scholarly journals RNA and protein synthesis in human peripheral blood polymorphonuclear leukocytes.

1979 ◽  
Vol 149 (1) ◽  
pp. 284-289 ◽  
Author(s):  
A Granelli-Piperno ◽  
J D Vassalli ◽  
E Reich
Keyword(s):  
Protein Synthesis ◽  
Peripheral Blood ◽  
Gel Electrophoresis ◽  
Polymorphonuclear Leukocytes ◽  
Cultured Cells ◽  
Human Peripheral Blood ◽  
Polyacrylamide Gel Electrophoresis ◽  
Con A ◽  
Rna And Protein Synthesis ◽  
Polypeptide Chains

Polymorphonuclear leukocytes purified from human peripheral blood synthesized RNA and proteins when placed in cell culture. Autoradiography of the cultured cells revealed that a majority of mature PMNs were engaged in macromolecule synthesis, and an analysis of newly synthesized proteins by SDS-polyacrylamide gel electrophoresis showed that many different polypeptide chains were synthesized by these cells. The rate of [3H]uridine incorporation and the pattern of newly synthesized proteins were modulated by Con A and glucocorticoids. These results suggest that in spite of their short lifetime and a large performed enzymatic apparatus, mature PMNs retain a substantial capacity for RNA and protein synthesis; and, further, that modulation of macromolecule synthesis forms part of the mechanism by which PMNs respond to inflammatory and anti-flammatory stimuli.

scholarly journals Effects of glutathione-oxidizing agents on microtubule assembly and microtubule-dependent surface properties of human neutrophils.

1976 ◽  
Vol 71 (3) ◽  
pp. 921-932 ◽  
Author(s):  
J M Oliver ◽  
D F Albertini ◽  
R D Berlin
Keyword(s):  
Concanavalin A ◽  
Peripheral Blood ◽  
Polymorphonuclear Leukocytes ◽  
Human Peripheral Blood ◽  
Microtubule Assembly ◽  
Human Neutrophils ◽  
Hexose Monophosphate ◽  
Con A ◽  
Oxidizing Agents ◽  
The Face

In human peripheral blood polymorphonuclear leukocytes and lymphocytes, GSH-oxidizing agents promote the movement of surface-bound concanavalin A (Con A) into caps and inhibit the assembly of microtubules (MT) that is normally induced by Con A binding. Con A capping and inhibition of MT assembly occur when GSH levels in cell suspensions are decreased by 30-70%, and return to GSH to control levels is accompanied by the appearance of cytoplasmic MT and by inhibition of the capping response with Con A. Oxidation of GSH markedly stimulates the hexose monophosphate shunt, and regeneration of GSH occurs rapidly. The data indicate that MT cannot be assembled or maintained in the face of decreased GSH levels. Thus, GSH homeostasis becomes critical during physiological events such as phagocytosis which simultaneously induce the assembly of MT and the production of agents like H2O2 that can oxidize GSH.

Partial characterization of an abnormal lactate dehydrogenase isoenzyme, LDH-1ex, in serum from a patient with hepatocellular carcinoma.

1989 ◽  
Vol 35 (5) ◽  
pp. 844-848
Author(s):  
D L Kalpaxis ◽  
E E Giannoulaki
Keyword(s):  
Hepatocellular Carcinoma ◽  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Heat Stable ◽  
Single Polypeptide ◽  
Polypeptide Chains

Abstract Serum from a patient with hepatocellular carcinoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), LDH-1ex, that on electrophoresis on 10-g/L agarose gel migrated anodally to the LDH-1 band. This isoenzyme was partly purified by ultrafiltration and preparative electrophoresis. Gel chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis studies of the resulting LDH-1ex preparation suggested that this isoenzyme is probably a tetramer made up of four single polypeptide chains (monomers), each having a molecular mass of about 32,000 Da. LDH-1ex was heat stable and reacted more readily with 2-hydroxybutyrate than did the slower migrating LDH-4 and LDH-5 isoenzymes. LDH-1ex showed no activity when lactate was omitted from the substrate solution or replaced by ethanol.

Urease. X. A study by gel electrophoresis of its dissociation by sodium dodecyl sulfate

1969 ◽  
Vol 47 (10) ◽  
pp. 989-991 ◽  
Author(s):  
D. P. Blattler ◽  
George Gorin
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Disulfide Bonds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Dodecyl Sulfate ◽  
Polypeptide Chains

Urease, m.w. 480 000, treated with an excess of sodium dodecyl sulfate is converted to a product of greatly increased mobility in polyacrylamide gel electrophoresis. We estimate its weight to be about 80 000. Treatment with excess thiol and detergent yielded the same product as detergent alone, indicating that the subunit or subunits do not contain polypeptide chains linked by disulfide bonds.

Effect of enucleation on protein synthesis during maturation of bovine oocytes in vitro

1997 ◽  
Vol 9 (6) ◽  
pp. 603 ◽  
Author(s):  
J. C. Bell ◽  
L. C. Smith ◽  
R. Rumpf ◽  
A. K. Goff
Keyword(s):  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Germinal Vesicle ◽  
Uv Exposure ◽  
One Dimensional ◽  
Repair Mechanisms ◽  
Bovine Oocytes

The role of the nucleus in protein synthesis reprogramming during oocyte maturation was examined in immature or mature bovine oocytes, enucleated at the germinal vesicle (GV) stage or the metaphase II (MII) stage. Cumulusoocyte complexes (COCs) were denuded before or after maturationin vitro. Denuded oocytes were (i) enucleated at the GV or MII stage (after DNA staining and ultraviolet (UV) exposure), (ii) stained and exposed to UV but not enucleated, or (iii) used as controls. After treatment, oocytes were labelled for 4 h with35S-methionine or were matured for 24 h before labelling. GV- or MII- karyoplasts and small portions of cytoplasm (cytoplasts), removed during enucleation, were also labelled. Labelled oocytes, karyoplasts or cytoplasts were prepared for one-dimensional polyacrylamide gel electrophoresis. Incorporation of labelled methionine into oocyte protein was measured. Enucleation did not affect protein synthesis reprogramming, but incorporation of 35S-methionine in immature UV-stained oocytes was high-possibly due to nuclear repair mechanisms. Protein proles of GV- and MII- karyoplasts differed from those of immature and mature oocytes. In conclusion, normal protein synthesis reprogramming in the cytoplasm can occur in the absence of the nucleus, and specic proteins are synthesized in the nuclear region.

Effects of Auxin-Like Herbicides on Nucleohistones in Cucumber and Wheat Roots

Weed Science ◽  
1973 ◽  
Vol 21 (3) ◽  
pp. 181-184 ◽  
Author(s):  
L. G. Chen ◽  
A. Ali ◽  
R. A. Fletcher ◽  
C. M. Switzer ◽  
G. R. Stephenson
Keyword(s):  
Triticum Aestivum ◽  
Protein Synthesis ◽  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Wheat Roots ◽  
Anisic Acid ◽  
Cucumber Roots ◽  
Dichlorophenoxy Acetic Acid ◽  
Dna Template

Roots of susceptible cucumber (Cucumis sativusL. ‘Chicago pickling’) and tolerant wheat (Triticum aestivumL. ‘Manitou’) seedlings were treated with 3,6-dichloro-o-anisic acid (dicamba) or (2,4-dichlorophenoxy)acetic acid (2,4-D) for either 10 or 46 hr. The roots were excised and nucleohistones were isolated and fractionated by polyacrylamide gel electrophoresis. In untreated cucumber roots there were four major nucleohistone fractions. Two of these fractions decreased or were not detectable 10 or 46 hr after treatment with dicamba or 2,4-D. In wheat, the nucleohistone fractions of the treated roots were similar to those of the controls. This suggests that in cucumber more of the DNA template is available for transcription. This suggestion was supported by the fact that the incorporation of14C-adenine into RNA in cucumber roots 10 hr after treatment with dicamba was increased by 50%, whereas in wheat there was no difference. Furthermore, the incorporation of14C-leucine into protein in cucumber roots 10 hr after treatment with dicamba was inhibited by 70%, indicating that the increased RNA produced was incapable of translating for protein synthesis. It is proposed that selective phytotoxicity of auxin-like herbicides is based on a differential alteration of RNA species and interference with protein synthesis.

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