A curated catalog of canine and equine keratin genes

Balmer, Pierre; Bauer, Anina; Pujar, Shashikant; McGarvey, Kelly M.; Welle, Monika Maria; Galichet, Arnaud; Müller, Eliane J.; Pruitt, Kim D.; Leeb, Tosso; Jagannathan, Vidhya

doi:10.1371/journal.pone.0180359

Cited by 20 publications

(34 citation statements)

References 31 publications

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“…KRT124 and KRT42 were recently identified by total RNA sequencing from canine and equine skin, suggesting that transcripts for these keratins are found in equine haired skin, although this result was not validated by any complementary methods [20]. We amplified neither KRT124 nor KRT42 from haired skin total RNA by RT-PCR (Fig 2), nor did we localize K124 to haired skin by ISH, immunoblotting, or indirect immunofluorescence histology (Fig 3-6), using samples from multiple horses of several breeds (S1 Table).…”

Section: Discussionmentioning

confidence: 99%

“…We amplified neither KRT124 nor KRT42 from haired skin total RNA by RT-PCR (Fig 2), nor did we localize K124 to haired skin by ISH, immunoblotting, or indirect immunofluorescence histology (Fig 3-6), using samples from multiple horses of several breeds (S1 Table). It is possible that the discrepancy relates to the anatomic location of the skin samples used since we collected samples from the dorsal region of the digit and the location of the skin biopsy used by Balmer, et al, is not specified [20]. Further investigation of equine skin keratin isoform expression is required to resolve this issue.…”

Section: Discussionmentioning

confidence: 99%

“…All oligonucleotides were synthesized by Integrated DNA Technologies, Inc. (Coralville, IA, USA). Alternate forward primers were designed to amplify the two KRT10 genes, KRT10A and KRT10B , since the equine KRT10 gene has undergone duplication [20]. For KRT124 , one set of primers was designed to amplify the 3’ exon ( KRT124 3’ ), which shows no homology to known keratins, and a second primer set was designed to amplify a region of the predicted transcript that shows some homology to several keratins ( KRT124 Mid ).…”

Section: Methodsmentioning

confidence: 99%

“…KRT42 and KRT124 exist only as pseudogenes in humans, KRT42P and KRT90P , respectively (the latter was formerly named KRT124P when equine KRT124 was named [1;18;20]). Murine Krt42 (formerly K17n or Ka22 ) mRNA is expressed in the nail unit [21].…”

Section: Introductionmentioning

confidence: 99%

“…A putative KRT124 ortholog, Krt90 (formerly Kb15 ), is translated from cDNA libraries in mice and rats [22] and was identified from the draft genomic sequence of the opossum [23]. KRT42 and KRT124 were recently identified and mapped to the canine and equine genomes, but their patterns of expression have not been described beyond their identification from RNA-seq data derived from skin biopsies from three dogs and one horse [20]. The lack of isoform-specific antibodies has impeded the detailed investigation of equine hoof capsule or lamellar tissue-specific keratins [19].…”

Section: Introductionmentioning

confidence: 99%

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The expression of equine keratins K42 and K124 is restricted to the hoof epidermal lamellae ofEquus caballus

Armstrong

Cassimeris

Santos

et al. 2019

Preprint

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HGH)2 29 Abstract 30 The equine hoof inner epithelium is folded into primary and secondary epidermal lamellae which 31 increase the dermo-epidermal junction surface area of the hoof and can be affected by laminitis, 32 a common disease of equids. Two keratin proteins (K), K42 and K124, are the most abundant 33 keratins in the hoof lamellar tissue of Equus caballus. We hypothesize that these keratins are 34 lamellar tissue-specific and could serve as differentiation-and disease-specific markers. Our 35 objective was to characterize the expression of K42 and K124 in equine stratified epithelia and to 36 generate monoclonal antibodies against K42 and K124. By RT-PCR analysis, keratin gene (KRT) 37 KRT42 and KRT124 expression was present in lamellar tissue, but not cornea, haired skin, or 38 hoof coronet. In situ hybridization studies showed that KRT124 localized to the suprabasal and, 39 to a lesser extent, basal cells of the lamellae, was absent from haired skin and hoof coronet, and 40 abruptly transitions from KRT124-negative coronet to KRT124-positive proximal lamellae. A 41 monoclonal antibody generated against full-length recombinant equine K42 detected a lamellar 42 keratin of the appropriate size, but also cross-reacted with other epidermal keratins. Three 43 monoclonal antibodies generated against N-and C-terminal K124 peptides detected a band of the 44 appropriate size in lamellar tissue and did not cross-react with proteins from haired skin, corneal 45 limbus, hoof coronet, tongue, glabrous skin, oral mucosa, or chestnut on immunoblots. K124 46 localized to lamellar cells by indirect immunofluorescence. This is the first study to demonstrate 47 the localization and expression of a hoof lamellar-specific keratin, K124, and to validate anti-48 K124 monoclonal antibodies. 3 49 1. Introduction 50 The skin and its appendages are made of stratified epithelia composed of keratinocytes, 51 defined by expression of keratin intermediate filament proteins (abbreviated K for proteins and 52 KRT for genes) [1]. Keratin filaments resist stretching (strain) and provide tensile strength to 53 epithelia and skin appendages. Tissue-and differentiation-specific variation in specific keratin 54 isoform content determines the physical and mechanical properties of diverse epithelial tissues 55 and of their keratinocyte building blocks [2;3]. Understanding how keratins function to provide 56 mechanical stability is crucial to our understanding of human diseases associated with keratin 57 mutations and abnormal keratin expression [4-8]. Here we describe unique keratins of the equine 58 (Equus caballus) epidermal lamellae, a highly specialized tissue that withstands extreme force 59 and provides a model for understanding how keratins provide mechanical strength to flexible 60 tissues. 61 Each single-toed foot of a 500 kg horse (E. caballus) must withstand peak ground reaction 62 forces of 2-5,000 N while protecting the underlying limb from trauma [9;10]. The equine 63 adaptation to single-toed unguligrade locomotion requires the ...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%