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  • *Tumor Suppressor Proteins  (1)
  • Acartia clausi  (1)
  • 1995-1999  (1)
  • 1990-1994  (1)
  • 1955-1959
  • 1
    ISSN: 1573-5117
    Keywords: Acartia clausi ; copepod ; tropical lagoon ; metabolic budgets
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Simultaneous measurements of respiration, excretion and production rates were carried out several times over a year period at five representative stations of the Ebrié Lagoon. Assuming a constant assimilation efficiency rate of 69.4%, we derived metabolic budgets for carbon, nitrogen and phosphorus. Daily specific ingestion rates calculated were rather generally high, and ranged between 54 and 159% of body carbon, between 26 and 102% of body nitrogen and between 108 and 307% of body phosphorus. Regional and seasonal variations depended mainly upon variations in trophic conditions. Curvilinear relationships between ingestion production, or net production efficiency K2, and food concentration (as chlorophyll-a + phaeopigments) showed that food could have been a limiting factor. Furthermore, K2 were low when compared with data from the literature (mean of 21% in carbon, 39% in nitrogen and 11% in phosphorus). Complementary laboratory experiments carried out on adults fed with enriched natural particles or algal cultures (Tetraselmis sp. or Dunaliella sp.) showed similar production (egg-production) vs food concentration curvilinear relationships as in the field. However, considerably higher maximal ingestion and production rates were obtained for animals fed algal cultures suggesting that optima for food acquisition and transformation were not reached in field conditions. Consequently, A. clausi, which represents more than 50% of the zooplankton biomass, appears to be rather inefficient in transforming the abundant particulate organic matter produced in the lagoon. This results from its high level of metabolic expenditure through respiration or excretion (about 50% of ingestion in terms of carbon) and from the small size and poor trophic value of food particles (high percentage of detritus).
    Type of Medium: Electronic Resource
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  • 2
    Publication Date: 1995-08-04
    Description: The p27 mammalian cell cycle protein is an inhibitor of cyclin-dependent kinases. Both in vivo and in vitro, p27 was found to be degraded by the ubiquitin-proteasome pathway. The human ubiquitin-conjugating enzymes Ubc2 and Ubc3 were specifically involved in the ubiquitination of p27. Compared with proliferating cells, quiescent cells exhibited a smaller amount of p27 ubiquitinating activity, which accounted for the marked increase of p27 half-life measured in these cells. Thus, the abundance of p27 in cells is regulated by degradation. The specific proteolysis of p27 may represent a mechanism for regulating the activity of cyclin-dependent kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pagano, M -- Tam, S W -- Theodoras, A M -- Beer-Romero, P -- Del Sal, G -- Chau, V -- Yew, P R -- Draetta, G F -- Rolfe, M -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):682-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mitotix Inc., Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624798" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Anaphase-Promoting Complex-Cyclosome ; Animals ; *Cell Cycle Proteins ; Cell Line ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/*antagonists & inhibitors ; Cysteine Endopeptidases/*metabolism ; Electroporation ; Enzyme Inhibitors/metabolism ; Humans ; Kinetics ; Leupeptins/pharmacology ; Ligases/metabolism ; Mice ; Microtubule-Associated Proteins/*metabolism ; Multienzyme Complexes/*metabolism ; Proteasome Endopeptidase Complex ; Rabbits ; Recombinant Proteins/metabolism ; Succinates/pharmacology ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; Ubiquitin-Conjugating Enzymes ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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