Methods for a prompt and reliable laboratory diagnosis of Pompe disease: Report from an international consensus meeting

B. Winchester, D. Bali, O. A. Bodamer, C. Caillaud, E. Christensen, A. Cooper, E. Cupler, M. Deschauer, K. Fumić, M. Jackson, P. Kishnani, L. Lacerda, J. Ledvinová, A. Lugowska, Z. Lukacs, I. Maire, H. Mandel, E. Mengel, W. Müller-Felber, M. PiraudA. Reuser, T. Rupar, I. Sinigerska, M. Szlago, F. Verheijen, O. P. van Diggelen, B. Wuyts, E. Zakharova, J. Keutzer

Research output: Contribution to journalArticle

97 Citations (Scopus)

Abstract

Pompe disease is an autosomal recessive disorder of glycogen metabolism caused by a deficiency of the lysosomal enzyme acid α-glucosidase (GAA). It presents at any age, with variable rates of progression ranging from a rapidly progressive course, often fatal by one-year of age, to a more slowly, but nevertheless relentlessly progressive course, resulting in significant morbidity and premature mortality. In infants, early initiation of enzyme replacement therapy is needed to gain the maximum therapeutic benefit, underscoring the need for early diagnosis. Several new methods for measuring GAA activity have been developed. The Pompe Disease Diagnostic Working Group met to review data generated using the new methods, and to establish a consensus regarding the application of the methods for the laboratory diagnosis of Pompe disease. Skin fibroblasts and muscle biopsy have traditionally been the samples of choice for measuring GAA activity. However, new methods using blood samples are rapidly becoming adopted because of their speed and convenience. Measuring GAA activity in blood samples should be performed under acidic conditions (pH 3.8-4.0), using up to 2 mM of the synthetic substrate 4-methylumbelliferyl-α-d-glucoside or glycogen (50 mg/mL), in the presence of acarbose (3-9 μM) to inhibit the isoenzyme maltase-glucoamylase. The activity of a reference enzyme should also be measured to confirm the quality of the sample. A second test should be done to support the diagnosis of Pompe disease until a program for external quality assurance and proficiency testing of the enzymatic diagnosis in blood is established.

Original languageEnglish
Pages (from-to)275-281
Number of pages7
JournalMolecular Genetics and Metabolism
Volume93
Issue number3
DOIs
StatePublished - Mar 1 2008

Fingerprint

Glycogen Storage Disease Type II
Clinical Laboratory Techniques
Blood
Glycogen
Enzymes
Acarbose
Glucosidases
Enzyme Replacement Therapy
Premature Mortality
alpha-Glucosidases
Biopsy
Glucosides
Fibroblasts
Quality assurance
Metabolism
Isoenzymes
Muscle
Early Diagnosis
Skin
Morbidity

Keywords

  • Acarbose
  • Acid maltase deficiency
  • Diagnosis
  • Enzyme assay
  • Glycogen storage disease type II
  • Lysosomal acid α-glucosidase
  • Pompe disease

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Endocrinology, Diabetes and Metabolism

Cite this

Methods for a prompt and reliable laboratory diagnosis of Pompe disease : Report from an international consensus meeting. / Winchester, B.; Bali, D.; Bodamer, O. A.; Caillaud, C.; Christensen, E.; Cooper, A.; Cupler, E.; Deschauer, M.; Fumić, K.; Jackson, M.; Kishnani, P.; Lacerda, L.; Ledvinová, J.; Lugowska, A.; Lukacs, Z.; Maire, I.; Mandel, H.; Mengel, E.; Müller-Felber, W.; Piraud, M.; Reuser, A.; Rupar, T.; Sinigerska, I.; Szlago, M.; Verheijen, F.; van Diggelen, O. P.; Wuyts, B.; Zakharova, E.; Keutzer, J.

In: Molecular Genetics and Metabolism, Vol. 93, No. 3, 01.03.2008, p. 275-281.

Research output: Contribution to journalArticle

Winchester, B, Bali, D, Bodamer, OA, Caillaud, C, Christensen, E, Cooper, A, Cupler, E, Deschauer, M, Fumić, K, Jackson, M, Kishnani, P, Lacerda, L, Ledvinová, J, Lugowska, A, Lukacs, Z, Maire, I, Mandel, H, Mengel, E, Müller-Felber, W, Piraud, M, Reuser, A, Rupar, T, Sinigerska, I, Szlago, M, Verheijen, F, van Diggelen, OP, Wuyts, B, Zakharova, E & Keutzer, J 2008, 'Methods for a prompt and reliable laboratory diagnosis of Pompe disease: Report from an international consensus meeting', Molecular Genetics and Metabolism, vol. 93, no. 3, pp. 275-281. https://doi.org/10.1016/j.ymgme.2007.09.006
Winchester, B. ; Bali, D. ; Bodamer, O. A. ; Caillaud, C. ; Christensen, E. ; Cooper, A. ; Cupler, E. ; Deschauer, M. ; Fumić, K. ; Jackson, M. ; Kishnani, P. ; Lacerda, L. ; Ledvinová, J. ; Lugowska, A. ; Lukacs, Z. ; Maire, I. ; Mandel, H. ; Mengel, E. ; Müller-Felber, W. ; Piraud, M. ; Reuser, A. ; Rupar, T. ; Sinigerska, I. ; Szlago, M. ; Verheijen, F. ; van Diggelen, O. P. ; Wuyts, B. ; Zakharova, E. ; Keutzer, J. / Methods for a prompt and reliable laboratory diagnosis of Pompe disease : Report from an international consensus meeting. In: Molecular Genetics and Metabolism. 2008 ; Vol. 93, No. 3. pp. 275-281.
@article{815d1b2b25ef4d4a9ca5e87c83ca3b5a,
title = "Methods for a prompt and reliable laboratory diagnosis of Pompe disease: Report from an international consensus meeting",
abstract = "Pompe disease is an autosomal recessive disorder of glycogen metabolism caused by a deficiency of the lysosomal enzyme acid α-glucosidase (GAA). It presents at any age, with variable rates of progression ranging from a rapidly progressive course, often fatal by one-year of age, to a more slowly, but nevertheless relentlessly progressive course, resulting in significant morbidity and premature mortality. In infants, early initiation of enzyme replacement therapy is needed to gain the maximum therapeutic benefit, underscoring the need for early diagnosis. Several new methods for measuring GAA activity have been developed. The Pompe Disease Diagnostic Working Group met to review data generated using the new methods, and to establish a consensus regarding the application of the methods for the laboratory diagnosis of Pompe disease. Skin fibroblasts and muscle biopsy have traditionally been the samples of choice for measuring GAA activity. However, new methods using blood samples are rapidly becoming adopted because of their speed and convenience. Measuring GAA activity in blood samples should be performed under acidic conditions (pH 3.8-4.0), using up to 2 mM of the synthetic substrate 4-methylumbelliferyl-α-d-glucoside or glycogen (50 mg/mL), in the presence of acarbose (3-9 μM) to inhibit the isoenzyme maltase-glucoamylase. The activity of a reference enzyme should also be measured to confirm the quality of the sample. A second test should be done to support the diagnosis of Pompe disease until a program for external quality assurance and proficiency testing of the enzymatic diagnosis in blood is established.",
keywords = "Acarbose, Acid maltase deficiency, Diagnosis, Enzyme assay, Glycogen storage disease type II, Lysosomal acid α-glucosidase, Pompe disease",
author = "B. Winchester and D. Bali and Bodamer, {O. A.} and C. Caillaud and E. Christensen and A. Cooper and E. Cupler and M. Deschauer and K. Fumić and M. Jackson and P. Kishnani and L. Lacerda and J. Ledvinov{\'a} and A. Lugowska and Z. Lukacs and I. Maire and H. Mandel and E. Mengel and W. M{\"u}ller-Felber and M. Piraud and A. Reuser and T. Rupar and I. Sinigerska and M. Szlago and F. Verheijen and {van Diggelen}, {O. P.} and B. Wuyts and E. Zakharova and J. Keutzer",
year = "2008",
month = "3",
day = "1",
doi = "10.1016/j.ymgme.2007.09.006",
language = "English",
volume = "93",
pages = "275--281",
journal = "Molecular Genetics and Metabolism",
issn = "1096-7192",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Methods for a prompt and reliable laboratory diagnosis of Pompe disease

T2 - Report from an international consensus meeting

AU - Winchester, B.

AU - Bali, D.

AU - Bodamer, O. A.

AU - Caillaud, C.

AU - Christensen, E.

AU - Cooper, A.

AU - Cupler, E.

AU - Deschauer, M.

AU - Fumić, K.

AU - Jackson, M.

AU - Kishnani, P.

AU - Lacerda, L.

AU - Ledvinová, J.

AU - Lugowska, A.

AU - Lukacs, Z.

AU - Maire, I.

AU - Mandel, H.

AU - Mengel, E.

AU - Müller-Felber, W.

AU - Piraud, M.

AU - Reuser, A.

AU - Rupar, T.

AU - Sinigerska, I.

AU - Szlago, M.

AU - Verheijen, F.

AU - van Diggelen, O. P.

AU - Wuyts, B.

AU - Zakharova, E.

AU - Keutzer, J.

PY - 2008/3/1

Y1 - 2008/3/1

N2 - Pompe disease is an autosomal recessive disorder of glycogen metabolism caused by a deficiency of the lysosomal enzyme acid α-glucosidase (GAA). It presents at any age, with variable rates of progression ranging from a rapidly progressive course, often fatal by one-year of age, to a more slowly, but nevertheless relentlessly progressive course, resulting in significant morbidity and premature mortality. In infants, early initiation of enzyme replacement therapy is needed to gain the maximum therapeutic benefit, underscoring the need for early diagnosis. Several new methods for measuring GAA activity have been developed. The Pompe Disease Diagnostic Working Group met to review data generated using the new methods, and to establish a consensus regarding the application of the methods for the laboratory diagnosis of Pompe disease. Skin fibroblasts and muscle biopsy have traditionally been the samples of choice for measuring GAA activity. However, new methods using blood samples are rapidly becoming adopted because of their speed and convenience. Measuring GAA activity in blood samples should be performed under acidic conditions (pH 3.8-4.0), using up to 2 mM of the synthetic substrate 4-methylumbelliferyl-α-d-glucoside or glycogen (50 mg/mL), in the presence of acarbose (3-9 μM) to inhibit the isoenzyme maltase-glucoamylase. The activity of a reference enzyme should also be measured to confirm the quality of the sample. A second test should be done to support the diagnosis of Pompe disease until a program for external quality assurance and proficiency testing of the enzymatic diagnosis in blood is established.

AB - Pompe disease is an autosomal recessive disorder of glycogen metabolism caused by a deficiency of the lysosomal enzyme acid α-glucosidase (GAA). It presents at any age, with variable rates of progression ranging from a rapidly progressive course, often fatal by one-year of age, to a more slowly, but nevertheless relentlessly progressive course, resulting in significant morbidity and premature mortality. In infants, early initiation of enzyme replacement therapy is needed to gain the maximum therapeutic benefit, underscoring the need for early diagnosis. Several new methods for measuring GAA activity have been developed. The Pompe Disease Diagnostic Working Group met to review data generated using the new methods, and to establish a consensus regarding the application of the methods for the laboratory diagnosis of Pompe disease. Skin fibroblasts and muscle biopsy have traditionally been the samples of choice for measuring GAA activity. However, new methods using blood samples are rapidly becoming adopted because of their speed and convenience. Measuring GAA activity in blood samples should be performed under acidic conditions (pH 3.8-4.0), using up to 2 mM of the synthetic substrate 4-methylumbelliferyl-α-d-glucoside or glycogen (50 mg/mL), in the presence of acarbose (3-9 μM) to inhibit the isoenzyme maltase-glucoamylase. The activity of a reference enzyme should also be measured to confirm the quality of the sample. A second test should be done to support the diagnosis of Pompe disease until a program for external quality assurance and proficiency testing of the enzymatic diagnosis in blood is established.

KW - Acarbose

KW - Acid maltase deficiency

KW - Diagnosis

KW - Enzyme assay

KW - Glycogen storage disease type II

KW - Lysosomal acid α-glucosidase

KW - Pompe disease

UR - http://www.scopus.com/inward/record.url?scp=38949192583&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=38949192583&partnerID=8YFLogxK

U2 - 10.1016/j.ymgme.2007.09.006

DO - 10.1016/j.ymgme.2007.09.006

M3 - Article

C2 - 18078773

AN - SCOPUS:38949192583

VL - 93

SP - 275

EP - 281

JO - Molecular Genetics and Metabolism

JF - Molecular Genetics and Metabolism

SN - 1096-7192

IS - 3

ER -