KRTAP5-1

Last update 23 Jan 2025

Basic Info

Synonyms

KAP5.1, keratin associated protein 5-1, Keratin-associated protein 5-1

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Introduction

In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.

100 Clinical Results associated with KRTAP5-1

100 Translational Medicine associated with KRTAP5-1

0 Patents (Medical) associated with KRTAP5-1

Literatures (Medical) associated with KRTAP5-1

18 Apr 2023·Langmuir : the ACS journal of surfaces and colloids

Exploring the Effects of Wetting and Free Fatty Acid Deposition on an Atomistic Hair Fiber Surface Model Incorporating Keratin-Associated Protein 5-1.

Article

Author: Coscia, Benjamin J. ; Giesen, David J. ; Mileo, Paulo G. M. ; Browning, Andrea R. ; Misra, Mayank ; Halls, Mathew D. ; Fonari, Alexandr ; Sanders, Jeffrey M.

The complex development of cosmetic and medical formulations relies on an ever-growing accuracy of predictive models of hair surfaces. Hitherto, modeling efforts have focused on the description of 18-methyl eicosanoic acid (18-MEA), the primary fatty acid covalently attached to the hair surface, without explicit modeling of the protein layer. Herein, the molecular details of the outermost surface of the human hair fiber surface, also called the F-layer, were studied using molecular dynamics (MD) simulations. The F-layer is composed primarily of keratin-associated proteins KAP5 and KAP10, which are decorated with 18-MEA on the outer surface of a hair fiber. In our molecular model, we incorporated KAP5-1 and evaluated the surface properties of 18-MEA through MD simulations, resulting in 18-MEA surface density, layer thickness, and tilt angles in agreement with previous experimental and computational studies. Subsequent models with reduced 18-MEA surface density were also generated to mimic damaged hair surfaces. Response to wetting of virgin and damaged hair showed rearrangement of 18-MEA on the surface, allowing for water penetration into the protein layer. To demonstrate a potential use case for these atomistic models, we deposited naturally occurring fatty acids and measured 18-MEA's response in both dry and wet conditions. As fatty acids are often incorporated in shampoo formulations, this work demonstrates the ability to model the adsorption of ingredients on hair surfaces. This study illustrates, for the first time, the complex behavior of a realistic F-layer at the molecular level and opens up the possibility of studying the adsorption behavior of larger, more complex molecules and formulations.

01 Dec 1997·Mammalian GenomeQ4 · BIOLOGY

Linkage mapping of wool keratin and keratin-associated protein genes in sheep

Q4 · BIOLOGY

Article

Author: Jill F. Maddox ; Grant W. Montgomery ; Kizanne P. Davies ; Robert J. McLaren ; Geraldine R. Rogers

The authors determined linkage relationships and genetic polymorphisms of sheep KRT and KAP gene families.Nine KRT and KAP genes together with Trichohyalin were mapped onto the sheep genetic linkage map, and six of these represent new assignments.The highly glycine-tyrosine KAPs (KAP6,1,8) were mapped to chromosome 1 and were closely linked to one another.The Trichohyalin gene was also mapped to chromosome 1.The KRT2,10, and KRT2,13 genes were mapped to chromosome 3 and were closely linked.KRT1.2 together with 2 members of the B2 high-sulfur KAP family (KAP1.1, KAP1.3) and 1 member of the BIIB high-sulfur KAP family (KAP3.2) were located on chromosome 2 and were all closely linked.KAP5.1 was mapped to chromosome 21.The data show clustering of some KRT and KAP genes.Genetic variation at both KRT and KAP loci may play an important role in determining various wool traits in sheep.

01 Sep 1994·Journal of Investigative DermatologyQ1 · MEDICINE

Differential Expression of Genes Encoding a Cysteine-Rich Keratin Family in the Hair Cuticle

Q1 · MEDICINE

Article

Author: Brendan J Jenkins ; Barry C Powell

In the hair follicle the cuticle develops as a thin layer of cells between the hair shaft cortex and the inner root sheath. Once the cuticle cells begin to differentiate they accumulate cysteine-rich granules in their cytoplasm but the identity of their constituent proteins has remained largely an enigma. In this report we show differential expression of a family of genes encoding cysteine-rich, glycine-rich keratins in the cuticle. Two clones of the sheep KAP5 gene family were isolated: the KAP5.4 cDNA encodes a protein of 190 amino acids (M(r) = 16,936) containing 32 mol% cysteine, 26 mol% glycine and the partial KAP5.5 cDNA encodes a protein of at least 197 amino acids (M(r) > or = 17,474) containing 29 mol% cysteine, 28 mol% glycine. The predicted amino acid sequences of the KAP5 family show extensive sequence conservation and all the proteins are composed almost entirely of cysteine-rich and glycine-rich repeats. Each KAP5 gene produces an approximately 1.5-kb mRNA species but the KAP5.4 and KAP5.5 mRNA levels appear to be severalfold greater than the KAP5.1 mRNA. Comparative tissue in situ hybridizations reveal a positive correlation between the onset of expression and follicle depth. For a given KAP5 gene two widely different cuticle expression patterns were noted amongst the follicle populations, and on the basis of follicle bulb cell kinetics they are consistent with expression in either sheep primary or secondary follicle types.

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