title: Polyamines as physiological substrates for transglutaminases.
abstract: When normal human blood lymphocytes are treated with mitogen in the presence of [3H]putrescine, label is incorporated into a few cellular proteins. Labeled N-(gamma-glutamyl) putrescine, N1-(gamma-glutamyl)spermidine, and N8-(gamma-glutamyl)spermidine were identified in exhaustive proteolytic digests of the cellular protein fraction. The enzyme-mediated clotting of rat seminal plasma to which 14C-labeled spermidine and spermine are added is accompanied by incorporation of the polyamines into a number of seminal plasma proteins. Proteolytic digests of the protein fraction from this clotted seminal plasma contain labeled N1-(gamma-glutamyl)spermidine, N8-(gamma-glutamyl)spermidine, N1,N8-bis(gamma-glutamyl)spermidine, N1-(gamma-glutamyl)spermine, and N1,N12-bis(gamma-glutamyl)spermine. These findings support a proposal that polyamines serve as substrates for transglutaminases both in cells and in an extracellular fluid. They show differences in cellular and extracellular substrate properties of the polyamines and indicate cross-linking through these amines in the extracellular system, but provide no evidence for such cross-linking in the cells.
mesh_terms: D006801:Humans; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000201:enzymology*; D008297:Male; D008934:Mitogens; D011073:Polyamines / Q000494:pharmacology; D012669:Seminal Vesicles / Q000502:physiology; D013095:Spermidine / Q000097:blood; D013096:Spermine / Q000097:blood; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
chemical_list: D008934:Mitogens; D011073:Polyamines; D013096:Spermine; D005723:gamma-Glutamyltransferase; D013095:Spermidine