Activity of Aspartate Transcarbamylase in Uninfected and Type 5 Adenovirus-Infected Hela Cells

Consigli, Richard A.; Ginsberg, Harold S.

doi:10.1128/jb.87.5.1034-1043.1964

Cited by 23 publications

(10 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Kit et al showed that the enhancement of thymidine kinase and DNA polymerase activities which occurred in monkey kidney cell cultures infected with simian adenovirus took place when DNA synthesis was stopped (15). On the other hand, the aspartic transcarbamylase activity induced in HeLa cells infected by human adenovirus type 5 did not increase under conditions of DNA synthesis inhibition (5).…”

Section: Discussionmentioning

confidence: 77%

Enhanced Deoxyribonucleic Acid Polymerase Activity in Human Embryonic Kidney Cultures Infected with Adenovirus 2 or 12

Ledinko

1968

J Virol

View full text Add to dashboard Cite

Deoxyribonucleic acid (DNA) polymerase activity was induced at approximately 18 to 20 hr after infection of secondary cultures of human embryonic kidney cells with adenovirus type 2 or type 12, and, at 30 to 50 hr after infection, the activity of this enzyme increased twoto threefold. The activity of thymidine kinase was also induced, but the activity of deoxycytidylic deaminase was not. The DNA content per cell at 71 hr after infection was 1.6-fold greater in adenovirus 2-infected cultures, and approximately 2.4-fold greater in adenovirus 12-infected cultures, than in the noninfected cultures. Several properties of DNA polymerase were studied. The enzymes in normal and adenovirus 2or 12-infected cell extracts were saturated by approximately the same concentration of heat-denatured salmon sperm DNA primer (160 Ag/ml); the enzyme activities had a similar broad pH optimum between 7.5 and 9. Extracts prepared from cells infected by either adenovirus did not activate DNA polymerase from noninfected cells, nor did the noninfected cell extracts inhibit enzyme activity of infected cell extracts. DNA polymerase in both normal and adenovirus 2or 12-infected cells was located predominantly in the nucleus. In each case, the cytoplasm had only 30% of the enzyme activity of the nucleus. At 40 hr after infection with adenovirus 2 or 12, the activities of the enzyme in the nuclear and cytoplasmic fractions increased twoto threefold. Puromycin, an inhibitor of protein synthesis, prevented DNA polymerase induction when added to cultures during the 18to 30-hr postinfection period, and it arrested the additional increase in enzyme activity when added after enzyme induction began. However, the increases in both DNA polymerase and thymidine kinase activities took place after treatment of infected cultures with 1-f3-D-arabinofuranosylcytosine, an inhibitor of DNA synthesis and adenovirus growth.

show abstract

Section: Discussionmentioning

confidence: 77%

Enhanced Deoxyribonucleic Acid Polymerase Activity in Human Embryonic Kidney Cultures Infected with Adenovirus 2 or 12

Ledinko

1968

J Virol

View full text Add to dashboard Cite

show abstract

“…The methods employed for tissue culture, propagation of virus, virus infectivity titrations, preparation of ATCase, and assay of enzyme were identical with those described in the accompanying paper (Consigli and Ginsberg, 1964). When enzyme was utilized for experiments on control mechanisms, all solutions mixed with enzyme contained 10-3 M mercaptoethanol and 10-4 M neutral ethylenediaminetetraacetic acid (EDTA) to protect active sites of the enzyme from reacting with trace heavy metals.…”

Section: Methodsmentioning

confidence: 99%

“…Aspartate transcarbamylase (ATCase) activity increases approximately 10 hr after infection and reaches maximal activity 18 hr after type 5 adenovirus infection of HeLa cells (Consigli and Ginsberg, 1964). The increased ATCase activity is detectable at approximately the time that biosynthesis of virus-precursor deoxyribonucleic acid (DNA) commences Dixon, 1959, 1961; Flanagan and Ginsberg, 1962), and is dependent upon DNA and protein synthesis (Consigli and Ginsberg, 1964). A comparison of the characteristics of ATCase from uninfected and infected HeLa cells indicated that enzyme from infected cells had an altered pH optimum, in-1 Pennsylvania Plan Scholar.…”

mentioning

confidence: 99%

“…That pyrimidines can inhibit increase in ATCase activity in adenovirus-infected cells was demonstrated. To investigate the mechanism of control of enzyme activity in HeLa cells, ATCase was partially purified (Consigli and Ginsberg, 1964), and the effect of end products as inhibitors was determined in vitro. The results of a representative experiment (Table 2) indicate that the cytidine phosphates were effective enzyme inhibitors, and cytidine triphosphate (CTP) was a better inhibitor than either cytidine diphosphate (CDP) or cytidine monophosphate (CMP).…”

mentioning

confidence: 99%

“…Effect of heat on characteristics of A TCase from uninfected and type 5 adenovirus-infected HeLa cells. ATCase from infected cells was reported to have a pH optimum and kinetics significantly different from enzyme extracted from uninfected HeLa cells (Consigli and Ginsberg, 1964). The finding that the activity of ATCase from uninfected cells could be increased by heat suggested that this treatment might alter the pH optimum and the kinetics of this enzyme so that it would be similar to ATCase from virus-infected cells.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Control of Aspartate Transcarbamylase Activity in Type 5 Adenovirus-Infected Hela Cells

Consigli

Ginsberg

1964

J Bacteriol

Self Cite

View full text Add to dashboard Cite

Consigli, Richard A. (University of Pennsylvania, Philadelphia), and Harold S. Ginsberg . Control of aspartate transcarbamylase activity in type 5 adenovirus-infected HeLa cells. J. Bacteriol. 87: 1027–1033. 1964.—Type 5 adenovirus infection induces increased aspartate transcarbamylase (ATCase) activity during the period of magnified nucleic acid biosynthesis. Increased activity can be prevented by addition of pyrimidines to the culture medium. ATCase in HeLa cells is regulated by feedback inhibition, and purified enzyme can be inhibited in vitro by cytidine triphosphate (CTP). The enzyme from infected cells has a pH optimum, maximal velocity, and K m for aspartate distinctly different from ATCase from control cells. However, heating of ATCase from uninfected cells converts the enzyme so that its characteristics are identical with enzyme from infected cells. Conversely, addition of CTP to ATCase from infected cells changes the characteristics of the enzyme so that they are the same as those of enzyme from uninfected cells. The evidence presented suggests that increased nucleic acid biosynthesis in infected cells initiates a release from feedback inhibition and increases ATCase activity by reducing the concentration of pyrimidines and purines in the acid-soluble pool.

show abstract

RNA and DNA Metabolism in Aging Cultured Cells

Michl

Svobodová

1970

Aging in Cell and Tissue Culture

View full text Add to dashboard Cite

Activity of Aspartate Transcarbamylase in Uninfected and Type 5 Adenovirus-Infected Hela Cells

Cited by 23 publications

References 28 publications

Enhanced Deoxyribonucleic Acid Polymerase Activity in Human Embryonic Kidney Cultures Infected with Adenovirus 2 or 12

Enhanced Deoxyribonucleic Acid Polymerase Activity in Human Embryonic Kidney Cultures Infected with Adenovirus 2 or 12

Control of Aspartate Transcarbamylase Activity in Type 5 Adenovirus-Infected Hela Cells

RNA and DNA Metabolism in Aging Cultured Cells

Contact Info

Product

Resources

About