| Literature DB >> 10357109 |
M Tajima1, S Miyake, K Takehana, A Kobayashi, O Yamato, Y Maede.
Abstract
A defect of the core protein of dermatan sulfate proteoglycan was suspected in a Holstein calf affected with a variant form of Ehlers-Danlos syndrome. The mutation was a guanine-to-adenine transition at nucleotide position 254, which resulted in a serine-to-asparagine substitution of the bovine proteoglycan core protein. This substitution occurred in the serine-glycine dipeptide repeat that was suspected to be the binding portion of dermatan sulfate. This point mutation in the genome was also detected by the use of restriction fragment length polymorphism (RFLP) and polymerase chain reaction (PCR) methods. The results of the RFLP and PCR indicated that the calf was a heterozygote of an abnormal gene and a normal gene of the core protein. The interpretation of these data revealed that the functional abnormality in cutaneous tissues of the calf was caused by an abnormal gene of the proteoglycan core protein, which induced a substitution of amino acid.Entities:
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Year: 1999 PMID: 10357109 DOI: 10.1892/0891-6640(1999)013<0202:gdodsp>2.3.co;2
Source DB: PubMed Journal: J Vet Intern Med ISSN: 0891-6640 Impact factor: 3.333