Feather Keratin: Composition, Structure and Biogenesis

Gregg, Keith; Rogers, George E.

doi:10.1007/978-3-662-00989-5_33

Cited by 112 publications

(145 citation statements)

References 78 publications

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“…10). This disposition is also present for different ␤ -keratins in the avian genome (Gregg and Rogers, 1986).…”

Section: Discussionmentioning

confidence: 62%

“…12). In particular, the sequence underlined in Figure 12, indicates as corebox, shows a 42-53% homology with avian keratins, and seems implicated in the formation of the framework of ␤-keratin filaments (Gregg and Rogers, 1986;Brush, 1993;Fraser and Parry, 1996).…”

Section: Discussionmentioning

confidence: 99%

“…as also the latter protein is polymerized into long cables in elongating barb and barbule cells during feather development (Gregg and Rogers, 1986;Brush, 1993;Fraser and Parry, 1996). Therefore, the presence of a central, conserved region in reptilian and avian keratins suggests that these proteins had a common, ancestral protein in stem-reptilian progenitors of modern reptiles and birds.…”

Section: Discussionmentioning

confidence: 99%

“…The ␤-keratins in both reptilian and avian skin are made of ␤-pleated sheets (strands) aggregated into a densely packed lattice and show a typ-ical X-ray and ultrastructural pattern of 3-to 4-nm electron pale filaments (Baden and Maderson, 1970;Fraser et al, 1972;Gregg and Rogers, 1986;Fraser and Parry, 1996). Generally, ␤-keratins have a smaller molecular weight (10 -22 kDa) than ␣-(soft)-keratins (40 -68 kDa; Brush, 1979, 1983;Sawyer et al, 2000;Alibardi and Toni, 2006a,b).…”

Section: Introductionmentioning

confidence: 99%

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Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Valle

Nardi

Toffolo

et al. 2006

Developmental Dynamics

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“…10). This disposition is also present for different ␤ -keratins in the avian genome (Gregg and Rogers, 1986).…”

Section: Discussionmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Valle

Nardi

Toffolo

et al. 2006

Developmental Dynamics

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“…From the maturation of barb ridges an axial ramus and symmetric barbules are later formed. The ramus and barb/barbule cells accumulate feather keratin that imparts both flexibility and resistance to traction (Gregg & Rogers 1986;Brush 1993;Sawyer et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Follicular patterns during feather morphogenesis in relation to the formation of asymmetric feathers, filoplumes and bristles

Alibardi

2009

Italian Journal of Zoology

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The present microscopic study on follicles of regenerating feathers describes the pattern of morphogenesis responsible for the formation of symmetric and asymmetric feathers, filoplumes and bristles. Barb ridges are generated in the ventral locus of the follicle and merge into a rachis located in the dorsal side after helicoidal growth along the ramogenic collar. Asymmetric feathers result from the elongation of rami of larger size on one side with respect to the opposite side of the follicle before merging into the rachis. The increase in length of barb ridges along the collar may derive from the higher number of cells incorporated in the ramus, from the increase of cell size or elongation within barb ridges, or from the shifting of the ventral locus along the collar. The latter produces the formation of more elongated rami on one side of the follicle with respect to the rami with the same size formed on the opposite side. These processes determine an increase of the length of helical growth of barbs on one side of the follicle and the formation of the longer rami in asymmetric feathers. The change in pattern of barb ridge formation gives origin to bristles and filoplumes.

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Immunocytochemical localization and biochemical analysis of α and β keratins in the avian lingual epithelium

Carver

Sawyer

1989

Am. J. Anat.

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The alpha and beta keratins are found as 10-nm and 3-nm cytoplasmic filaments, respectively. While the alpha keratins are produced in essentially all vertebrate epithelia (Franke et al.: Exp. Cell Res., 116:429-445, 1978; Sun et al.: Proc. Natl. Acad. Sci. USA, 76:2813-2817, 1979), the beta keratins have been demonstrated only in specific epithelial tissues of birds and reptiles (Sawyer et al.: In: Biology of the Integument: Vertebrates. J. Bereiter-Hahn, A.G. Matoltsy, and K.S. Richards, eds. Springer-Verlag, Berlin, Vol. 2, pp. 194-238, 1986; Landmann: In: Biology of the Integument: Vertebrates. J. Bereiter-Hahn, A.G. Matoltsy, and K.S. Richards, eds. Springer-Verlag, Berlin, Vol. 2, pp. 150-187, 1986). Recently, Homberger and Brush (Zoomorphology, 106:103-114, 1986) have demonstrated that within the lingual epithelium of parrots, beta keratins are expressed exclusively in the anterior ventral region. While it is well established that epidermal-dermal interactions are important for the regional expression of the beta keratin genes in the avian scutate scales and feathers, little is known about the expression of beta keratins in other epithelial structures such as the tongue. We have used biochemical and immunocytochemical techniques to analyze the alpha and beta keratins of the lingual epithelium of the chick as an initial step in the characterization of this model system for developmental studies. We have found that alpha keratins are present throughout the lingual epithelium. The anterior ventral epithelium contains alpha keratin polypeptides characteristic of skin-type differentiation, while the epithelium of the dorsal and posterior ventral regions contains alpha keratin polypeptides characteristic of esophageal-type differentiation (O'Guin et al.: In: Current Topics in Developmental Biology: The Molecular and Developmental Biology of Keratins. A.A. Moscona and A. Monroy, eds. R.H. Sawyer, vol. ed. Academic Press, New York, Vol. 22, pp. 282-306, 1987). Beta keratins are produced only in the differentiated epithelial cells of the anterior ventral region of the tongue. Immunoelectron microscopy demonstrates that the alpha and beta keratins of the stratum intermedium and corneum of the anterior ventral region are found together in the large filament bundles characteristic of this region. The preexistence of the alpha keratins in the cells destined to produce beta keratins as well as the colocalization of these keratins in the filament bundles of these cells suggests that a functional relationship may exist between the alpha and beta keratins.

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Feather Keratin: Composition, Structure and Biogenesis

Cited by 112 publications

References 78 publications

Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Cloning and characterization of scale β‐keratins in the differentiating epidermis of geckoes show they are glycine‐proline‐serine–rich proteins with a central motif homologous to avian β‐keratins

Follicular patterns during feather morphogenesis in relation to the formation of asymmetric feathers, filoplumes and bristles

Immunocytochemical localization and biochemical analysis of α and β keratins in the avian lingual epithelium

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