Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P41181 (collecting duct)
 5,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The three-dimensional ultrastructure of principal cells in the rat renal collecting duct was studied by scanning electron microscopy (SEM) using the NaOH digestion technique and the aldehyde prefixosmium-DMSO-osmium method, as well as by transmission electron microscopy (TEM). Special reference was given to the basal labyrinth of the cells and its numerous ruffles and infoldings of the basal plasma membrane. Observations showed that, as the collecting duct descends from the cortical collecting duct (CCD) to the terminal portion of the inner medullary collecting duct (t-IMCD), the pattern of the labyrinth gradually simplified and the ruffles grew thinner. In the CCD, the labyrinth was conspicuously complicated in structure, being formed of tightly arranged ruffles of uniform shape and thickness (70 nm). From the outer medullary collecting duct (OMCD) to the initial portion of inner medullary collecting duct (i-IMCD), the labyrinth became less complicated due to the mingling of wide flattened ruffles. Also, the basal infoldings were reduced in depth (from 700 nm in CCD to 500-600 nm in i-IMCD). In the t-IMCD, the labyrinth was rudimental, and instead presented small grooves (300 nm in depth) which corresponded to indentions of the basal plasma membrane. The regional simplification of the labyrinth was accompanied by morphological changes in mitochondria suggesting their functional decline: the electron density and number of cristae were reduced, these being changed in shape from plate-like to vesicular. These morphological data readily account for the potential for active transport by the collecting duct, which is highest in the CCD and is decreased towards the t-IMCD, and which may function merely as an excretory duct of urine from the papilla. The present study three-dimensionally demonstrates fine-structural heterogeneity in different segments of the collecting duct of the rat kidney.
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PMID:A combined SEM and TEM study on the basal labyrinth of the collecting duct in the rat kidney. 1157 30

The nucleotide sequence data reported have been deposited in the DDBJ, EMBL, GenBank(R) and GSDB Nucleotide Sequence Databases under accession numbers AY196089, AY196090, AY376663, AY377920 and AY376664. Recently, a new class of histone methyltransferases that plays an indirect role in chromatin silencing by targeting a conserved lysine residue in the nucleosome core was described, namely the Dot1 (disruptor of telomeric silencing) family [Feng, Wang, Ng, Erdjument-Bromage, Tempst, Struhl and Zhang (2002) Curr. Biol. 12, 1052-1058; van Leeuwen, Gafken and Gottschling (2002) Cell (Cambridge, Mass.) 109, 745-756; Ng, Feng, Wang, Erdjument-Bromage, Tempst, Zhang and Struhl (2002) Genes Dev. 16, 1518-1527]. In the present study, we report the isolation, genomic organization and in vivo expression of a mouse Dot1 homologue (mDot1). Expressed sequence tag analysis identified five mDot1 mRNAs (mDot1a-mDot1e) derived from alternative splicing. mDot1a and mDot1b encode 1540 and 1114 amino acids respectively, whereas mDot1c-mDot1e are incomplete at the 5'-end. mDot1a is closest to its human counterpart (hDot1L), sharing 84% amino acid identity. mDot1b is truncated at its N- and C-termini and contains an internal deletion. The five mDot1 isoforms are encoded by 28 exons on chromosome 10qC1, with exons 24 and 28 further divided into two and four sections respectively. Alternative splicing occurs in exons 3, 4, 12, 24, 27 and 28. Northern-blot analysis with probes corresponding to the methyltransferase domain or the mDot1a-coding region detected 7.6 and 9.5 kb transcripts in multiple tissues, but only the 7.6 kb transcript was evident in mIMCD3-collecting duct cells. Transfection of mDot1a-EGFP constructs (where EGFP stands for enhanced green fluorescent protein) into human embryonic kidney (HEK)-293T or mIMCD3 cells increased the methylation of H3-K79 but not H3-K4, -K9 or -K36. Furthermore, DMSO induced mDot1 gene expression and methylation specifically at H3-K79 in mIMCD3 cells in a time- and dose-dependent manner. Collectively, these results add new members to the Dot1 family and show that mDot1 is involved in a DMSO-mediated signal-transduction pathway in collecting duct cells.
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PMID:Structure and regulation of the mDot1 gene, a mouse histone H3 methyltransferase. 1457 10