Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles

Yu, Zhidong; Gordon, Steven W.; Nixon, A. J.; Bawden, C. Simon; Rogers, Michael A.; Wildermoth, J. E.; Maqbool, Nauman J.; Pearson, A. J.

doi:10.1016/j.diff.2008.10.009

Cited by 73 publications

(57 citation statements)

References 62 publications

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“…Few studies have been conducted on the regulation of fiber diameter (Itenge et al, 2009). The differentially expressed genes in the present study are involved in several biological pathways relevant to the development of hair follicles and hair growth (WNT, adhesion effect) (Zhang et al, 1997;Yu et al, 2009). Previous studies have shown that lower gene enrichment in protein synthesis and altered biological functions, such as cell proliferation and apoptosis, result in reduced fiber diameter and the corresponding length of wool, and ultimately decrease wool production.…”

Section: Relationship Between Candidate Genes and Wool Traitsmentioning

confidence: 77%

“…Research has shown that Wnt5a combined with FZD3 triggered phosphatidyl inositol kinase (PI3K) mediated by protein kinase Akt phosphorylation, which promotes its downstream functions (Hung et al, 2001;Yu et al, 2009). PI3K is a member of the PI3K family and plays a crucial role in cell function, acting as an extracellular signal molecule.…”

Section: Relationship Between Candidate Genes and Wool Traitsmentioning

confidence: 99%

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Comparative study of 13 candidate genes applying multi-reference normalization to detect the expression of different fineness in skin tissues of wool sheep

et al. 2017

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ABSTRACT. Fiber diameter is a useful indicator of wool traits and it is the main determinant of wool quality and value. A comparative study was conducted to analyze the abundance and expression of 13 candidate genes using expression profile microarray analysis and to identify novel molecular markers associated with wool traits to provide a molecular basis for improving wool quality in sheep. Genes associated with fineness of skin tissue were identified using a real-time reverse transcriptase-polymerase chain reaction method with 18SrRNA, β-Actin, and GAPDH used for multi-reference normalization. The results indicated that the expression levels of TXNIP, TFDP1, and FAIM genes in super-fine type wool sheep were higher than those in fine-type wool sheep; the corresponding expression ratios of superfine to fine wool sheep were 1.45, 1.57, and 2.55, respectively. The expression levels of PIK3CA, ADAM9, and FZD3 genes were lower in super-fine wool sheep compared with fine-type wool sheep; the corresponding expression ratios were 0.61, 0.65, and 0.52, respectively. The other genes tested (RPS6KA, ABCG2, GSTA1, PTPN13, GJB3, PPARD, and LAMB1) were similarly expressed in both types of wool sheep. These results infer that lower expression of PIK3CA, ADAM9, and FZD3 genes was associated with lower fiber diameter, whereas lower expression of TXNIP, TFDP1, and FAIM genes was associated with higher fiber diameter.

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Section: Relationship Between Candidate Genes and Wool Traitsmentioning

confidence: 77%

Section: Relationship Between Candidate Genes and Wool Traitsmentioning

confidence: 99%

Comparative study of 13 candidate genes applying multi-reference normalization to detect the expression of different fineness in skin tissues of wool sheep

et al. 2017

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“…It has been reported that the expression of K38 occurs in distinct cells that are randomly scattered throughout the entire cortex (Langbein et al, 1999). It has been also reported that K38 is asymmetrically expressed in the cortex of crimped human hair and wool (Thibaut et al, 2007;Yu et al, 2009). Further work is required to understand the biological significance of K38.…”

Section: Discussionmentioning

confidence: 90%

“…3g-i and p-r), indicating a particularly low affinity of K38 for either K81 or K85. Because K38 is produced in the lower cortex following the expression of the first pair K35-K85 and simultaneously with K31 (Langbein et al, 1999;Langbein and Schweizer, 2005;Yu et al, 2009), the low affinity of K38 for K85 seems to be a disadvantage when competing with K35 and K31 for heterotypic complex formation with K85 in a cell.…”

Section: Discussionmentioning

confidence: 99%

“…K35 and K85 are the first pairs expressed in the human hair matrix/pre-cortex in the early stages of differentiation, while K36 and K81 are expressed in the mid-to upper cortex at an advanced stage of differentiation (Langbein et al, 1999(Langbein et al, , 2001Langbein and Schweizer, 2005;Schweizer et al, 2007). K38 is expressed in cells scattered randomly throughout the entire cortex (Langbein et al, 1999;Langbein and Schweizer, 2005;Yu et al, 2009), and is suggested to be related to the curvature of a hair fiber (Thibaut et al, 2007). We observed that the affinities in the heterotypic subunit interactions depend on the combination of type I and II hair keratins.…”

Section: Introductionmentioning

confidence: 99%

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<i>In vitro</i> Assembly Properties of Human Type I and II Hair Keratins

Honda

Koike

Kubo

et al. 2014

Cell Struct. Funct.

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ABSTRACT. Multiple type I and II hair keratins are expressed in hair-forming cells but the role of each protein in hair fiber formation remains obscure. In this study, recombinant proteins of human type I hair keratins (K35, K36 and K38) and type II hair keratins (K81 and K85) were prepared using bacterial expression systems. The heterotypic subunit interactions between the type I and II hair keratins were characterized using twodimensional gel electrophoresis and surface plasmon resonance (SPR). Gel electrophoresis showed that the heterotypic complex-forming urea concentrations differ depending on the combination of keratins. K35-K85 and K36-K81 formed relatively stable heterotypic complexes. SPR revealed that soluble K35 bound to immobilized K85 with a higher affinity than to immobilized K81. The in vitro intermediate filament (IF) assembly of the hair keratins was explored by negative-staining electron microscopy. While K35-K81, K36-K81 and K35-K36-K81 formed IFs, K35-K85 afforded tight bundles of short IFs and large paracrystalline assemblies, and K36-K85 formed IF tangles. K85 promotes lateral association rather than elongation of short IFs. The in vitro assembly properties of hair keratins depended on the combination of type I and II hair keratins. Our data suggest the functional significance of K35-K85 and K36-K81 with distinct assembly properties in the formation of macrofibrils.

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De novo filament formation by human hair keratins K85 and K35 follows a filament development pattern distinct from cytokeratin filament networks

et al. 2021

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Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles

Cited by 73 publications

References 62 publications

Comparative study of 13 candidate genes applying multi-reference normalization to detect the expression of different fineness in skin tissues of wool sheep

Comparative study of 13 candidate genes applying multi-reference normalization to detect the expression of different fineness in skin tissues of wool sheep

<i>In vitro</i> Assembly Properties of Human Type I and II Hair Keratins

De novo filament formation by human hair keratins K85 and K35 follows a filament development pattern distinct from cytokeratin filament networks

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