Abstract: The present invention provides methods for stimulating mu-opioid receptors with agonist peptides in a mammal in need thereof. The methods comprise administering to the mammal an effective amount of a selective mu-opioid receptor agonist peptide that comprises at least two ?-amino acid residues. At least one of the amino acid residues has a positive charge. The amino acid residue in the first position is a tyrosine or tyrosine derivative. The amino acid in the second position is a D-?-amino acid. The present invention also provides methods of treating a mammal suffering from conditions or diseases by administering to the mammal an effective amount of the peptides.

Abstract: The present invention provides methods for stimulating a mu-opioid receptor agonist peptide in a mammal in need thereof. The methods comprise administering to the mammal an effective amount of a selective mu-opioid receptor agonist peptide that comprises at least two ?-amino acid residues. At least one of the amino acid residues has a positive charge. The amino acid residue in the first position is a tyrosine or tyrosine derivative. The amino acid in the second position is a D-?-amino acid. The present invention also provides methods of treating a mammal suffering from conditions or diseases by administering to the mammal an effective amount of the peptides.

Abstract: The present invention relates to the cloning of human pro-protein converting enzyme 5 (PC5) CDNA isolated from human adrenal gland messenger RNA. Additionally, this invention relates to a method for reducing restenosis occurring at an injured vascular site comprising delivering to the injured site an antisense nucleic acid to suppress the expression of human PC5.

Abstract: This invention relates to a novel and seventh member of the subtilisin-kexin family isolated from rat, which has been named rPC7. The rat spleen cDNA has been totally sequenced. A shorter DNA sequence has been obtained for human, which corresponds to a portion of the catalytic region of a human pro-hormone convertase corresponding to the rat pro-hormone convertase. PC7 clearly distinguishes from the other mammalian members of the subtilisin-kexin family. Its tissue distribution is ubiquitous, but its presence is particularly remarkable in lymphoid tissues. It is present in LoVo cells that are able to cleave the HIV gp160 protein into active gp120/gp41 proteins and that are deficient in other effective pro-hormone convertases known up to date. Therefore, it is proposed that PC7 is a good candidate as a maturation enzyme responsible for the conversion of HIV gp160 protein in target CD.sup.+4 cells.