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      Breed, Coat Color, and Hair Length as Risk Factors for Hyperthyroidism in Cats

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          Abstract

          Background

          Hyperthyroidism is very common in older cats, but the etiopathogenesis is poorly understood. Decreased risk of hyperthyroidism has been reported in certain colorpoint breeds, and this observation previously has been hypothesized to result from relatively greater tyrosine availability for thyroid hormone production because of limited ability to convert tyrosine to melanin pigment. However, studies investigating a potential link between coat pigmentation and risk of hyperthyroidism are limited.

          Objective

          To identify associations between coat phenotype and hyperthyroidism by investigation of breed, coat color, and hair length as risk factors for the disease.

          Animals

          Data were used from 4,705 cats aged ≥10 years, referred to a single veterinary teaching hospital (2006–2014) in the United Kingdom.

          Methods

          Retrospective, epidemiological, cross‐sectional study using Bayesian multivariable logistic regression to assess risk factors for hyperthyroidism.

          Results

          Burmese (odds ratio [ OR], 0.01; 0.00–0.23; P = .004), Tonkinese ( OR, 0.05; 0.00–0.95; P = .046), Persian ( OR, 0.21; 0.10–0.44; P < .001), Siamese ( OR, 0.27; 0.12–0.61; P = .002), Abyssinian ( OR, 0.04; 0.00–0.74; P = .031), and British shorthair ( OR, 0.47; 0.28–0.79; P = .004) breeds had decreased risk of hyperthyroidism compared to domestic shorthairs. Longhaired, nonpurebred cats ( OR, 1.30; 1.03–1.64; P = .028) were at increased risk of hyperthyroidism. Coat color/pattern was not associated with hyperthyroidism in nonpurebred cats.

          Conclusions and Clinical Importance

          We identified decreased risk of hyperthyroidism in the Tonkinese, Abyssinian, and British shorthair breeds, identified an association between risk of hyperthyroidism and hair length, and confirmed decreased risk in Burmese, Siamese, and Persian breeds. Additional studies are warranted to further investigate these findings.

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          Most cited references28

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          Tyrosinase and related proteins in mammalian pigmentation.

          Tyrosinase is the key enzyme in pigment synthesis, initiating a cascade of reactions which convert the amino acid tyrosine to the melanin biopolymer. Two other tyrosinase-related proteins (TRP) are known, TRP-1 (probably DHICAoxidase) and TRP-2 (DOPAchrome tautomerase). These proteins show about 40% homology, and recent results have indicated that the genes might be derived from a common ancestor. We will discuss recent findings on genomic organization, and on the proteins and their presumed function, which is important for eumelanin synthesis in mouse and man.
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            Role of Estrogen in Thyroid Function and Growth Regulation

            Thyroid diseases are more prevalent in women, particularly between puberty and menopause. It is wellknown that estrogen (E) has indirect effects on the thyroid economy. Direct effects of this steroid hormone on thyroid cells have been described more recently; so, the aim of the present paper was to review the evidences of these effects on thyroid function and growth regulation, and its mechanisms. The expression and ratios of the two E receptors, α and β , that mediate the genomic effects of E on normal and abnormal thyroid tissue were also reviewed, as well as nongenomic, distinct molecular pathways. Several evidences support the hypothesis that E has a direct role in thyroid follicular cells; understanding its influence on the growth and function of the thyroid in normal and abnormal conditions can potentially provide new targets for the treatment of thyroid diseases.
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              Quantitative analysis of eumelanin and pheomelanin in humans, mice, and other animals: a comparative review.

              The color of hair, skin, and eyes in animals mainly depends on the quantity, quality, and distribution of the pigment melanin, which occurs in two types: black to brown eumelanin and yellow to reddish pheomelanin. Microanalytical methods to quantify the amounts of eumelanin and pheomelanin in biological materials were developed in 1985. The methods are based on the chemical degradation of eumelanin to pyrrole-2,3,5-tricarboxylic acid and of pheomelanin to aminohydroxyphenylalanine isomers, which can be analyzed and quantitated by high performance liquid chromatography. This review summarizes and compares eumelanin and pheomelanin contents in various pigmented tissues obtained from humans, mice, and other animals. These methods have become valuable tools to study the functions of melanin, the control of melanogenesis, and the actions and interactions of pigmentation genes. The methods have also found applications in many clinical studies. High levels of pheomelanin are found only in yellow to red hairs of mammals and in red feathers of birds. It remains an intriguing question why lower vertebrates such as fishes do not synthesize pheomelanin. Detectable levels of pheomelanin are detected in human skin regardless of race, color, and skin type. However, eumelanin is always the major constituent of epidermal melanin, and the skin color appears to be determined by the quantity of melanin produced but not by the quality.
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                Author and article information

                Contributors
                vcrossley@rvc.ac.uk
                Journal
                J Vet Intern Med
                J. Vet. Intern. Med
                10.1111/(ISSN)1939-1676
                JVIM
                Journal of Veterinary Internal Medicine
                John Wiley and Sons Inc. (Hoboken )
                0891-6640
                1939-1676
                13 June 2017
                Jul-Aug 2017
                : 31
                : 4 ( doiID: 10.1111/jvim.2017.31.issue-4 )
                : 1028-1034
                Affiliations
                [ 1 ] Department of Clinical Science and Services Royal Veterinary College University of London London UK
                [ 2 ] Research Support Office Royal Veterinary College University of London London UK
                [ 3 ] Department of Comparative Biomedical Sciences Royal Veterinary College University of London London UK
                Author notes
                [*] [* ]Corresponding author: V.J. Crossley, Department of Clinical Sciences and Services, Royal Veterinary College, Royal College Street, London NW1 0TU, UK.; e‐mail: vcrossley@ 123456rvc.ac.uk
                Author information
                http://orcid.org/0000-0003-3216-5902
                Article
                JVIM14737
                10.1111/jvim.14737
                5508346
                28612380
                6f3c0388-ee7c-4edc-b592-11a3cef9cc97
                Copyright © 2017 The Authors. Journal of Veterinary Internal Medicine published by Wiley Periodicals, Inc. on behalf of the American College of Veterinary Internal Medicine.

                This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.

                History
                : 26 September 2016
                : 28 February 2017
                : 11 April 2017
                Page count
                Figures: 0, Tables: 2, Pages: 7, Words: 7162
                Funding
                Funded by: The Beryl Evetts and Robert Luff Animal Welfare Trust Ltd
                Funded by: MSD Animal Health
                Categories
                Standard Article
                SMALL ANIMAL
                Standard Articles
                Endocrinology
                Custom metadata
                2.0
                jvim14737
                July/August 2017
                Converter:WILEY_ML3GV2_TO_NLMPMC version:5.1.4 mode:remove_FC converted:13.07.2017

                Veterinary medicine
                cat,pigment,tyrosinase,tyrosine
                Veterinary medicine
                cat, pigment, tyrosinase, tyrosine

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