Title
Characterization of FMR1 proteins isolated from different tissues Characterization of FMR1 proteins isolated from different tissues
Author
Faculty/Department
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences. Pharmacy
Publication type
article
Publication
Oxford ,
Subject
Chemistry
Biology
Human medicine
Source (journal)
Human molecular genetics. - Oxford
Volume/pages
4(1995) :5 , p. 895-901
ISSN
0964-6906
ISI
A1995QX78000015
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
FMR1 protein expression was studied in different tissues, In human, monkey and murine tissues, high molecular mass FMR1 proteins (67-80 kDa) are found, as shown in lymphoblastoid cell lines. The identity of these proteins was confirmed by their absence in tissues from patients with the fragile X syndrome and a FMR1 knock-out mouse, An Ile367Asn substitution in the FMR1 protein did not alter the translation, processing and localization of FMR1 proteins in lymphoblastoid cells from a patient carrying this mutation, All the high molecular mass FMR1 proteins isolated from normal lymphoblastoid cells and cells from the patient with the Ile367Asn substitution were able to bind RNA, However, the FMR1 proteins of the patient had reduced affinity for RNA binding at high salt concentrations, In some human, monkey and murine tissues low molecular mass FMR1 proteins (39-41 kDa) were found, which had the same N terminus as the 67-90 kDa isoforms, but differ in their C terminus and are therefore most likely the result of carboxy-terminal proteolytic cleavage, These low molecular mass FMR1 proteins did not bind RNA, in contrast with the high molecular mass FMR1 proteins; The significance of these low molecular mass' proteins remains to be studied.
E-info
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