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91.
Molecular cloning and characterization of an alpha1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans 总被引:2,自引:1,他引:1
We report on the identification, molecular cloning, and characterization of
an alpha1,3 fucosyltransferase (alpha1,3FT) expressed by the nematode,
Caenorhabditis elegans . Although C. elegans glycoconjugates do not express
the Lewis x antigen Galbeta1-- >4[Fucalpha1-->3]GlcNAcbeta-->R,
detergent extracts of adult C.elegans contain an alpha1,3FT that can
fucosylate both nonsialylated and sialylated acceptor glycans to generate
the Lexand sialyl Lexantigens, as well as the lacdiNAc-containing acceptor
GalNAcbeta1-->4GlcNAcbeta1-- >R to generate GalNAcbeta1-->4
[Fucalpha1-->3]GlcNAcbeta1-->R. A search of the C.elegans genome
database revealed the existence of a gene with 20-23% overall identity to
all five cloned human alpha1,3FTs. The putative cDNA for the C.elegans
alpha1,3FT (CEFT-1) was amplified by PCR from a cDNA lambdaZAP library,
cloned, and sequenced. COS7 cells transiently transfected with cDNA
encoding CEFT-1 express the Lex, but not sLexantigen. The CEFT-1 in the
transfected cell extracts can synthesize Lex, but not sialyl Lex, using
exogenous acceptors. A second fucosyltransferase activity was detected in
extracts of C. elegans that transfers Fuc in alpha1,2 linkage to Gal
specifically on type-1 chains. The discovery of alpha-fucosyltransferases
in C. elegans opens the possibility of using this well-characterized
nematode as a model system for studying the role of fucosylated glycans in
the development and survival of C.elegans and possibly other helminths.
相似文献
92.
The acidic glycolipid fraction (AF) of the porcine, parasitic nematode,
Ascaris suum , consisted of two subfractions. The major component AF II
reacted with orcinol-sulfuric acid and molybdate, while the minor component
AF I gave a positive reaction with azure-A, a cationic dye specific for
sulfatides. Sugar constituent analysis, methanolysis, methylation analysis,
matrix-assisted laser desorption/ionization time- of-flight mass
spectrometry, liquid secondary-ion mass spectrometry, and gas-liquid
chromatography/mass spectrometry specified AF II to be an unusual
phosphoinositolglycosphingolipid (Galalpha1-Ins-P-1ceramide) and the minor
component AF I to be a 3-sulfogalactosylcerebroside (HSO3-
3Galss1-1ceramide). The ceramide moiety of both components consisted of
lignoceric (C24:0) and cerebronic (C24h:0) acids and mainly C17 iso-
branched sphingosine. Immunohistochemical localization studies of the
glycolipid-bound antigenic determinants with a polyclonal antiserum against
AF II and an anti-sulfatide monoclonal antibody against AF I revealed the
presence of the AF II-epitope in the intestine, whereas the AF I-epitope
was found in the hypodermis, contractile zone of somatic muscle cells and
the external musculature of the uterus. To our knowledge, this is the first
report of the presence of a sulfatide in an invertebrate.
相似文献
93.
94.
C J Pritzlaff L Wideman J Y Weltman R D Abbott M E Gutgesell M L Hartman J D Veldhuis A Weltman 《Journal of applied physiology》1999,87(2):498-504
To investigate the effects of exercise intensity on growth hormone (GH) release, 10 male subjects were tested on 6 randomly ordered occasions [1 control condition (C), 5 exercise conditions (Ex)]. Serum GH concentrations were measured in samples obtained at 10-min intervals between 0700 and 0900 (baseline) and 0900 and 1300 (exercise+ recovery). Integrated GH concentrations (IGHC) were calculated by trapezoidal reconstruction. During Ex subjects exercised for 30 min (0900-0930) at one of the following intensities [normalized to the lactate threshold (LT)]: 25 and 75% of the difference between LT and rest (0.25LT and 0.75LT, respectively), at LT, and at 25 and 75% of the difference between LT and peak (1.25LT and 1.75LT, respectively). No differences were observed among conditions for baseline IGHC. Exercise+recovery IGHC (mean +/- SE: C = 250 +/- 60; 0.25LT = 203 +/- 69; 0.75LT = 448 +/- 125; LT = 452 +/- 119; 1.25LT = 512 +/- 121; 1.75LT = 713 +/- 115 microg x l(-1) x min(-1)) increased linearly with increasing exercise intensity (P < 0.05). Deconvolution analysis revealed that increasing exercise intensity resulted in a linear increase in the mass of GH secreted per pulse and GH production rate [production rate increased from 16. 5 +/- 4.5 (C) to 32.1 +/- 5.2 microg x distribution volume(-1) x min(-1) (1.75LT), P < 0.05], with no changes in GH pulse frequency or half-life of elimination. We conclude that the GH secretory response to exercise is related to exercise intensity in a linear dose-response pattern in young men. 相似文献
95.
Wideman L Weltman JY Patrie JT Bowers CY Shah N Story S Veldhuis JD Weltman A 《American journal of physiology. Regulatory, integrative and comparative physiology》2000,279(4):R1467-R1477
We investigated the ability of exercise, a multipathway, potent, physiological stimulus for GH release, to alter the synergistic interaction of L-arginine (A) and GH-related peptide (GHRP)-2 (G) observed at rest and the ability of gender to further modulate this putative interaction. Subjects (9 men and 9 early follicular phase women) completed 30 min of constant load aerobic exercise in combination with intravenous infusions of saline (S), A (30 g over 30 min), G (1 microg/kg bolus), or both (AG) in separate study sessions in randomly assigned order. Measures of GH release were logarithmically transformed for statistical analysis. Similar to rest, exercise maintained the rank order (AG > G > A > S) of effective stimulation of GH release for the key response measures in men or women, a gender disparity in the time to reach the maximal serum GH concentration, the calculated endogenous GH half-life, and the observed effect of preinfusion (basal) serum GH concentrations on determining secretagogue responsiveness. Exercise potentiated the individual stimulatory actions of A and G, while blunting the relative magnitude of the synergistic (supra-additive) interaction observed at rest. We infer from the present data that 1) exercise is likely to induce release of both GHRH and somatostatin, 2) L-arginine may facilitate the effect of exercise by limiting somatostatin release, 3) GHRP-2 could further enhance the stimulatory impact of exercise by opposing central actions of somatostatin and/or heightening endogenous GHRH release, and 4) gender strongly controls the relative but not absolute magnitude of A/G synergy both at rest and after exercise. 相似文献
96.
Markéta Petrů Jeremy Wideman Kristoffer Moore Felicity Alcock Tracy Palmer Pavel Doležal 《BMC biology》2018,16(1):141
Background
Bacteria and mitochondria contain translocases that function to transport proteins across or insert proteins into their inner and outer membranes. Extant mitochondria retain some bacterial-derived translocases but have lost others. While BamA and YidC were integrated into general mitochondrial protein transport pathways (as Sam50 and Oxa1), the inner membrane TAT translocase, which uniquely transports folded proteins across the membrane, was retained sporadically across the eukaryote tree.Results
We have identified mitochondrial TAT machinery in diverse eukaryotic lineages and define three different types of eukaryote-encoded TatABC-derived machineries (TatAC, TatBC and TatC-only). Here, we investigate TatAC and TatC-only machineries, which have not been studied previously. We show that mitochondria-encoded TatAC of the jakobid Andalucia godoyi represent the minimal functional pathway capable of substituting for the Escherichia coli TatABC complex and can transport at least one substrate. However, selected TatC-only machineries, from multiple eukaryotic lineages, were not capable of supporting the translocation of this substrate across the bacterial membrane. Despite the multiple losses of the TatC gene from the mitochondrial genome, the gene was never transferred to the cell nucleus. Although the major constraint preventing nuclear transfer of mitochondrial TatC is likely its high hydrophobicity, we show that in chloroplasts, such transfer of TatC was made possible due to modifications of the first transmembrane domain.Conclusions
At its origin, mitochondria inherited three inner membrane translocases Sec, TAT and Oxa1 (YidC) from its bacterial ancestor. Our work shows for the first time that mitochondrial TAT has likely retained its unique function of transporting folded proteins at least in those few eukaryotes with TatA and TatC subunits encoded in the mitochondrial genome. However, mitochondria, in contrast to chloroplasts, abandoned the machinery multiple times in evolution. The overall lower hydrophobicity of the Oxa1 protein was likely the main reason why this translocase was nearly universally retained in mitochondrial biogenesis pathways.97.
Jeremy G. Wideman Sebastian W. K. Lackey Martin A. Srayko Kacie A. Norton Frank E. Nargang 《PloS one》2013,8(8)
The endoplasmic reticulum mitochondria encounter structure (ERMES) tethers the ER to mitochondria and contains four structural components: Mmm1, Mdm12, Mdm10, and Mmm2 (Mdm34). The Gem1 protein may play a role in regulating ERMES function. Saccharomyces cerevisiae and Neurospora crassa strains lacking any of Mmm1, Mdm12, or Mdm10 are known to show a variety of phenotypic defects including altered mitochondrial morphology and defects in the assembly of β-barrel proteins into the mitochondrial outer membrane. Here we examine ERMES complex components in N. crassa and show that Mmm1 is an ER membrane protein containing a Cys residue near its N-terminus that is conserved in the class Sordariomycetes. The residue occurs in the ER-lumen domain of the protein and is involved in the formation of disulphide bonds that give rise to Mmm1 dimers. Dimer formation is required for efficient assembly of Tom40 into the TOM complex. However, no effects are seen on porin assembly or mitochondrial morphology. This demonstrates a specificity of function and suggests a direct role for Mmm1 in Tom40 assembly. Mutation of a highly conserved region in the cytosolic domain of Mmm1 results in moderate defects in Tom40 and porin assembly, as well as a slight morphological phenotype. Previous reports have not examined the role of Mmm2 with respect to mitochondrial protein import and assembly. Here we show that absence of Mmm2 affects assembly of β-barrel proteins and that lack of any ERMES structural component results in defects in Tom22 assembly. Loss of N. crassa Gem1 has no effect on the assembly of these proteins but does affect mitochondrial morphology. 相似文献
98.
RD Calixto R Verlengia AH Crisp TB Carvalho MD Crepaldi AA Pereira AK Yamada GR da Mota CR Lopes 《Biology of sport / Institute of Sport》2014,31(4):289-294
This study aimed to compare the effects of different velocities of eccentric muscle actions on acute blood lactate and serum growth hormone (GH) concentrations following free weight bench press exercises performed by resistance-trained men. Sixteen healthy men were divided into two groups: slow eccentric velocity (SEV; n = 8) and fast eccentric velocity (FEV; n = 8). Both groups performed four sets of eight eccentric repetitions at an intensity of 70% of their one repetition maximum eccentric (1RMecc) test, with 2-minute rest intervals between sets. The eccentric velocity was controlled to 3 seconds per range of motion for SEV and 0.5 seconds for the FEV group. There was a significant difference (P < 0.001) in the kinetics of blood lactate removal (at 3, 6, 9, 15, and 20 min) and higher mean values for peak blood lactate (P = 0.001) for the SEV group (9.1 ± 0.5 mM) compared to the FEV group (6.1 ± 0.4 mM). Additionally, serum GH concentrations were significantly higher (P < 0.001) at 15 minutes after bench press exercise in the SEV group (1.7 ± 0.6 ng · mL−1) relative to the FEV group (0.1 ± 0.0 ng · mL−1). In conclusion, the velocity of eccentric muscle action influences acute responses following bench press exercises performed by resistance-trained men using a slow velocity resulting in a greater metabolic stress and hormone response. 相似文献
99.
100.