Abstract
Activation of plasminogen (plg) to plasmin by the staphylococcal activator, staphylokinase (SAK), is effectively regulated by the circulating inhibitor, alpha2-antiplasmin (alpha2AP). Here it is demonstrated that intact Staphylococcus aureus cells and solubilized staphylococcal cell wall proteins not only protected SAK-promoted plg activation against the inhibitory effect of alpha2AP but also enhanced the activation. The findings suggest that the surface-associated plg activation by SAK may have an important physiological function in helping staphylococci in tissue dissemination. Amino acid sequencing of tryptic peptides originating from the 59-, 56- and 43-kDa proteins, isolated as putative plg-binding proteins, identified them as staphylococcal inosine 5'-monophosphate dehydrogenase, alpha-enolase, and ribonucleotide reductase subunit 2, respectively.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antifibrinolytic Agents / pharmacology
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Bacterial Proteins / metabolism*
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Cell Wall / chemistry
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Cell Wall / metabolism
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Enzyme Activation / physiology
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Fibrinolysin / antagonists & inhibitors
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Fibrinolysin / metabolism
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IMP Dehydrogenase / isolation & purification
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IMP Dehydrogenase / metabolism
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IMP Dehydrogenase / pharmacology
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Metalloendopeptidases / metabolism*
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Molecular Sequence Data
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Phosphopyruvate Hydratase / metabolism
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Plasminogen / metabolism*
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Ribonucleotide Reductases / isolation & purification
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Ribonucleotide Reductases / metabolism
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Ribonucleotide Reductases / pharmacology
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Staphylococcus aureus / metabolism*
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alpha-2-Antiplasmin / pharmacology*
Substances
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Antifibrinolytic Agents
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Bacterial Proteins
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alpha-2-Antiplasmin
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Plasminogen
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IMP Dehydrogenase
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Ribonucleotide Reductases
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Fibrinolysin
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Metalloendopeptidases
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auR protein, Staphylococcus aureus
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Phosphopyruvate Hydratase