KLKs and their hormone-like signaling actions: a new life for the PSA-KLK family

2014 ◽  
Vol 395 (9) ◽  
pp. 915-929 ◽  
Author(s):  
Morley D. Hollenberg

Abstract Human kallikrein-related peptidases (KLKs), including the well-known prostate cancer biomarker, prostate-specific antigen (PSA-KLK3), along with 14 other serine proteinase KLK family members are now known to regulate cells by cleaving and activating members of the G-protein-coupled proteinase-activated receptor (PAR) family. This hormone-like signaling action of the KLKs has provided a new perspective for understanding the biological roles that KLKs may play in normal and pathophysiological settings. This overview summarizes the circumstances leading up to the discovery of this action of the KLKs and provides an overview of the diverse impact on tissue function that may result from KLK-triggered PAR activation.

1991 ◽  
Vol 37 (9) ◽  
pp. 1618-1625 ◽  
Author(s):  
H Lilja ◽  
A Christensson ◽  
U Dahlén ◽  
M T Matikainen ◽  
O Nilsson ◽  
...  

Abstract Immunologic measurements of the serum concentration of prostate-specific antigen (PSA), an abundant prostatic-secreted serine proteinase, are frequently used to monitor patients with prostate cancer, though it has not been ascertained whether this immunoreactivity represents a PSA zymogen, the active proteinase, or PSA complexed to extracellular proteinase inhibitors. To characterize the PSA immunoreactivity in serum, we used monoclonal antibodies produced against PSA and a polyclonal rabbit IgG against alpha 1-antichymotrypsin in the design of three noncompetitive PSA assays: assay T, which detected PSA both when present as the active proteinase and when complexed to alpha 1-antichymotrypsin; assay F, which recognized the active proteinase but most poorly detected PSA complexed to alpha 1-antichymotrypsin; and assay C, which was specific for PSA complexed to alpha 1-antichymotrypsin. We used the three assays to measure PSA immunoreactivity in 64 patients' sera and in the effluent after gel chromatography of sera from four patients. This identified an 80- to 90-kDa complex between PSA and alpha 1-antichymotrypsin as the predominant fraction of the PSA immunoreactivity in blood plasma; an immunoreactive 25- to 40-kDa compound was the minor fraction.


2017 ◽  
Vol 8 (2) ◽  
pp. 690-700 ◽  
Author(s):  
Pavel Damborský ◽  
Dominika Damborská ◽  
Štefan Belický ◽  
Ján Tkáč ◽  
Jaroslav Katrlík

2008 ◽  
Vol 100 (21) ◽  
pp. 1487-1488 ◽  
Author(s):  
Ian M. Thompson ◽  
Catherine M. Tangen ◽  
Alan R. Kristal

2004 ◽  
Vol 171 (4S) ◽  
pp. 334-334
Author(s):  
Walter J. Simoneaux ◽  
Caleb B. Bozeman ◽  
Brett S. Carver ◽  
Donald A. Elmajian

2004 ◽  
Vol 171 (4S) ◽  
pp. 439-440
Author(s):  
Yoshio Naya ◽  
Herbert A. Fritsche ◽  
Viju A. Bhadkamkar ◽  
Stephen D. Mikolajczyk ◽  
Harry G. Rittenhouse ◽  
...  

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