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Frequent Detection of Pituitary-Derived PrPres in Human Prion Diseases.

発表形態:
原著論文
主要業績:
主要業績
単著・共著:
共著
発表年月:
2019年10月
DOI:
10.1093/jnen/nlz075
会議属性:
指定なし
査読:
有り
リンク情報:

日本語フィールド

著者:
*Honda H, Matsumoto M, Shijo M, Hamasaki H, Sadashima S, Suzuki SO, Aishima S, Kai K, Nakayama KI, Sasagasako N, Iwaki T.
題名:
Frequent Detection of Pituitary-Derived PrPres in Human Prion Diseases.
発表情報:
J Neuropathol Exp Neurol. 巻: 78 号: 10 ページ: 922-929
キーワード:
概要:
Human prion diseases including sporadic Creutzfeldt-Jakob disease (sCJD), inherited prion diseases, and acquired human prion diseases are lethal neurodegenerative diseases. One of the major sources of iatrogenic Creutzfeldt-Jakob disease was human growth hormone (hGH-iCJD) derived from contaminated cadaveric pituitaries. The incidence of hGH-iCJD has decreased since changing from growth hormone extracted from human cadaveric pituitaries to recombinant pituitary hormones. However, extensive analysis on the localization and detecting of abnormal prion protein in the pituitary gland are limited. In this study, we examined 9 autopsied brains and pituitary glands from 6 patients with prion disease (3 Gerstmann-Sträussler-Scheinker disease, 2 sCJD, and 1 dura mater graft-associated CJD) and 3 individuals with nonprion diseases. Western blot analysis of pituitary samples demonstrated unique glycoforms of normal cellular prion protein with molecular weights of 30-40 kDa, which was higher than the typical 25-35 kDa prion protein in brains. Proteomic analysis also revealed prion protein approximately the molecular weight of 40 kDa in pituitary samples. Moreover, proteinase K-resistant Prion protein was frequently detected in pituitary samples of the prion diseases. Immunohistochemistry for Prion protein revealed mosaic cellular distribution preferentially in growth hormone- or prolactin-producing cells.
抄録:

英語フィールド

Author:
*Honda H, Matsumoto M, Shijo M, Hamasaki H, Sadashima S, Suzuki SO, Aishima S, Kai K, Nakayama KI, Sasagasako N, Iwaki T.
Title:
Frequent Detection of Pituitary-Derived PrPres in Human Prion Diseases.
Announcement information:
J Neuropathol Exp Neurol. Vol: 78 Issue: 10 Page: 922-929
An abstract:
Human prion diseases including sporadic Creutzfeldt-Jakob disease (sCJD), inherited prion diseases, and acquired human prion diseases are lethal neurodegenerative diseases. One of the major sources of iatrogenic Creutzfeldt-Jakob disease was human growth hormone (hGH-iCJD) derived from contaminated cadaveric pituitaries. The incidence of hGH-iCJD has decreased since changing from growth hormone extracted from human cadaveric pituitaries to recombinant pituitary hormones. However, extensive analysis on the localization and detecting of abnormal prion protein in the pituitary gland are limited. In this study, we examined 9 autopsied brains and pituitary glands from 6 patients with prion disease (3 Gerstmann-Sträussler-Scheinker disease, 2 sCJD, and 1 dura mater graft-associated CJD) and 3 individuals with nonprion diseases. Western blot analysis of pituitary samples demonstrated unique glycoforms of normal cellular prion protein with molecular weights of 30-40 kDa, which was higher than the typical 25-35 kDa prion protein in brains. Proteomic analysis also revealed prion protein approximately the molecular weight of 40 kDa in pituitary samples. Moreover, proteinase K-resistant Prion protein was frequently detected in pituitary samples of the prion diseases. Immunohistochemistry for Prion protein revealed mosaic cellular distribution preferentially in growth hormone- or prolactin-producing cells.


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