Keratin and associated proteins of the equine hoof wall.
Abstract: In this study, we described water-insoluble proteins extracted from the germinative regions (stratum internum and coronary band epithelium) and the cornified outer surface (stratum medium) of the equine hoof wall. Two major types of polypeptides were identified: the intermediate filaments (IF) and the IF-associated proteins. The IF, including keratins, composed a major portion of this fraction, had electrophoretic mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the range of 40 to 80 kDa, and reacted with acidic or basic keratin-specific monoclonal antibodies. Differences in the composition of keratins between germinative layers and the stratum medium were seen. Another less well-characterized group of polypeptides associated with the IF also were extracted with the water-insoluble polypeptide fraction. These associated proteins had an apparent molecular weight between 10 and 30 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and contained a higher percentage of sulfur-containing amino acids than did the IF. Water-insoluble protein fractions compared favorably with those found in other less-specialized keratinizing tissue with respect to size, immunoreactivity with monoclonal antibody, and amino acid composition.
Publication Date: 1992-10-01 PubMed ID: 1280927
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The article covers the investigation conducted around the water-insoluble proteins extracted from different parts of the horse hoof. It highlights the two prevalent types of polypeptides identified: intermediate filaments (including keratins) and intermediate filament-associated proteins.
Research and Findings
- The main focus of this research is to analyze the proteins in the equine hoof wall. These proteins include keratins and associated proteins, virtually insoluble in water, sourced from particular regions of the hoof such as the stratum internum, coronary band epithelium, and the stratum medium.
- The researchers used electrophoresis (a lab technique used to separate DNA, RNA, or protein molecules) as part of their methods to identify two major variants of polypeptides. These include Intermediate Filaments (IF), namely keratins, and IF-associated proteins, both fundamental components of the insoluble protein fraction.
- Keratin and their matching polypeptides showed differing compositions in the various germinative layers compared to the stratum medium. They had an apparent molecular weight ranging from 40 to 80 kDa and exhibited reactions with both acidic and basic keratin-specific monoclonal antibodies. Monoclonal antibodies are antibodies made from identical immune cells that are clones of an individual parent cell, and thus extremely specific to a particular antigen.
- The research further pointed out a less characterized group of polypeptides found along with the IF. These associated proteins exhibit a molecular weight between 10 and 30 kDa and are relatively richer in sulfur-containing amino acids compared to the intermediate filaments.
- The composition, size, and immunoreactivity (tendency to provoke an immune response) with monoclonal antibody of these water-insoluble protein fractions were compared favorably with proteins found in less specialized keratinizing tissues.
Significance of the Research
- The research provides important insights into the proteinic makeup of the equine hoof wall, particularly the water-insoluble proteins.
- The identification and comparison of keratins and associated proteins in different components of the hoof potentially contribute to further scientific understanding of hoof physiology and disease mechanisms.
- This extensive knowledge might also prove useful for developing improved treatments and preventative measures for hoof health in horses, as keratins play crucial roles in maintaining the structural integrity of hooves.
Cite This Article
APA
Grosenbaugh DA, Hood DM.
(1992).
Keratin and associated proteins of the equine hoof wall.
Am J Vet Res, 53(10), 1859-1863.
Publication
Researcher Affiliations
- Department of Veterinary Physiology and Pharmacology, Texas A&M University, College Station 77843-4466.
MeSH Terms
- Amino Acids / analysis
- Animals
- Culture Techniques
- Hoof and Claw / chemistry
- Hoof and Claw / metabolism
- Horses / metabolism
- Immunoblotting
- Intermediate Filament Proteins / analysis
- Intermediate Filament Proteins / chemistry
- Intermediate Filaments / chemistry
- Keratins / analysis
- Keratins / biosynthesis
- Solubility
Citations
This article has been cited 4 times.- Armstrong C, Cassimeris L, Da Silva Santos C, Micoogullari Y, Wagner B, Babasyan S, Brooks S, Galantino-Homer H. The expression of equine keratins K42 and K124 is restricted to the hoof epidermal lamellae of Equus caballus. PLoS One 2019;14(9):e0219234.
- Nolte W, Thaller G, Kuehn C. Selection signatures in four German warmblood horse breeds: Tracing breeding history in the modern sport horse. PLoS One 2019;14(4):e0215913.
- Linardi RL, Megee SO, Mainardi SR, Senoo M, Galantino-Homer HL. Expression and localization of epithelial stem cell and differentiation markers in equine skin, eye and hoof. Vet Dermatol 2015 Aug;26(4):213-e47.
- Finno CJ, Stevens C, Young A, Affolter V, Joshi NA, Ramsay S, Bannasch DL. SERPINB11 frameshift variant associated with novel hoof specific phenotype in Connemara ponies. PLoS Genet 2015 Apr;11(4):e1005122.
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