WordNet

small room in which a monk or nun lives (同)cubicle
a device that delivers an electric current as the result of a chemical reaction (同)electric cell
a room where a prisoner is kept (同)jail cell, prison cell
(biology) the basic structural and functional unit of all organisms; they may exist as independent units of life (as in monads) or may form colonies or tissues as in higher plants and animals
any small compartment; "the cells of a honeycomb"
a small unit serving as part of or as the nucleus of a larger political movement (同)cadre
an impairment of health or a condition of abnormal functioning
the 9th letter of the Roman alphabet (同)i
caused by or altered by or manifesting disease or pathology; "diseased tonsils"; "a morbid growth"; "pathologic tissue"; "pathological bodily processes" (同)morbid, pathologic, pathological

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(刑務所の)『独房』;(修道院の)小さい独居室 / (ミツバチの)みつ房,巣穴 / 小さい部屋 / 『細胞』 / 電池 / 花粉室 / (共産党などの)細胞
(体の)『病気』,疾患 / (精神・道徳などの)病気,病弊
女性の話術芸人 =diseur
『私は』私が
iodineの化学記号
病気にかかった / 病的な,不健全な(morbid)

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/06 05:08:48」(JST)

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Inclusion-cell (I-cell) disease, also referred to as mucolipidosis II (ML II),^[1]^[2] is part of the lysosomal storage disease family and results from a defective phosphotransferase (an enzyme of the Golgi apparatus). This enzyme transfers phosphate to mannose residues on specific proteins, and serves as a marker for them to be targeted to lysosomes within the cell. Without this marker, the proteins are instead excreted outside the cell—the default pathway for proteins moving through the Golgi apparatus. Lysosomes cannot function without these proteins, which function as catabolic enzymes for the normal breakdown of substances (e.g. oligosaccharides, lipids, and glycosaminoglycans)^[3] in various tissues throughout the body (i.e. fibroblasts). As a result, a buildup of these substances occurs within lysosomes because they cannot be degraded, resulting in the characteristic I-cells, or "inclusion cells." These cells can be identified under the microscope. In addition, the defective lysosomal enzymes normally found only within lysosomes are instead found in high concentrations in the blood.

Presentation

Mucolipidosis II (ML II) is a particularly severe form of ML that has a significant resemblance to another mucopolysaccharidoses called Hurler syndrome. Generally only laboratory testing can distinguish the two as the presentation is so similar. There are high plasma levels of lysosomal enzymes and are often fatal in childhood.^[4] Typically, by the age of 6 months, failure to thrive and developmental delays are obvious symptoms of this disorder. Some physical signs, such as abnormal skeletal development, coarse facial features, and restricted joint movement, may be present at birth. Children with ML II usually have enlargement of certain organs, such as the liver (hepatomegaly) or spleen (splenomegaly), and sometimes even the heart valves. Affected children often have stiff claw-shaped hands and fail to grow and develop in the first months of life. Delays in the development of their motor skills are usually more pronounced than delays in their cognitive (mental processing) skills. Children with ML II eventually develop a clouding on the cornea of their eyes and, because of their lack of growth, develop short-trunk dwarfism (underdeveloped trunk). These young patients are often plagued by recurrent respiratory tract infections, including pneumonia, otitis media (middle ear infections), bronchitis and carpal tunnel syndrome. Children with ML II generally die before their seventh year of life, often as a result of congestive heart failure or recurrent respiratory tract infections.

Pathophysiology

I-cell disease is an autosomal recessive disorder caused by a deficiency of GlcNAc phosphotransferase, which phosphorylates mannose residues to mannose-6-phosphate on N-linked glycoproteins in the Golgi apparatus within the cell. Without mannose-6-phosphate to target them to the lysosomes, the enzymes are transported from the Golgi to the extracellular space, resulting in large intracellular inclusions of molecules requiring lysosomal degradation in patients with the disease (hence the name of the disorder).^[5] Hydrolases secreted into the blood stream cause little problem as they are deactivated in the neutral pH of the blood.

It can be associated with GNPTA.^[6] In a case report, it was complicated by severe dilative cardiomyopathy(DCM)^[7]

Though rare, a deficiency of phosphodiesterase which would cleave GlcNAc from the Mannose 6 Phosphate tag will also cause I-Cell.^[5]

The presence of lipids, glycosaminoglycans (GAG's) and carbohydrates in the blood provide for the distinguishing characteristic to separate I-Cell from Hurlers Syndrome, in Hurlers, only glycosaminoglycans would be present.

Treatment

A cure does not exist for I-Cell disease/Mucolipidosis II disease. Treatment is limited to controlling or reducing the symptoms that are associated with this disorder. Nutritional supplements, particularly iron and vitamin B12, are often recommended for individuals with I-Cell disease. Physical therapy to improve motor delays and speech therapy to improve language acquisition are treatment options. Surgery can remove the thin layer of corneal clouding to temporarily improve the complication. It is possible that bone marrow transplant may be helpful in delaying or correcting the neurological deterioration that occurs with I-Cell disease.[1]

References

^ "mucolipidosis II" at Dorland's Medical Dictionary
^ Plante M, Claveau S, Lepage P, et al. (March 2008). "Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population". Clin. Genet. 73 (3): 236–44. doi:10.1111/j.1399-0004.2007.00954.x. PMID 18190596.
^ Bamshad, Lynn B. Jorde, John C. Carey, Michael J. (2010). Medical genetics (4th ed.). Philadelphia: Mosby/Elsevier. ISBN 9780323053730.
^ Le, Tao (2014). First Aid for the USMLE 2014. New York: McGraw Hill Education. p. 77. ISBN 9780071831420.
^ ^a ^b Champe, Pamela (2004). Lippincott's Illustrated Reviews: Biochemistry. Richard A Harvey, Denise R Ferrier (3rd ed.). Philadelphia, Pa.: Lippincott-Raven. p. 167. ISBN 0-7817-2265-9.
^ Tiede S, Storch S, Lübke T, et al. (2005). "Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase". Nat. Med. 11 (10): 1109–12. doi:10.1038/nm1305. PMID 16200072.
^ Sahha.gov.mt - 2006 Dec;29_1

External links

mucolipidoses at NINDS — article derived from detail sheet available here
I cell disease at NIH's Office of Rare Diseases
GeneReview/NIH/UW entry on Mucolipidosis II
Hide and Seek Foundation For Lysosomal Disease Research

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 先天性代謝異常：疫学、病因、および臨床的特徴 inborn errors of metabolism epidemiology pathogenesis and clinical features
2. ムコ多糖症：臨床的特徴および診断 mucopolysaccharidoses clinical features and diagnosis
3. Sickle cell disease in sub-Saharan Africa
4. 鎌状赤血球症を有する小児に対する定期的な包括的ケア routine comprehensive care for children with sickle cell disease
5. 鎌状赤血球症を伴う成人における急性胸部症候群 acute chest syndrome in adults with sickle cell disease

English Journal

Fast urinary screening of oligosaccharidoses by MALDI-TOF/TOF mass spectrometry.

Bonesso L, Piraud M, Caruba C, Van Obberghen E, Mengual R, Hinault C.Author information Biochemistry Laboratory, University Hospital, Nice, France. hinault@unice.fr.AbstractBACKGROUND: Oligosaccharidoses, which belong to the lysosomal storage diseases, are inherited metabolic disorders due to the absence or the loss of function of one of the enzymes involved in the catabolic pathway of glycoproteins and indirectly of glycosphingolipids. This enzymatic deficiency typically results in the abnormal accumulation of uncompletely degraded oligosaccharides in the urine. Since the clinical features of many of these disorders are not specific for a single enzyme deficiency, unambiguous screening is critical to limit the number of costly enzyme assays which otherwise must be performed.
Orphanet journal of rare diseases.Orphanet J Rare Dis.2014 Feb 6;9(1):19. doi: 10.1186/1750-1172-9-19.
BACKGROUND: Oligosaccharidoses, which belong to the lysosomal storage diseases, are inherited metabolic disorders due to the absence or the loss of function of one of the enzymes involved in the catabolic pathway of glycoproteins and indirectly of glycosphingolipids. This enzymatic deficiency typica
PMID 24502792

Radiological and clinical characterization of the lysosomal storage disorders: non-lipid disorders.

Xing M, Parker EI, Moreno-De-Luca A, Harmouche E, Terk MR.Author information Division of Musculoskeletal Imaging, Department of Radiology and Imaging Sciences, Emory University Hospital, Atlanta, GA, USA.AbstractLysosomal storage diseases (LSDs) are a large group of genetic metabolic disorders that result in the accumulation of abnormal material, such as mucopolysaccharides, glycoproteins, amino acids and lipids, within cells. Since many LSDs manifest during infancy or early childhood, with potentially devastating consequences if left untreated, timely identification is imperative to prevent irreversible damage and early death. In this review, the key imaging features of the non-lipid or extralipid LSDs are examined and correlated with salient clinical manifestations and genetic information. Disorders are stratified based on the type of excess material causing tissue or organ dysfunction, with descriptions of the mucopolysaccharidoses, mucolipidoses, alpha-mannosidosis, glycogen storage disorder II and cystinosis. In addition, similarities and differences in radiological findings between each of these LSDs are highlighted to facilitate further recognition. Given the rare and extensive nature of the LSDs, mastery of their multiple clinical and radiological traits may seem challenging. However, an understanding of the distinguishing imaging characteristics of LSDs and their clinical correlates may allow radiologists to play a key role in the early diagnosis of these progressive and potentially fatal disorders.
The British journal of radiology.Br J Radiol.2014 Jan;87(1033):20130467. doi: 10.1259/bjr.20130467. Epub 2013 Nov 14.
Lysosomal storage diseases (LSDs) are a large group of genetic metabolic disorders that result in the accumulation of abnormal material, such as mucopolysaccharides, glycoproteins, amino acids and lipids, within cells. Since many LSDs manifest during infancy or early childhood, with potentially deva
PMID 24234586

Japanese Journal

ライソゾーム病症例における気道病変の検討

仲野敦子,有本友季子,吉江うらら,工藤典代
小児耳鼻咽喉科 31(1), 54-58, 2010-03-01
NAID 10026419218

Acid Sphingomyelinase : Relation of ^<93>Lysine Residue on the Ratio of Intracellular to Secreted Enzyme Activity

TAKAHASHI IKUKO,TAKAHASHI TSUTOMU,MIKAMI TAMAKI,KOMATSU MASAKI,OHURA TOSHIHIRO,SCHUCHMAN EDWARD H.,TAKADA GORO
THE TOHOKU JOURNAL OF EXPERIMENTAL MEDICINE 206(4), 333-340, 2005-08-01
NAID 10016478002

Related Pictures

★リンクテーブル★

リンク元	「mucolipidosis type II」「mucolipidosis type IV」「mucolipidosis type I」「I細胞病」「酸性加水分解酵素欠損症」
関連記事	「disease」「I」「Id」「cell」

「mucolipidosis type II」

I-cell disease
	Mannose-6-phosphate (M6P). I-cell disease involves a failure to add M6P to proteins.
Classification and external resources
Specialty	endocrinology
ICD-10	E77.0
ICD-9-CM	272.7
OMIM	252500
DiseasesDB	29175
eMedicine	ped/1150
MeSH	D009081
GeneReviews	Mucolipidosis II;
	[edit on Wikidata]