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Molecular Biology Reports - Metabolic syndrome is an agglomeration of disorders including obesity, diabetes and cardiovascular diseases and characterized as chronic mild inflammation which elevates... 相似文献
144.
Mutational Analysis of the Human Immunodeficiency Virus Type 1 Vpu Transmembrane Domain That Promotes the Enhanced Release of Virus-Like Particles from the Plasma Membrane of Mammalian Cells 总被引:3,自引:3,他引:0
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Mousumi Paul Suparna Mazumder Nicholas Raja M. Abdul Jabbar 《Journal of virology》1998,72(2):1270-1279
Human immunodeficiency virus type 1 Vpu is a multifunctional phosphoprotein composed of the N-terminal transmembrane (VpuTM) and C-terminal cytoplasmic domains. Each of these domains regulates a distinct function of the protein; the transmembrane domain is critical in virus release, and phosphorylation of the cytoplasmic domain is necessary for CD4 proteolysis. We carried our experiments to identify amino acids in the VpuTM domain that are important in the process of virus-like particle (VLP) release from HeLa cells. VLPs are released from the plasma membrane of HeLa cells at constitutive levels, and Vpu expression enhanced the release of VLPs by a factor of 10 to 15. Deletion of two to five amino acids from both N- and C-terminal ends or the middle of the VpuTM domain generated mutant Vpu proteins that have lost the ability to enhance VLP release. These deletion mutants have not lost the ability to associate with the wild-type or mutant Vpu proteins and formed complexes with equal efficiency. They were also transported normally to the Golgi complex. Furthermore, a Vpu protein having the CD4 transmembrane and Vpu cytoplasmic domains was completely inactive, and Vpu proteins harboring hybrid Vpu-CD4 TM domains were also defective in the ability to enhance the release of VLPs. When tested for functional complementation in cotransfected cells, two inactive proteins were not able to reconstitute Vpu activity that enhances the release of Gag particles. Coexpression of functional CD4/Vpu hybrids or wild-type Vpu with inactive mutant CD4/Vpu proteins revealed that mutations in the VpuTM domain could dominantly interfere with Vpu activity in Gag release. Taken together, these results demonstrated that the structural integrity of the VpuTM domain is critical for Vpu activity in the release of VLPs from the plasma membrane of mammalian cells. 相似文献
145.
Rita Sikdar Uma Ganguly Pratima Pal Barsanjit Mazumder Parimal C. Sen 《Molecular and cellular biochemistry》1991,103(2):121-130
The goat spermatozoa membranes isolated after treatment with octa (ethylene glycol) mono n-dodecyl ether (C12E8) followed by discontinuous sucrose density gradient centrifugation have been found to contain an ATPase that is stimulated by externally added Ca2+ only. The membrane fraction has also found to contain Mg2+-dependent Ca2+-ATPase activity, however the former activity is about 2 fold higher than the latter. The molecular weight of the enzyme is found to be about 97,000 on SDS-polyacrylamide gel. The optimum concentration of Ca2+ required for maximum activity is 3 mM for both Mg2+-dependent and Mg2+-independent Ca2+-ATPase. Histidine and imidazole buffers are found to be the most suitable for dependent and independent enzyme activities respectively. ATP with an optimum concentration of 4 mM is observed to be the best substrate than any other nucleotides. The inhibitors like trifluoperazine and vanadate and group specific probes e.g. DTNB and TNBS inhibit these two enzymes but at different rates. Ca2+-uptake study shows that the uptake in the presence of Ca2+ and ATP is higher than in the presence of Mg2+, Ca2+ and ATP. The findings lead us to believe that the Mg2+-independent Ca2+-ATPase has some role in Ca2+ transport like Mg2+-dependent enzyme.Abbreviations Tris
Tris (hydroxymethyl) amino ethane
- Hepes-N
2-hydroxy ethyl piperizine-N1-2-ethane sulfonic acid
- Pipes-Piperizine-N
N1-bis(2-ethane sulfonic acid)
- EGTA
Ethylene Glycol-bis (-amino ethyl ether)
- N, N, N1, N1
Tetraacetic Acid, sodium salt
- TFP
Trifluoperazine
- DTNB
5,51 Dithiobis (2 nitrobenzoic acid)
- TNBS
2, 4, 6-Trinitrobenzene Sulfonate
- C12E8
Octa (ethylene glycol) mono n-dodecyl ether
- PMSF
Phenylmethyl Sulfonyl Fluoride
- PAGE
Polyacrylamide Gel Electrophoresis
- PME
-Mercapto Ethanol 相似文献
146.
Mazumder Amitabha Grimm Elizabeth A. Rosenberg Steven A. 《Cancer immunology, immunotherapy : CII》1983,16(1):1-10
Cancer Immunology, Immunotherapy - We have previously demonstrated that cancer patients' peripheral blood lymphocytes (PBL) allosensitized against single or pool normal donor PBL are capable of... 相似文献
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In view of the importance of Pi in the control of cell metabolism, it was of interest to study the mechanism and regulation of Pi uptake by ascites tumor cells. For this purpose, the incorporation of 32Pi into Ehrlich Lettré cells was compared when competitive anions and inhibitors which alter cation movements were present. Anions such as sulfanilate (35 mm) and succinate (30 mm) decrease 32Pi uptake by ca. 35%, suggesting that transport is mediated by a protein similar to the 100,000 Mr anion carrier isolated from erythrocyte membranes. Furosemide, a diuretic which bears a structural analogy to sulfanilate inhibitors of anion transport, also decreases 32Pi incorporation at concentrations as low as 2 × 10?5m. This inhibitor blocks cation exchange in ascites tumor cells, and from the present data, it is suggested that a possible function of the furosemidesensitive cation exchange protein is to facilitate anion transport. Ouabain, known to inhibit (Na+ + K+)-ATPase and its dephosphorylation, stimulates the rate of incorporation of 32Pi into cells and also raises the net inorganic phosphate level. The stimulation of 32Pi incorporation is decreased by sulfanilate or succinate. In contrast to the effects of ouabain, addition of 10 mm K+, which is known to stimulate (Na+ + K+)-ATPase and its dephosphorylation, decreases 32Pi incorporation. These observations suggest that anion transport and energy-dependent Na+ and K+ movements may be closely coupled to the intact cell. 相似文献
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Ternary complex formation between eukaryotic initiation factor 2 (eIF-2), initiator Met-tRNA and guanosine 5′-(β, γ-imino) triphosphate [GMP-P(NH)P] is strongly inhibited by mRNA in the system. Developing embryos contain a factor which displays a novel activity, namely the ability to counteract the mRNA-induced inhibition of ternary complex formation. This factor is heat-labile. It is proposed that the factor may play an important role in protein biosynthesis by preventing mRNA from inhibiting an early step of peptide chain initiation. 相似文献