a higher proportion of β-keratin genes than other skin regions. In feather filament morphogenesis, β-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 β-keratin forms. α-and β-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 β-keratin genes contribute to the morphological and structural diversity of different avian skin appendages, with feather-β-keratins conferring more possible composites in building intrafeather architecture complexity, setting up a platform of morphological evolution of functional forms in feathers.skin appendage | feather | scale | claw | beak | Evo-Devo

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Avian keratin genes I. A molecular analysis of the structure and expression of a group of feather keratin genes

Cited by 79 publications

References 43 publications

Localization and Characterization of Specific Cornification Proteins in Avian Epidermis

Localization and Characterization of Specific Cornification Proteins in Avian Epidermis

The role of β-sheets in the structure and assembly of keratins

Topographical mapping of α- and β-keratins on developing chicken skin integuments: Functional interaction and evolutionary perspectives

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