Abstract: The present invention provides both a method and means for regulating I?B? degradation, NF?B activity, and NF?B-dependent gene expression within living cells, tissues, and organs in-situ. The selective regulation is performed using native PR-39 peptide or one of its shorter-length homologs, for interaction with such I?B? and proteasomes as are present in the cytoplasm of viable cells. The result of PR-39 peptide interaction with I?B? is a selective alteration in the intracellular proteolytic activity of proteasomes, which in turn, causes a reduction of I?B?, a decrease of NF?B activity, and a down-regulation of NF?B-dependent gene expression.

Abstract: The present invention provides both a method and means for regulating angiogenesis within living cells, tissues, and organs in-situ. The regulation is performed using native PR-39 peptide or one of its shorter-length homologs, for direct interaction with the ?7 subunit of such proteasomes as one present in the cytoplasm of viable cells. The result of PR-39 peptide interaction with proteasomes is a decrease in the intracellular degradation of active peptides such as HIF-1? and a consequential stimulation of angiogenesis in-situ.

Abstract: The present invention provides both a method and means for regulating I?B? degradation, NF?B activity, and NF?B-dependent gene expression within living cells, tissues, and organs in-situ. The selective regulation is performed using native PR-39 peptide or one of its shorter-length homologs, for interaction with such I?B? and proteasomes as are present in the cytoplasm of viable cells. The result of PR-39 peptide interaction with I?B? is a selective alteration in the intracellular proteolytic activity of proteasomes, which in turn, causes a reduction of I?B?, a decrease of NF?B activity, and a down-regulation of NF?B-dependent expression.

Abstract: The present invention provides both a method and means for regulating I?B? degradation, NF?B activity, and NF?B-dependent gene expression within living cells, tissues, and organs in-situ. The selective regulation is performed using native PR-39 peptide or one of its shorter-length homologs, for interaction with such I?B? and proteasomes as are present in the cytoplasm of viable cells. The result of PR-39 peptide interaction with I?B? is a selective alteration in the intracellular proteolytic activity of proteasomes, which in turn, causes a reduction of I?B?, a decrease of NF?B activity, and a down-regulation of NF?B-dependent gene expression.

Abstract: The present invention provides both a method and means for regulating I&kgr;B&agr; degradation, NF&kgr;B activity, and NF&kgr;B-dependent gene expression within living cells, tissues, and organs in-situ. The selective regulation is performed using native PR-39 peptide or one of its shorter-length homologs, for interaction with such I&kgr;B&agr; and proteasomes as are present in the cytoplasm of viable cells. The result of PR-39 peptide interaction with I&kgr;B&agr; is a selective alteration in the intracellular proteolytic activity of proteasomes, which in turn, causes a reduction of I&kgr;B&agr;, a decrease of NF&kgr;B activity, and a down-regulation of NF&kgr;B-dependent gene expression.