Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding
Hampe, Christiane S ; Hammerle, Lisa P ; Falorni, Alberto ; Robertson, John D. and Lernmark, Åke LU
(2001)
In FEBS Letters
488(3).
p.185-189
- Abstract
The role of K396 in the enzymatic catalysis and the antigenicity of the 65 kDa isoform of glutamate decarboxylase (GAD65) was analyzed using the K396R GAD65 mutant. GAD65 is a major autoantigen in Type 1 diabetes and autoantibodies directed to GAD65 are widely used markers for this disease. We found that (1) recombinant human GAD65 is fully enzymatically active; (2) the K396R mutation abolished GAD65 activity; and (3) the K396R mutant retained full antigenicity to GAD65 autoantibodies in serum from Type 1 diabetes patients, but not to polyclonal antibodies raised to the catalytic domain.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/ea02044e-5b96-429a-94fc-5c25438d148d
- author
- Hampe, Christiane S
; Hammerle, Lisa P
; Falorni, Alberto
; Robertson, John D.
and Lernmark, Åke
LU
- publishing date
- 2001-01-19
- type
- Contribution to journal
- publication status
- published
- keywords
- Autoimmunity, Diabetes, Glutamate decarboxylase, Pyridoxal 5-phosphate
- in
- FEBS Letters
- volume
- 488
- issue
- 3
- pages
- 5 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0035910379
- pmid:11163769
- ISSN
- 0014-5793
- DOI
- 10.1016/S0014-5793(00)02429-7
- language
- English
- LU publication?
- no
- id
- ea02044e-5b96-429a-94fc-5c25438d148d
- date added to LUP
- 2017-09-07 09:05:36
- date last changed
- 2025-10-14 09:40:49
@article{ea02044e-5b96-429a-94fc-5c25438d148d,
abstract = {{<p>The role of K396 in the enzymatic catalysis and the antigenicity of the 65 kDa isoform of glutamate decarboxylase (GAD65) was analyzed using the K396R GAD65 mutant. GAD65 is a major autoantigen in Type 1 diabetes and autoantibodies directed to GAD65 are widely used markers for this disease. We found that (1) recombinant human GAD65 is fully enzymatically active; (2) the K396R mutation abolished GAD65 activity; and (3) the K396R mutant retained full antigenicity to GAD65 autoantibodies in serum from Type 1 diabetes patients, but not to polyclonal antibodies raised to the catalytic domain.</p>}},
author = {{Hampe, Christiane S and Hammerle, Lisa P and Falorni, Alberto and Robertson, John D. and Lernmark, Åke}},
issn = {{0014-5793}},
keywords = {{Autoimmunity; Diabetes; Glutamate decarboxylase; Pyridoxal 5-phosphate}},
language = {{eng}},
month = {{01}},
number = {{3}},
pages = {{185--189}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding}},
url = {{http://dx.doi.org/10.1016/S0014-5793(00)02429-7}},
doi = {{10.1016/S0014-5793(00)02429-7}},
volume = {{488}},
year = {{2001}},
}