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  • 1
    ISSN: 1432-2145
    Keywords: snRNA ; snRNP polypeptides ; Nuclear splicing ; Pollen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In eucaryotes, the nuclei contain small ribonucleoprotein particles (snRNPs) which mediate splicing of RNA precursors. The male gametophytes of Pinus radiata and Viburnum tinus have more than one U1 snRNA isospecies and some snRNP polypeptides detected by northern and western blotting with probes complementary to tomato U1 snRNA and by protein immunodetection. The snRNP components were localized in both vegetative and generative nuclei of the pollen grain by in situ hybridization and immunocytochemistry. This study suggests that vegetative and generative nuclei contain the splicing apparatus for the post-transcriptional RNA processing in the pollen grain.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0730-2312
    Keywords: glucose transporters ; sperm ; dehydroascorbic acid ; fructose ; 2-deoxy-D-glucose ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We analyzed the expression of hexose transporters in human testis and in human, rat, and bull spermatozoa and studied the uptake of hexoses and vitamin C in bull spermatozoa. Immunocytochemical and reverse transcription-polymerase chain reaction analyses demonstrated that adult human testis expressed the hexose transporters GLUT1, GLUT2, GLUT3, GLUT4, and GLUT5. Immunoblotting experiments demonstrated the presence of proteins of about 50-70 kD reactive with anti-GLUT1, GLUT2, GLUT3, and GLUT5 in membranes prepared from human spermatozoa, but no proteins reactive with GLUT4 antibodies were detected. Immunolocalization experiments confirmed the presence of GLUT1, GLUT2, GLUT3, GLUT5, and low levels of GLUT4 in human, rat, and bull spermatozoa. Each transporter isoform showed a typical subcellular localization in the head and the sperm tail. In the tail, GLUT3 and GLUT5 were present at the level of the middle piece in the three species examined, GLUT1 was present in the principal piece, and the localization of GLUT2 differed according of the species examined. Bull spermatozoa transported deoxyglucose, fructose, and the oxidized form of vitamin C, dehydroascorbic acid. Transport of deoxyglucose and dehydroascorbic acid was inhibited by cytochalasin B, indicating the direct participation of facilitative hexose transporters in the transport of both substrates by bull spermatozoa. Transport of fructose was not affected by cytochalasin B, which is consistent for an important role for GLUT5 in the transport of fructose in these cells. The data show that human, rat, and bull spermatozoa express several hexose transporter isoforms that allow for the efficient uptake of glucose, fructose, and dehydroascorbic acid by these cells. J. Cell. Biochem. 71:189-203, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
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  • 3
    ISSN: 0730-2312
    Keywords: FBPase ; gluconeogenesis ; perinuclear association ; metabolic zonation ; immunolocalization ; subcellular fractionation ; confocal microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The localization of fructose 1,6-bisphosphatase (D-Fru-1,6-P2-1-phosphohydrolase, EC 3.1.3.11) in rat kidney and liver was determined immunohistochemically using a polyclonal antibody raised against the enzyme purified from pig kidney. The immunohistochemical analysis revealed that the bisphosphatase was preferentially localized in hepatocytes of the periportal region of the liver and was absent from the perivenous region. Fructose-1,6-bisphosphatase was also preferentially localized in the cortex of the kidney proximal tubules and was absent in the glomeruli, loops of Henle, collecting and distal tubules, and in the renal medulla. As indicated by immunocytochemistry using light microscopy and confirmed with the use of reflection confocal microscopy, the enzyme was preferentially localized in a perinuclear position in the liver and the renal cells. Subcellular fractionation studies followed by enzyme activity assays revealed that a majority of the cellular fructose-1,6-bisphosphatase activity was associated to subcellular particulate structures. Overall, the data support the concept of metabolic zonation in liver as well as in kidney, and establish the concept that the Fructose-1,6-bisphosphatase is a particulate enzyme that can not be considered a soluble enzyme in the classical sense. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
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