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Glycobiology Advance Access published online on May 16, 2006
Glycobiology, doi:10.1093/glycob/cwl002
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received April 3, 2006
Revised May 10, 2006
Accepted May 11, 2006

Article

Molecular cloning and characterization of rat Pomt1 and Pomt2

Hiroshi Manya 1 1, Atsuro Chiba 2 1, Richard U. Margolis 3, and Tamao Endo 1 *

1 Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, Itabashi-ku, Tokyo 173-0015, Japan
2 Department of Neurology, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan
3 Department of Pharmacology, New York University Medical Center, New York, New York 10016, USA

* To whom correspondence should be addressed.
Tamao Endo, E-mail: endo{at}tmig.or.jp


  Abstract

Mammalian O-mannosylation, although an uncommon type of protein modification, is essential for normal brain and muscle development. Defective O-mannosylation causes congenital muscular dystrophy with abnormal neuronal migration (Walker-Warburg syndrome). Here, we have identified and cloned rat Pomt1 and Pomt2, which are homologues of human POMT1 and POMT2, with identities of 86% and 90%, respectively, at the amino acid level. Coexpression of both genes was found to be necessary for enzymatic activity, as is the case with human POMT1 and POMT2. Northern and RT-PCR analyses revealed that rat Pomt1 and Pomt2 are expressed in all tissues but most strongly in testis. In situ hybridization histochemistry of rat brain revealed that Pomt1 and Pomt2 mRNA are coexpressed in neurons (dentate gyrus and CA1-CA3 region of the hippocampus, and cerebellar Purkinje cells). Two transcription initiation sites were observed in rat Pomt2, resulting in two forms: a testis form and a somatic form. The two forms had equal protein O-mannosyltransferase activity when coexpressed with rat Pomt1. Coexpression studies also showed that the human and rat protein O-mannosyltransferases are interchangeable, providing further evidence for the closeness of their structures.

Keywords: rat/protein O-mannosyltransferase activity/glycosylation/Pomt1 and Pomt2.

1 These authors contributed equally to this work.


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M. Lommel, T. Willer, and S. Strahl
POMT2, a key enzyme in Walker-Warburg syndrome: somatic sPOMT2, but not testis-specific tPOMT2, is crucial for mannosyltransferase activity in vivo
Glycobiology, August 1, 2008; 18(8): 615 - 625.
[Abstract] [Full Text] [PDF]


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