Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis

被引：404

作者：

Topaz, O

Shurman, DI

Bergman, R

Indelman, M

Ratajczak, P

Mizrachi, M

Khamaysi, Z

Behar, D

Petronius, D

Friedman, V

Zelikovic, I

Raimer, S

Metzker, A

Richard, G

Sprecher, E ^{[1
]}

机构：

[1] Technion Israel Inst Technol, Rambam Med Ctr, Dept Dermatol, Haifa, Israel

[2] Technion Israel Inst Technol, Rambam Med Ctr, Lab Mol Dermatol, Haifa, Israel

[3] Technion Israel Inst Technol, Bruce Rappaport Fac Med, Haifa, Israel

[4] Thomas Jefferson Univ, Dept Dermatol & Cutaneous Biol, Philadelphia, PA 19107 USA

[5] Rambam Med Ctr, Pediat Nephrol Unit, Haifa, Israel

[6] Rambam Med Ctr, Lab Dev Nephrol, Haifa, Israel

[7] Univ Texas, Med Branch, Dept Dermatol, Galveston, TX USA

来源：

NATURE GENETICS | 2004年 / 36卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/ng1358

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Familial tumoral calcinosis (FTC; OMIM 211900) is a severe autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Using linkage analysis, we mapped the gene underlying FTC to 2q24-q31. This region includes the gene GALNT3, which encodes a glycosyltransferase responsible for initiating mucin-type O-glycosylation. Sequence analysis of GALNT3 identified biallelic deleterious mutations in all individuals with FTC, suggesting that defective post-translational modification underlies the disease.

引用

页码：579 / 581

页数：3

共 15 条

[1] cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine - Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3 [J].