1974
DOI: 10.1016/0014-4827(74)90489-3
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Suppressive effect of protease inhibitors on heterokaryons containing chick erythrocyte nuclei

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Cited by 14 publications
(5 citation statements)
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“…The first protein peak, eluted with starting buffer, contained neutral proteinases active towards casein at pH 7.5 (fractions 10-15), and acid proteinases active towards hemoglobin at pH 3.5 (fractions [14][15][16][17][18][19][20][21][22][23][24][25]. After the gradient elution started the second protein peak appeared at 0.15 M NaC1, possessing only neutral proteinase activity (casein pH 7.5).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The first protein peak, eluted with starting buffer, contained neutral proteinases active towards casein at pH 7.5 (fractions 10-15), and acid proteinases active towards hemoglobin at pH 3.5 (fractions [14][15][16][17][18][19][20][21][22][23][24][25]. After the gradient elution started the second protein peak appeared at 0.15 M NaC1, possessing only neutral proteinase activity (casein pH 7.5).…”
Section: Resultsmentioning
confidence: 99%
“…There are now several reports dealing with neutral proteinases and inhibitors of these proteinases, since they are thought to be involved in a number of diseases, involving blood-clotting [15,16], inflammation and allergic states [17], emphysema [18], carcinoma [19], diseases of connective tissue [20] and collagen metabolism [2] and finally in protein synthesis [21]. It has been known that neutral proteinases are located in so-called azurophil granules [22].…”
Section: Discussionmentioning
confidence: 99%
“…The fact that at least some of the globin synthesized early after transplantation was translated from preexisting mRNA was also supported by data showing that early synthesis was at least partially refractory to actinomycin D. The interpretation of such results is, however, tenuous since the precise effects of the drug on the partially decondensed chromatin present in reactivating nuclei is undetermined. In fact, chicken erythrocyte chromatin is apparently unique in that it does not vary in its ability to bind actinomycin D throughout either condensation occurring during normal development or decondensation after nuclear reactivation (15,31). Furthermore, it has also been shown that actinomycin D can inhibit the rate of initiation of polypeptide synthesis (14) and that low levels of the drug result in an accumulation of globin mRNA in murine erythroleukemia cells (56).…”
Section: Methodsmentioning
confidence: 99%
“…In addition, TLCK has been shown to inhibit protein synthesis in poliovirusinfected HeLa cells (21) and RNA synthesis in lymphocytes (26) in the concentration range (1 X 10-4 M) previously reported (14) to selectively inhibit the growth of SV40-transformed cells. Thus, TLCK may also cause growth inhibition via inhibition of macromolecular synthesis rather than by inhibiting cellular proteases.…”
mentioning
confidence: 98%
“…The mechanism by which TPCK inhibits protein synthesis in mammalian cells is not known; it may inactivate one of the peptide chain elongation factors in protein synthesis as it does in bacteria (24,25), and (or) it may act by inhibiting cellular RNA synthesis (26) which is required for protein synthesis. Whatever the mechanism, the growth inhibitory effects of TPCK can no longer simply be ascribed to inhibition of proteolytic activity.…”
mentioning
confidence: 99%