Identification of a New Thyroglobulin Variant: A Guanine-to-Adenine Transition Resulting in the Substitution of Arginine 2510 by Glutamine

MENDIVE, FERNANDO M.; ROSSETTI, LILIANA C.; VASSART, GILBERT; VASSART, GILBERT; TARGOVNIK , HÉCTOR M.

THYROID

MARY ANN LIEBERT INC

Lugar: New York; Año: 1997 vol. 7 p. 587 - 591

1050-7256

We analyzed thyroglobulin (Tg) reverse transcription polymerase chain reaction (RT-PCR) products from three congenital goiters and three normal thyroid tissues by Taq I digestion. Tg coding sequences were amplified from position 57 to 8448 in 12 amplification fragments. A Taq I restriction fragment length polymorphism was detected in the most 3' RT-PCR product (nt 7584 through 8448). Data from the sequence showed aG^A transition(nt 7627) causing the disappearance of the Taq I site in position 7625. It produced the substitution of arginine for a glutamine at position 2510. Afterwards, we established that the glutamine alíele is present in normal unrelated individuals, with an allelic frequency of 62%. This Tg variant is thus widely represented in the human population. The available sequence information from rat and bovine Tg showed the presence, in both, of glutamine at position 2510.