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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0185117,
umls-concept:C0205164,
umls-concept:C0332514,
umls-concept:C0439148,
umls-concept:C0596901,
umls-concept:C0599220,
umls-concept:C1519249,
umls-concept:C1709634,
umls-concept:C1709694,
umls-concept:C2911684
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pubmed:issue |
3
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pubmed:dateCreated |
1994-2-25
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pubmed:databankReference |
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pubmed:abstractText |
The asymmetric unit membrane (AUM) is a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. It contains quasi-crystalline arrays of 12-nm protein particles each of which is composed of six dumbbell-shaped subdomains. In this paper we describe the precursor sequence, processing and in vitro membrane insertion properties of bovine uroplakin II (UPII), a 15-kDa major protein component of AUM. The cDNA-deduced amino acid sequence revealed that UPII is synthesized as a precursor protein containing a cleavable signal peptide of approximately 26 amino acids, a long pro-sequence of approximately 59 residues harboring three potential N-glycosylation sites, and the mature polypeptide of 100 residues. In vitro translation of UPII mRNA demonstrated that UPII is indeed first synthesized as a 19-kDa precursor, which loses its signal peptide upon insertion into added microsomes; this process is accompanied by the acquisition of high mannose-type oligosaccharides giving rise to a 28-kDa precursor which is completely protected from the digestion by exogenous proteases. These results, together with the presence of a stretch of 25 hydrophobic amino acids at the C terminus, suggest that UPII protein is anchored to the lipid bilayer via its C-terminal membrane-spanning domain with its major N-terminal domain exposed luminally. The formation of the 15-kDa mature UPII requires the removal of the pro-sequence by a furin-like endoprotease. Since only mature UPII devoid of this pro-sequence can interact with 27-kDa uroplakin I, the proteolytic processing of UPII precursor may play an important role in regulating the assembly of AUM. Finally, we showed that genomic sequences cross-hybridizing with bovine UPII cDNA are present in many mammals suggesting that UPII performs a highly conserved function in the terminally differentiated cells of mammalian urinary bladder epithelium.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Poly A,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1775-84
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:7507484-Amino Acid Sequence,
pubmed-meshheading:7507484-Animals,
pubmed-meshheading:7507484-Base Sequence,
pubmed-meshheading:7507484-Blotting, Southern,
pubmed-meshheading:7507484-Cattle,
pubmed-meshheading:7507484-Cell Differentiation,
pubmed-meshheading:7507484-Cell Fractionation,
pubmed-meshheading:7507484-Cell Line,
pubmed-meshheading:7507484-Cell Membrane,
pubmed-meshheading:7507484-Centrifugation, Density Gradient,
pubmed-meshheading:7507484-Cyanogen Bromide,
pubmed-meshheading:7507484-DNA,
pubmed-meshheading:7507484-DNA Primers,
pubmed-meshheading:7507484-Epithelial Cells,
pubmed-meshheading:7507484-Epithelium,
pubmed-meshheading:7507484-Gene Expression,
pubmed-meshheading:7507484-Gene Library,
pubmed-meshheading:7507484-Humans,
pubmed-meshheading:7507484-Macromolecular Substances,
pubmed-meshheading:7507484-Mammals,
pubmed-meshheading:7507484-Membrane Proteins,
pubmed-meshheading:7507484-Microsomes,
pubmed-meshheading:7507484-Molecular Sequence Data,
pubmed-meshheading:7507484-Molecular Weight,
pubmed-meshheading:7507484-Peptide Fragments,
pubmed-meshheading:7507484-Poly A,
pubmed-meshheading:7507484-Polymerase Chain Reaction,
pubmed-meshheading:7507484-Protein Biosynthesis,
pubmed-meshheading:7507484-Protein Conformation,
pubmed-meshheading:7507484-Protein Processing, Post-Translational,
pubmed-meshheading:7507484-Protein Structure, Secondary,
pubmed-meshheading:7507484-RNA,
pubmed-meshheading:7507484-RNA, Messenger,
pubmed-meshheading:7507484-Restriction Mapping,
pubmed-meshheading:7507484-Species Specificity,
pubmed-meshheading:7507484-Transfection,
pubmed-meshheading:7507484-Trypsin,
pubmed-meshheading:7507484-Urinary Bladder,
pubmed-meshheading:7507484-Uroplakin II
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pubmed:year |
1994
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pubmed:articleTitle |
Precursor sequence, processing, and urothelium-specific expression of a major 15-kDa protein subunit of asymmetric unit membrane.
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pubmed:affiliation |
Ronald O. Perelman Department of Dermatology, Kaplan Comprehensive Cancer Center, New York University School of Medicine, New York 10016.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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