Glycogen storage disease type II pathophysiology: Difference between revisions
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{{Glycogen storage disease type II}} | {{Glycogen storage disease type II}} | ||
{{CMG}}; {{AE}} | {{CMG}}; {{AE}} {{Anmol}} | ||
==Overview== | ==Overview== | ||
Glycogen storage disease type 2 (GSD type 2) results due to deficiency of [[lysosomal enzyme]] [[Acid alpha-glucosidase|acid α-glucosidase]] (GAA). GSD type 2 is the most severe type of GSD leading to death in earlier stages of life. Deficiency of GAA leads to accumulation of glycogen in [[lysosomes]] of various tissues, most commonly in [[cardiac]], [[skeletal]], and [[smooth muscle cells]]. There is a progressive accumulation of glycogen and its substrates in tissues leading to debilitation, [[organ failure]] and finally death. GSD type 2 follows an [[Autosomal recessive|autosomal recessive pattern]]. GAA [[gene mutation]] responsible for [[lysosomal enzyme]] [[Acid alpha-glucosidase|acid α-glucosidase]] (GAA) deficiency in GSD type 2 and is located on [[chromosome]] locus 17q25. On gross pathology, characteristic findings of glycogen storage disease type 2 include [[cardiomegaly]] and [[myopathy]]. On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include [[muscle]] has PAS-positive ([[diastase]] sensitive) [[vacuoles]]. | |||
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==Pathophysiology== | ==Pathophysiology== | ||
===Pathogenesis=== | ===Pathogenesis=== | ||
*Glycogen storage disease type 2 (GSD type 2) results due to deficiency of lysosomal enzyme acid α-glucosidase (GAA).<ref name="pmid13954110">{{cite journal| author=HERS HG| title=alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease). | journal=Biochem J | year= 1963 | volume= 86 | issue= | pages= 11-6 | pmid=13954110 | doi= | pmc=1201703 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=13954110 }} </ref> | *Glycogen storage disease type 2 (GSD type 2) results due to deficiency of [[lysosomal enzyme]] [[Acid alpha-glucosidase|acid α-glucosidase]] (GAA).<ref name="pmid13954110">{{cite journal| author=HERS HG| title=alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease). | journal=Biochem J | year= 1963 | volume= 86 | issue= | pages= 11-6 | pmid=13954110 | doi= | pmc=1201703 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=13954110 }} </ref> | ||
*GSD type 2 is the most severe type of GSD leading to death in earlier stages of life. | *GSD type 2 is the most severe type of GSD leading to death in earlier stages of life. | ||
*Deficiency of GAA leads to accumulation of glycogen in lysosomes of various tissues, most commonly in cardiac, skeletal, and smooth muscle cells.<ref name="pmid15126982">{{cite journal| author=Kishnani PS, Howell RR| title=Pompe disease in infants and children. | journal=J Pediatr | year= 2004 | volume= 144 | issue= 5 Suppl | pages= S35-43 | pmid=15126982 | doi=10.1016/j.jpeds.2004.01.053 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15126982 }} </ref> | *Deficiency of GAA leads to accumulation of glycogen in [[lysosomes]] of various tissues, most commonly in [[cardiac]], [[skeletal]], and [[smooth muscle cells]].<ref name="pmid15126982">{{cite journal| author=Kishnani PS, Howell RR| title=Pompe disease in infants and children. | journal=J Pediatr | year= 2004 | volume= 144 | issue= 5 Suppl | pages= S35-43 | pmid=15126982 | doi=10.1016/j.jpeds.2004.01.053 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15126982 }} </ref> | ||
*There is a progressive accumulation of glycogen and its substrates in tissues leading to debilitation, organ failure and finally death.<ref name="pmid16702877">{{cite journal| author=ACMG Work Group on Management of Pompe Disease. Kishnani PS, Steiner RD, Bali D, Berger K, Byrne BJ et al.| title=Pompe disease diagnosis and management guideline. | journal=Genet Med | year= 2006 | volume= 8 | issue= 5 | pages= 267-88 | pmid=16702877 | doi=10.109701.gim.0000218152.87434.f3 | pmc=3110959 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16702877 }} </ref> | *There is a progressive accumulation of glycogen and its substrates in tissues leading to debilitation, [[organ failure]] and finally death.<ref name="pmid16702877">{{cite journal| author=ACMG Work Group on Management of Pompe Disease. Kishnani PS, Steiner RD, Bali D, Berger K, Byrne BJ et al.| title=Pompe disease diagnosis and management guideline. | journal=Genet Med | year= 2006 | volume= 8 | issue= 5 | pages= 267-88 | pmid=16702877 | doi=10.109701.gim.0000218152.87434.f3 | pmc=3110959 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16702877 }} </ref> | ||
*There are a range of severity and varies with: | *There are a range of severity and varies with: | ||
**Age of onset | **Age of onset | ||
**Organ involvement including degree and severity of muscular involvement (skeletal, respiratory, cardiac) | **Organ involvement including degree and severity of [[muscular]] involvement ([[skeletal]], [[respiratory]], [[cardiac]]) | ||
**Rate of progression | **Rate of progression | ||
*It is believed that movement of muscle and increased myofibril rigidity during contraction leads to rupture of lysosomes in muscle. These ruptured lysosomes in muscles releases glycogen and other lysosomal contents leading to destruction of muscles.<ref name="pmid6199885">{{cite journal| author=Griffin JL| title=Infantile acid maltase deficiency. I. Muscle fiber destruction after lysosomal rupture. | journal=Virchows Arch B Cell Pathol Incl Mol Pathol | year= 1984 | volume= 45 | issue= 1 | pages= 23-36 | pmid=6199885 | doi= | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=6199885 }} </ref> | *It is believed that movement of muscle and increased [[myofibril]] rigidity during contraction leads to rupture of [[lysosomes]] in [[muscle]]. These ruptured [[lysosomes]] in muscles releases [[glycogen]] and other [[lysosomal]] contents leading to destruction of [[muscles]].<ref name="pmid6199885">{{cite journal| author=Griffin JL| title=Infantile acid maltase deficiency. I. Muscle fiber destruction after lysosomal rupture. | journal=Virchows Arch B Cell Pathol Incl Mol Pathol | year= 1984 | volume= 45 | issue= 1 | pages= 23-36 | pmid=6199885 | doi= | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=6199885 }} </ref> | ||
*Other cells including marcophages deposits glycogen and its substrates in lysosomes. | *Other cells including [[marcophages]] also deposits [[glycogen]] and its substrates in [[lysosomes]]. [[Lysosome|Lysosomes]] in these tissues usually does not rupture. | ||
===Metabolic Pathway=== | |||
[[File:GSD TYPE II.png|center|800px|frame| Metabolic pathways showing defects in various glycogen storage disease type II, (ɔ) Image courtesy of WikiDoc.org, by '''"[[User:Anmol Pitliya|Dr. Anmol Pitliya]]"''']] | |||
==Genetics== | ==Genetics== | ||
*GSD type 2 follows an [[Autosomal recessive|autosomal recessive pattern]].<ref name="pmid2111708">{{cite journal| author=Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R| title=Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. | journal=DNA Cell Biol | year= 1990 | volume= 9 | issue= 2 | pages= 85-94 | pmid=2111708 | doi=10.1089/dna.1990.9.85 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2111708 }} </ref> | *GSD type 2 follows an [[Autosomal recessive|autosomal recessive pattern]].<ref name="pmid2111708">{{cite journal| author=Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R| title=Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. | journal=DNA Cell Biol | year= 1990 | volume= 9 | issue= 2 | pages= 85-94 | pmid=2111708 | doi=10.1089/dna.1990.9.85 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2111708 }} </ref> | ||
*GAA [[gene mutation]] responsible for lysosomal enzyme acid α-glucosidase (GAA) deficiency in GSD type 2 and is located on [[chromosome]] locus 17q25.<ref name="pmid3049072">{{cite journal| author=Hoefsloot LH, Hoogeveen-Westerveld M, Kroos MA, van Beeumen J, Reuser AJ, Oostra BA| title=Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. | journal=EMBO J | year= 1988 | volume= 7 | issue= 6 | pages= 1697-704 | pmid=3049072 | doi= | pmc=457155 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=3049072 }} </ref><ref name="pmid2268276">{{cite journal| author=Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA| title=Characterization of the human lysosomal alpha-glucosidase gene. | journal=Biochem J | year= 1990 | volume= 272 | issue= 2 | pages= 493-7 | pmid=2268276 | doi= | pmc=1149727 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2268276 }} </ref><ref name="pmid2111708">{{cite journal| author=Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R| title=Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. | journal=DNA Cell Biol | year= 1990 | volume= 9 | issue= 2 | pages= 85-94 | pmid=2111708 | doi=10.1089/dna.1990.9.85 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2111708 }} </ref><ref name="pmid8786092">{{cite journal| author=Kuo WL, Hirschhorn R, Huie ML, Hirschhorn K| title=Localization and ordering of acid alpha-glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. | journal=Hum Genet | year= 1996 | volume= 97 | issue= 3 | pages= 404-6 | pmid=8786092 | doi= | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=8786092 }} </ref> | *GAA [[gene mutation]] responsible for [[lysosomal enzyme]] [[Acid alpha-glucosidase|acid α-glucosidase]] (GAA) deficiency in GSD type 2 and is located on [[chromosome]] locus 17q25.<ref name="pmid3049072">{{cite journal| author=Hoefsloot LH, Hoogeveen-Westerveld M, Kroos MA, van Beeumen J, Reuser AJ, Oostra BA| title=Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. | journal=EMBO J | year= 1988 | volume= 7 | issue= 6 | pages= 1697-704 | pmid=3049072 | doi= | pmc=457155 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=3049072 }} </ref><ref name="pmid2268276">{{cite journal| author=Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA| title=Characterization of the human lysosomal alpha-glucosidase gene. | journal=Biochem J | year= 1990 | volume= 272 | issue= 2 | pages= 493-7 | pmid=2268276 | doi= | pmc=1149727 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2268276 }} </ref><ref name="pmid2111708">{{cite journal| author=Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R| title=Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. | journal=DNA Cell Biol | year= 1990 | volume= 9 | issue= 2 | pages= 85-94 | pmid=2111708 | doi=10.1089/dna.1990.9.85 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=2111708 }} </ref><ref name="pmid8786092">{{cite journal| author=Kuo WL, Hirschhorn R, Huie ML, Hirschhorn K| title=Localization and ordering of acid alpha-glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization. | journal=Hum Genet | year= 1996 | volume= 97 | issue= 3 | pages= 404-6 | pmid=8786092 | doi= | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=8786092 }} </ref> | ||
==Associated Conditions== | ==Associated Conditions== | ||
Conditions associated with glycogen storage disease type 2 include:<ref name="pmid16133732" /> | |||
* [[Cardiomegaly]] | |||
* [[Hepatomegaly]] | |||
* [[Cardiomyopathy]] | |||
==Gross Pathology== | ==Gross Pathology== | ||
*On gross pathology, [ | *On gross pathology, characteristic findings of glycogen storage disease type 2 include [[cardiomegaly]] and [[myopathy]].<ref name="pmid25183957">{{cite journal| author=Lim JA, Li L, Raben N| title=Pompe disease: from pathophysiology to therapy and back again. | journal=Front Aging Neurosci | year= 2014 | volume= 6 | issue= | pages= 177 | pmid=25183957 | doi=10.3389/fnagi.2014.00177 | pmc=4135233 | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=25183957 }} </ref> | ||
==Microscopic Pathology== | ==Microscopic Pathology== | ||
*On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include:<ref name="pmid16133732">{{cite journal| author=Winkel LP, Hagemans ML, van Doorn PA, Loonen MC, Hop WJ, Reuser AJ et al.| title=The natural course of non-classic Pompe's disease; a review of 225 published cases. | journal=J Neurol | year= 2005 | volume= 252 | issue= 8 | pages= 875-84 | pmid=16133732 | doi=10.1007/s00415-005-0922-9 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16133732 }} </ref> | *On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include:<ref name="pmid16133732">{{cite journal| author=Winkel LP, Hagemans ML, van Doorn PA, Loonen MC, Hop WJ, Reuser AJ et al.| title=The natural course of non-classic Pompe's disease; a review of 225 published cases. | journal=J Neurol | year= 2005 | volume= 252 | issue= 8 | pages= 875-84 | pmid=16133732 | doi=10.1007/s00415-005-0922-9 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=16133732 }} </ref> | ||
**Muscle | **[[Muscle]] has PAS-positive ([[diastase]] sensitive) [[vacuoles]] | ||
{| | |||
| | |||
*** | [[File:Glycogen storage disorder (PAS stain).jpg|center|thumb|400px|Glycogen storage disease type II PAS stain - [https://commons.wikimedia.org/wiki/File%3AGlycogen_storage_disorder_(PAS_stain).jpg Source:By Department of Pathology, Calicut Medical College, via Wikimedia Commons]]] | ||
**** | | | ||
[[File:Glycogen storage disorder (PAS with diastase).jpg|center|thumb|400px|Glycogen storage disease type II PAS with diastase stain - [https://commons.wikimedia.org/wiki/File%3AGlycogen_storage_disorder_(PAS_with_diastase).jpg Source:By Department of Pathology, Calicut Medical College, via Wikimedia Commons]]] | |||
|} | |||
*On electron microscopic evaluation of [[skeletal muscle]] damage as classic infantile GSD type 2 progress include:<ref name="pmid17075580">{{cite journal| author=Thurberg BL, Lynch Maloney C, Vaccaro C, Afonso K, Tsai AC, Bossen E et al.| title=Characterization of pre- and post-treatment pathology after enzyme replacement therapy for Pompe disease. | journal=Lab Invest | year= 2006 | volume= 86 | issue= 12 | pages= 1208-20 | pmid=17075580 | doi=10.1038/labinvest.3700484 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=17075580 }} </ref> | |||
{| | |||
! style="background:#4479BA; color: #FFFFFF;" align="center" + |Stage | |||
! style="background:#4479BA; color: #FFFFFF;" align="center" + | Microscopic findings | |||
|- | |||
| style="background:#DCDCDC;" align="center" + |Stage 1 | |||
| style="background:#F5F5F5;" + | | |||
*Small [[glycogen]]-filled [[lysosomes]] in between intact [[myofibrils]] | |||
|- | |||
| style="background:#DCDCDC;" align="center" + |Stage 2 | |||
| style="background:#F5F5F5;" + | | |||
*Increase in [[cytoplasmic]] [[glycogen]] and the size and number of [[lysosomes]] combined with fragmentation of [[myofibrils]] | |||
|- | |||
| style="background:#DCDCDC;" align="center" + |Stage 3 | |||
| style="background:#F5F5F5;" + | | |||
*[[Glycogen]]-filled [[lysosomes]] are tightly packed | |||
*Some show [[membrane]] rupture | |||
*Only few [[myofibril]] fragments remain | |||
|- | |||
| style="background:#DCDCDC;" align="center" + |Stages 4 | |||
| style="background:#F5F5F5;" + | | |||
*Most [[glycogen]] is [[cytoplasmic]] | |||
*The contractile elements of [[muscle]] cells are completely lost | |||
|- | |||
| style="background:#DCDCDC;" align="center" + |Stage 5 | |||
| style="background:#F5F5F5;" + | | |||
*The [[cells]] bloat due to the influx of water as [[glycogen]] is diluted. | |||
|} | |||
==References== | ==References== | ||
{{reflist|2}} | {{reflist|2}} | ||
{{WS}} | |||
{{WH}} | |||
[[Category:Endocrinology]] | [[Category:Endocrinology]] | ||
[[Category:Hepatology]] | [[Category:Hepatology]] | ||
[[Category:Gastroenterology]] | |||
[[Category:Pediatrics]] | |||
[[Category:Up-To-Date]] | |||
[[Category:Genetic disorders]] | |||
[[Category:Metabolic disorders]] |
Latest revision as of 14:21, 29 March 2018
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Anmol Pitliya, M.B.B.S. M.D.[2]
Overview
Glycogen storage disease type 2 (GSD type 2) results due to deficiency of lysosomal enzyme acid α-glucosidase (GAA). GSD type 2 is the most severe type of GSD leading to death in earlier stages of life. Deficiency of GAA leads to accumulation of glycogen in lysosomes of various tissues, most commonly in cardiac, skeletal, and smooth muscle cells. There is a progressive accumulation of glycogen and its substrates in tissues leading to debilitation, organ failure and finally death. GSD type 2 follows an autosomal recessive pattern. GAA gene mutation responsible for lysosomal enzyme acid α-glucosidase (GAA) deficiency in GSD type 2 and is located on chromosome locus 17q25. On gross pathology, characteristic findings of glycogen storage disease type 2 include cardiomegaly and myopathy. On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include muscle has PAS-positive (diastase sensitive) vacuoles.
Pathophysiology
Pathogenesis
- Glycogen storage disease type 2 (GSD type 2) results due to deficiency of lysosomal enzyme acid α-glucosidase (GAA).[1]
- GSD type 2 is the most severe type of GSD leading to death in earlier stages of life.
- Deficiency of GAA leads to accumulation of glycogen in lysosomes of various tissues, most commonly in cardiac, skeletal, and smooth muscle cells.[2]
- There is a progressive accumulation of glycogen and its substrates in tissues leading to debilitation, organ failure and finally death.[3]
- There are a range of severity and varies with:
- Age of onset
- Organ involvement including degree and severity of muscular involvement (skeletal, respiratory, cardiac)
- Rate of progression
- It is believed that movement of muscle and increased myofibril rigidity during contraction leads to rupture of lysosomes in muscle. These ruptured lysosomes in muscles releases glycogen and other lysosomal contents leading to destruction of muscles.[4]
- Other cells including marcophages also deposits glycogen and its substrates in lysosomes. Lysosomes in these tissues usually does not rupture.
Metabolic Pathway
Genetics
- GSD type 2 follows an autosomal recessive pattern.[5]
- GAA gene mutation responsible for lysosomal enzyme acid α-glucosidase (GAA) deficiency in GSD type 2 and is located on chromosome locus 17q25.[6][7][5][8]
Associated Conditions
Conditions associated with glycogen storage disease type 2 include:[9]
Gross Pathology
- On gross pathology, characteristic findings of glycogen storage disease type 2 include cardiomegaly and myopathy.[10]
Microscopic Pathology
- On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include:[9]
- On electron microscopic evaluation of skeletal muscle damage as classic infantile GSD type 2 progress include:[11]
Stage | Microscopic findings |
---|---|
Stage 1 |
|
Stage 2 |
|
Stage 3 | |
Stages 4 |
|
Stage 5 |
References
- ↑ HERS HG (1963). "alpha-Glucosidase deficiency in generalized glycogenstorage disease (Pompe's disease)". Biochem J. 86: 11–6. PMC 1201703. PMID 13954110.
- ↑ Kishnani PS, Howell RR (2004). "Pompe disease in infants and children". J Pediatr. 144 (5 Suppl): S35–43. doi:10.1016/j.jpeds.2004.01.053. PMID 15126982.
- ↑ ACMG Work Group on Management of Pompe Disease. Kishnani PS, Steiner RD, Bali D, Berger K, Byrne BJ; et al. (2006). "Pompe disease diagnosis and management guideline". Genet Med. 8 (5): 267–88. doi:10.109701.gim.0000218152.87434.f3 Check
|doi=
value (help). PMC 3110959. PMID 16702877. - ↑ Griffin JL (1984). "Infantile acid maltase deficiency. I. Muscle fiber destruction after lysosomal rupture". Virchows Arch B Cell Pathol Incl Mol Pathol. 45 (1): 23–36. PMID 6199885.
- ↑ 5.0 5.1 Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R (1990). "Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences". DNA Cell Biol. 9 (2): 85–94. doi:10.1089/dna.1990.9.85. PMID 2111708.
- ↑ Hoefsloot LH, Hoogeveen-Westerveld M, Kroos MA, van Beeumen J, Reuser AJ, Oostra BA (1988). "Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex". EMBO J. 7 (6): 1697–704. PMC 457155. PMID 3049072.
- ↑ Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA (1990). "Characterization of the human lysosomal alpha-glucosidase gene". Biochem J. 272 (2): 493–7. PMC 1149727. PMID 2268276.
- ↑ Kuo WL, Hirschhorn R, Huie ML, Hirschhorn K (1996). "Localization and ordering of acid alpha-glucosidase (GAA) and thymidine kinase (TK1) by fluorescence in situ hybridization". Hum Genet. 97 (3): 404–6. PMID 8786092.
- ↑ 9.0 9.1 Winkel LP, Hagemans ML, van Doorn PA, Loonen MC, Hop WJ, Reuser AJ; et al. (2005). "The natural course of non-classic Pompe's disease; a review of 225 published cases". J Neurol. 252 (8): 875–84. doi:10.1007/s00415-005-0922-9. PMID 16133732.
- ↑ Lim JA, Li L, Raben N (2014). "Pompe disease: from pathophysiology to therapy and back again". Front Aging Neurosci. 6: 177. doi:10.3389/fnagi.2014.00177. PMC 4135233. PMID 25183957.
- ↑ Thurberg BL, Lynch Maloney C, Vaccaro C, Afonso K, Tsai AC, Bossen E; et al. (2006). "Characterization of pre- and post-treatment pathology after enzyme replacement therapy for Pompe disease". Lab Invest. 86 (12): 1208–20. doi:10.1038/labinvest.3700484. PMID 17075580.