Glycogen storage disease type II pathophysiology: Difference between revisions
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**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> | |||
*Other cells including marcophages deposits glycogen and its substrates in lysosomes. | |||
==Genetics== | ==Genetics== | ||
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief:
Overview
The exact pathogenesis of [disease name] is not fully understood.
OR
It is thought that [disease name] is the result of / is mediated by / is produced by / is caused by either [hypothesis 1], [hypothesis 2], or [hypothesis 3].
OR
[Pathogen name] is usually transmitted via the [transmission route] route to the human host.
OR
Following transmission/ingestion, the [pathogen] uses the [entry site] to invade the [cell name] cell.
OR
[Disease or malignancy name] arises from [cell name]s, which are [cell type] cells that are normally involved in [function of cells].
OR
The progression to [disease name] usually involves the [molecular pathway].
OR
The pathophysiology of [disease/malignancy] depends on the histological subtype.
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 deposits glycogen and its substrates in lysosomes.
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
Gross Pathology
- On gross pathology, [feature1], [feature2], and [feature3] are characteristic findings of [disease name].
Microscopic Pathology
- On microscopic histopathological analysis, characteristic findings of glycogen storage disease type 2 include:[9]
- Muscle
- Light microscopy
- PAS-positive (diastase sensitive) vacuoles
- Electron microscopy
- Membrane bound glycogen
- Light microscopy
- Muscle
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.
- ↑ 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.