WordNet
- a salt of phosphoric acid (同)orthophosphate, inorganic_phosphate
- carbonated drink with fruit syrup and a little phosphoric acid
PrepTutorEJDIC
- 〈U〉リン酸塩 / 《複数形で》リン酸肥料
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/19 14:39:12」(JST)
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- 1. 高リン血症の原因および治療 causes and treatment of hyperphosphatemia
- 2. 慢性腎疾患における高リン血症の治療 treatment of hyperphosphatemia in chronic kidney disease
- 3. 低リン血症の診断および治療 diagnosis and treatment of hypophosphatemia
- 4. マンノース結合レクチン欠損症 mannose binding lectin deficiency
- 5. 急性リン酸腎症 acute phosphate nephropathy
English Journal
- Testosterone influences the expression and distribution of the cation-dependent mannose-6-phosphate receptor in rat epididymis. Implications in the distribution of enzymes.
- Carvelli L1, Bannoud N, Aguilera AC, Sartor T, Malossi E, Sosa MA.Author information 1Laboratorio de Biología y Fisiología Celular 'Dr. Francisco Bertini', Instituto de Histología y Embriología, CONICET - Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, Mendoza, Argentina; Instituto de Ciencias Básicas (ICB), Universidad Nacional de Cuyo, Mendoza, Argentina.AbstractThe mammalian epididymis plays a role in sperm maturation through its secretory activity. Among the proteins secreted by the epithelium, there are significant amounts of acid hydrolases. In most cell types, the normal distribution of lysosomal enzymes is mediated by mannose-6-phosphate receptors (MPRs). In this study, we analysed the expression and distribution of the cation-dependent MPR (CD-MPR) in epididymis from control, castrated or castrated rats with testosterone replacement. It was observed that expression of CD-MPR increased due to castration in all regions of the epididymis, which was reversed by injection of testosterone. We also measured the activity of α-mannosidase and observed that the castration tends to increase the retention of this enzyme in the tissue, which is reversed by the hormone replacement. In corpus, this resulted in a reduced secretion of the enzyme. Immunohistochemistry showed that CD-MPR has a supranuclear location (different from the cation-independent MPR), most likely in principal cells, and low reactivity in other cell types. The signal in castrated animals was more intense and tended to redistribute towards the apical cytoplasm. Thus, we concluded that expression and distribution of CD-MPR is affected by decrease of testosterone in rat epididymis, and this could change the distribution of lysosomal enzymes.
- Andrologia.Andrologia.2014 Apr;46(3):224-30. doi: 10.1111/and.12065. Epub 2013 Jan 7.
- The mammalian epididymis plays a role in sperm maturation through its secretory activity. Among the proteins secreted by the epithelium, there are significant amounts of acid hydrolases. In most cell types, the normal distribution of lysosomal enzymes is mediated by mannose-6-phosphate receptors (MP
- PMID 23290006
- Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.
- van Meel E1, Qian Y, Kornfeld SA.Author information 1Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.AbstractThe lysosomal storage disorder mucolipidosis III αβ is caused by mutations in the αβ subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransferase). This Golgi-localized enzyme mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases, and loss of function results in impaired lysosomal targeting of these acid hydrolases and decreased lysosomal degradation. Here we show that two patient missense mutations, Lys4Gln and Ser15Tyr, in the N-terminal cytoplasmic tail of the α subunit of phosphotransferase impair retention of the catalytically active enzyme in the Golgi complex. This results in mistargeting of the mutant phosphotransferases to lysosomes, where they are degraded, or to the cell surface and release into the medium. The finding that mislocalization of active phosphotransferase is the basis for mucolipidosis III αβ in a subset of patients shows the importance of single residues in the cytoplasmic tail of a Golgi-resident protein for localization to this compartment.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2014 Mar 4;111(9):3532-7. doi: 10.1073/pnas.1401417111. Epub 2014 Feb 18.
- The lysosomal storage disorder mucolipidosis III αβ is caused by mutations in the αβ subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransferase). This Golgi-localized enzyme mediates the first step in the synthesis of the mannose 6-phosphate recognition
- PMID 24550498
- Insulin-like growth factor II peptide fusion enables uptake and lysosomal delivery of α-N-acetylglucosaminidase to mucopolysaccharidosis type IIIB fibroblasts.
- Kan SH, Troitskaya LA, Sinow CS, Haitz K, Todd AK, Di Stefano A, Le SQ, Dickson PI, Tippin BL.Author information *Department of Pediatrics, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, CA 90502, U.S.A.AbstractEnzyme replacement therapy for MPS IIIB (mucopolysaccharidosis type IIIB; also known as Sanfilippo B syndrome) has been hindered by inadequate mannose 6 phosphorylation and cellular uptake of rhNAGLU (recombinant human α-N-acetylglucosaminidase). We expressed and characterized a modified rhNAGLU fused to the receptor-binding motif of IGF-II (insulin-like growth factor 2) (rhNAGLU-IGF-II) to enhance its ability to enter cells using the cation-independent mannose 6-phosphate receptor, which is also the receptor for IGF-II (at a different binding site). RhNAGLU-IGF-II was stably expressed in CHO (Chinese-hamster ovary) cells, secreted and purified to apparent homogeneity. The Km and pH optimum of the fusion enzyme was similar to those reported for rhNAGLU. Both intracellular uptake and confocal microscopy suggested that MPS IIIB fibroblasts readily take up the fusion enzyme via receptor-mediated endocytosis that was inhibited significantly (P<0.001) by the monomeric IGF-II peptide. Glycosaminoglycan storage was reduced by 60% (P<0.001) to near background levels in MPS IIIB cells after treatment with rhNAGLU-IGF-II, with half-maximal correction at concentrations of 3-12 pM. A similar cellular uptake mechanism via the IGF-II receptor was also demonstrated in two different brain tumour-derived cell lines. Fusion of rhNAGLU to IGF-II enhanced its cellular uptake while maintaining enzymatic activity, supporting its potential as a therapeutic candidate for treating MPS IIIB.
- The Biochemical journal.Biochem J.2014 Mar 1;458(2):281-9. doi: 10.1042/BJ20130845.
- Enzyme replacement therapy for MPS IIIB (mucopolysaccharidosis type IIIB; also known as Sanfilippo B syndrome) has been hindered by inadequate mannose 6 phosphorylation and cellular uptake of rhNAGLU (recombinant human α-N-acetylglucosaminidase). We expressed and characterized a modified rhNAGLU f
- PMID 24266751
Japanese Journal
- ARF1 and ARF4 regulate recycling endosomal morphology and retrograde transport from endosomes to the Golgi apparatus.
- Nakai Waka,Kondo Yumika,Saitoh Akina,Naito Tomoki,Nakayama Kazuhisa,Shin Hye-Won
- Molecular biology of the cell 24(16), 2570-2581, 2013-08
- … Small GTPases of the ADP-ribosylation factor (ARF) family, except for ARF6, mainly localize to the Golgi apparatus, where they trigger formation of coated carrier vesicles. …
- NAID 120005324911
- Isolation, Purification, and Biochemical Characterization of Two Forms of Lysosomal β-N-Acetylhexosaminidase from the Invertebrate Unio
- VENUGOPAL Ashapogu,SIVAKUMAR Nadimpalli
- Bioscience, Biotechnology, and Biochemistry 77(3), 497-504, 2013-03
- NAID 40019625480
- マンノース6リン酸受容体相同ドメインを有するレクチンおよびタンパク質による糖鎖認識の分子構造基盤
- Satoh Tadashi
- Trends in glycoscience and glycotechnology 24(138-140), 193-202, 2012-07
- NAID 40019538232
Related Links
- The M6P tag is added to such proteins in the cis-Golgi apparatus. Specifically, in a reaction involving uridine diphosphate (UDP) and N-acetylglucosamine, the enzyme N-acetylglucosamine-1-phosphate transferase catalyzes the N-linked ...
- In the fields of biochemistry and cell biology, mannose 6-phosphate receptors ( MPRs) are proteins that bind newly synthesized lysosomal hydrolases in the trans-Golgi network (TGN) and deliver them to pre-lysosomal compartments.
Related Pictures
★リンクテーブル★
「マンノース6-リン酸」
- 英
- mannose 6-phosphate, mannose-6-phosphate, M6P
- 同
- マンノース6リン酸
- 関
- リソソーム、ゴルジ装置、マンノース6-リン酸受容体、mannose-6-phosphate recognition markers、マンノース
- first aid step1 2006 p.83
USMLE
- Q book p.139 31
「M6P」
「mannose 6-phosphate receptor」
- マンノース6リン酸受容体、マンノース6リン酸レセプター
「cation-independent mannose 6-phosphate receptor」
- 関
- CI-MPR
「cation-dependent mannose 6-phosphate receptor」
- 関
- CD-MPR
「mannose-6-phosphate isomerase」
「phosphate」
- n.
- 関
- inorganic phosphate、orthophosphate、orthophosphoric acid、phospho、phosphoester、phosphoric、phosphoric acid、phosphoric acid ester、phosphorus