Janita Lövgren

TL;DR: A peptide sequence with a high degree of specificity for PSA is identified and improved K(m)s and k(cat)s over previously used substrates are determined and it should be possible to use the HSSKLQ peptide as a carrier to target peptide-coupled prodrugs for selective activation within sites of PSA-secreting, metastatic prostate cancer cells and not within the blood or other nonprostatic normal tissues.

TL;DR: Results indicate that hK2 is responsible for the activation of proPSA, a finding that may be very important for understanding of the role of these two kallikreins in the reproductive system and in prostate cancer biology.

TL;DR: Measurements show that in addition to the previously known secretion in seminal plasma, hK2 is secreted in amniotic fluid, breast milk, and saliva, suggesting that the two proteases might form a functional unit but not always as demonstrated by the sole presence of h kallikrein 2 in saliva.

TL;DR: The enzymatic activity of hK2 is likely to be reversibly regulated by Zn2+ in prostatic fluid and regulation may be impaired in CAP and advanced metastatic cancer resulting in lack of control of the hK1 activity and a need for other means of control.

TL;DR: A novel immunofluorometric MAb-MAb assay for the specific detection of hK2 was designed, designed to prevent both free and complexed PSA from reacting in subsequent immunoreactions.