title: [Effects of biogenic phosphates on protease-induced protein cleavage and functioning of plasminogen activators].
abstract: We showed, using the method of lysis of fibrin plates and five substrate proteins in a thin layer of agar gel, that inorganic orthophosphate (0.001-0.06 M) enhances by 50-250% the activatory functions of streptokinase, urokinase, and tissue plasminogen activator and, in general, by 1.2-12.0 times enhances protein lysis by trypsin, alpha-chymotrypsin, subtilisin, papain, bacterial metalloprotease, and even pepsin at a concentration < 4 mM. At higher concentrations, phosphate sharply inhibited pepsin activity and inhibited by 40-50% gelatin lysis by papain and gelatin (at a peak concentration) and casein lysis by metalloprotease. Inorganic pyrophosphate ions at concentrations of 10(-8)-10(-1) M enhanced the cleavage of a number of proteins by serine proteases and, at concentrations of 10(-5) -10(-3) M, the activities of pepsin, plasminogen tissue activator, and streptokinase by 100 and 40%, respectively. The pyrophosphate concentrations of > 10(-3) and >10(-4) M inhibited pepsin- and metalloprotease-induced lysis of virtually all proteins. ATP increased casein lysis by serine proteases, metalloprotease, and pepsin by 20-60% at concentration of 10(-3) M and by 30-260% at 10(-2) M concentration. At concentrations of 10-2 M, it inhibited the cleavage of some proteins by trypsin, chymotrypsin, papain, and metalloprotease by 20-100%, and, at concentrations of 10(-3) M, lysis of albumin with pepsin and other proteins (except for fibrinogen) by metalloprotease. A GTP concentration of 10(-7)-10(-2) M increased protein degradation by serine proteases, papain, and gelatin lysis by pepsin by 20-90%, whereas albumin lysis was inhibited by 40-70%. The presence of 10(-6)-10(-5) M GTP led to a slightly increased degradation of hemoglobin and casein by bacterial metalloprotease, while 10(-3) M GTP induced a drop in the activity of the metalloprotease by 20-50%. ADP could enhance gelatin lysis by trypsin, casein lysis by pepsin and papain, and inhibited metalloprotease activity by 20-100% (at 10(-3) M). Peculiarities of the effects of AMP and GD(M)P on gelatin lysis were found.
authors.forename: N S
authors.initials: NS
authors.lastname: Pyzhova
authors.forename: V N
authors.initials: VN
authors.lastname: Nikandrov
mesh_terms: D000818:Animals; D001798:Blood Proteins / Q000737:chemistry*; D002364:Caseins / Q000737:chemistry*; D002417:Cattle; D011756:Diphosphates / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry; D005780:Gelatin / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry; D006801:Humans; D009711:Nucleotides / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry*; D010710:Phosphates / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry; D013552:Swine; D010959:Tissue Plasminogen Activator / Q000737:chemistry
chemical_list: D001798:Blood Proteins; D002364:Caseins; D011756:Diphosphates; D006454:Hemoglobins; D009711:Nucleotides; D010710:Phosphates; D012709:Serum Albumin; D005780:Gelatin; D005340:Fibrinogen; D010447:Peptide Hydrolases; D010959:Tissue Plasminogen Activator