ABSTRACT
Seminal vesicle protein 4 (SV-IV) is a highly flexible molecule that in aqueous solution behaves as a concentration-dependent self-associating system in which the degree of association (monomer <--> dimer <--> trimer equilibrium) seems to be related to its biological activities. This review reports the functional role of SV-IV in seminal clotting exerted through the modulation of inflammation, hemostasis, and sperm protection against the damage induced by immunological or reactive oxygen species during the long journey of spermatozoa in the female genital tract.
Subject(s)
Peptides/immunology , Semen/immunology , Seminal Vesicle Secretory Proteins/immunology , Animals , Female , Hemostasis/immunology , Humans , Inflammation/immunology , Inflammation/metabolism , Male , Peptides/genetics , Peptides/metabolism , Protein Conformation , Reactive Oxygen Species/immunology , Reactive Oxygen Species/metabolism , Semen/chemistry , Semen/metabolism , Seminal Vesicle Secretory Proteins/chemistry , Seminal Vesicle Secretory Proteins/metabolism , Spermatozoa/immunology , Spermatozoa/metabolism , Structure-Activity RelationshipABSTRACT
In the present study, we have utilized the transglutaminase (TGase) enzyme to modify the primary structure of VIP with diaminopropane (DAP) at the level of the Gln16. We have investigated the conformational stability of VIP and VIP-DAP in solution by limited proteolysis experiments. The VIP-DAP appears to be more resistant to the proteolytic attack of trypsin, thus indicating that the derivatization in position 16 is able to stabilize the structure of the peptide. However, we have studied their role in cell cycle modulation and antioxidant activity in the oropharyngeal epidermoid carcinoma KB cells.
