ABSTRACT
BACKGROUND: Although 5-aminolevulinic acid (5-ALA) is used for the photodynamic diagnosis of bladder tumors, hypotension is the most commonly observed adverse effect. We present a case of 5-ALA-induced severe hypotension during transurethral resection of a bladder tumor. CASE PRESENTATION: A 68-year-old man underwent transurethral resection of a bladder tumor using 5-ALA under general anesthesia. Three hours before anesthesia induction, ALA 20 mg/kg was administered orally. After anesthesia induction, his blood pressure decreased to 47/32 mmHg. Although we used phenylephrine and ephedrine, hypotension persisted at 50/33 mmHg. Bolus administration of noradrenaline slightly increased his blood pressure to 65/39 mmHg. Following this, bolus administration of adrenaline elevated his blood pressure. We decided to perform surgery under continuous administration of adrenaline. CONCLUSIONS: Our case report suggests that anesthesiologists should consider 5-ALA-induced hypotension as a differential diagnosis for hypotension occurring after anesthesia induction. Moreover, ephedrine and phenylephrine might be less effective in treating this condition.
ABSTRACT
Cytoplasmic polyadenylation element-binding proteins (CPEBs) are well-conserved RNA-binding proteins, which regulate mRNA translation mainly through control of poly(A) elongation. Here, we show that CPB-3, one of the four CPEB homologs in C. elegans, positively regulates multiple aspects of oocyte production. CPB-3 protein was highly expressed in early meiotic regions of the hermaphrodite gonad. Worms deficient in cpb-3 were apparently impaired in germ cell proliferation and differentiation including sperm/oocyte switching and progression of female meiosis. We also show that cpb-3 is likely to promote the meiotic entry in parallel with gld-3, a component of one of the redundant but essential genetic pathways for the entry to and progression through meiosis. Taken together, CPEB appears to have a conserved role in the early phase of meiosis and in the sperm/oocyte specification, in addition to its reported function during meiotic progression.
Subject(s)
Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans Proteins/physiology , Caenorhabditis elegans/physiology , Germ Cells/cytology , RNA-Binding Proteins/metabolism , RNA-Binding Proteins/physiology , Animals , Cell Differentiation , Cell Proliferation , Female , Genetic Speciation , Male , Meiosis , Oocytes/cytology , Spermatozoa/cytology , Two-Hybrid System TechniquesABSTRACT
The Deleted in Azoospermia (DAZ) gene family encodes putative translational activators that are required for meiosis and other aspects of gametogenesis in animals. The single Caenorhabditis elegans homologue of DAZ, daz-1, is an essential factor for female meiosis. Here, we show that daz-1 is important for the switch from spermatogenesis to oogenesis (the sperm/oocyte switch), which is an essential step for the hermaphrodite germline to produce oocytes. RNA interference of the daz-1 orthologue in a related nematode, Caenorhabditis briggsae, resulted in a complete loss of the sperm/oocyte switch. The C. elegans hermaphrodite deficient in daz-1 also revealed a failure in the sperm/oocyte switch if the genetic background was conditional masculinization of germline. DAZ-1 could bind specifically to mRNAs encoding the FBF proteins, which are translational regulators for the sperm/oocyte switch and germ stem cell proliferation. Expression of the FBF proteins seemed to be lowered in the daz-1 mutant at the stage for the sperm/oocyte switch. Conversely, a mutation in gld-3, a gene that functionally counteracts FBF, could partially restore oogenesis in the daz-1 mutant. Together, we propose that daz-1 plays a role upstream of the pathway for germ cell sex determination.
Subject(s)
Caenorhabditis elegans Proteins/metabolism , Caenorhabditis elegans/growth & development , Oogenesis/genetics , RNA-Binding Proteins/metabolism , Spermatogenesis/genetics , Amino Acid Sequence , Animals , Caenorhabditis elegans/genetics , Caenorhabditis elegans Proteins/genetics , Deleted in Azoospermia 1 Protein , Female , Gametogenesis , Gene Deletion , Gene Expression Regulation, Developmental , Male , Molecular Sequence Data , Oocytes/growth & development , RNA Interference , RNA, Messenger/metabolism , RNA-Binding Proteins/genetics , Sex Determination Processes , Spermatozoa/growth & developmentABSTRACT
The structure, transformation, and bioactivity of single living Schizosaccharomyces pombe cells at the molecular level have been studied in vivo by time- and space-resolved Raman spectroscopy. A time resolution of 100 s and a space resolution of 250 nm have been achieved with the use of a confocal Raman microspectrometer. The space-resolved Raman spectra of living S. pombe cells at different cell cycle stages were recorded in an effort to elucidate the molecular compositions of organelles, including nuclei, cytoplasm, mitochondria, and septa. The time- and space-resolved measurement of the central part of a dividing yeast cell showed continuous spectral evolution from that of the nucleus to those of the cytoplasm and mitochondria and finally to that of the septum, in accordance with the transformation during the cell cycle. A strong Raman band was observed at 1602 cm(-)(1) only when cells were under good nutrient conditions. The effect of a respiration inhibitor, KCN, on a living yeast cell was studied by measuring the Raman spectra of its mitochondria. A sudden disappearance of the 1602 cm(-)(1) band followed by the change in the shape and intensity of the phospholipid bands was observed, indicating a strong relationship between the cell activity and the intensity of this band. We therefore call this band "the Raman spectroscopic signature of life". The Raman mapping of a living yeast cell was also carried out. Not only the distributions of molecular species but also those of active mitochondria in the cell were successfully visualized in vivo.
Subject(s)
Cell Cycle , Organelles/chemistry , Schizosaccharomyces/chemistry , Schizosaccharomyces/cytology , Cell Cycle/genetics , Cell Division , Cell Nucleus/chemistry , Cell Nucleus/genetics , Cell Nucleus/metabolism , G1 Phase , G2 Phase , Green Fluorescent Proteins/metabolism , Microscopy, Fluorescence , Mitochondria/chemistry , Mitochondria/genetics , Mitochondria/metabolism , Organelles/genetics , Organelles/metabolism , S Phase , Schizosaccharomyces/genetics , Schizosaccharomyces/metabolism , Spectrum Analysis, Raman/methodsABSTRACT
PGL-1 is a constitutive protein component of C. elegans germ granules, also known as P granules. Maternally supplied PGL-1 is essential for germline development but only at elevated temperature, raising the possibility that redundant factors provide sufficient function at lower temperatures. We have identified two PGL-1-related proteins, PGL-2 and PGL-3, by sequence analysis of the C. elegans genome and by a yeast two-hybrid screen for proteins that interact with PGL-1. PGL-3 is associated with P granules at all stages of development, while PGL-2 is associated with P granules only during postembryonic development. All three PGL proteins interact with each other in vitro. Furthermore, PGL-1 and PGL-3 are co-immunoprecipitated from embryo extracts, indicating that they are indeed in the same protein complex in vivo. Nevertheless, each PGL protein localizes to P granules independently of the other two. pgl-2 or pgl-3 single-mutant worms do not show obvious defects in germline development. However, pgl-1; pgl-3 (but not pgl-2; pgl-1) double-mutant hermaphrodites and males show significantly enhanced sterility at all temperatures, compared to pgl-1 alone. Mutant hermaphrodites show defects in germline proliferation and in production of healthy gametes and viable embryos. Our findings demonstrate that both PGL-2 and PGL-3 are components of P granules, both interact with PGL-1, and at least PGL-3 functions redundantly with PGL-1 to ensure fertility in both sexes of C. elegans.
