The dipeptidyl peptidase IV family in cancer and cell biology.
Of the 600+ known proteases identified to date in mammals, a significant percentage is involved or implicated in pathogenic and cancer processes. The dipeptidyl peptidase IV (DPIV) gene family, comprising four enzyme members [DPIV (EC 3.4.14.5), fibroblast activation protein, DP8 and DP9] and two nonenzyme members [DP6 (DPL1) and DP10 (DPL2)], are interesting in this regard because of their multiple diverse functions, varying patterns of distribution/localization and subtle, but significant, differences in structure/substrate recognition. In addition, their engagement in cell biological processes involves both enzymatic and nonenzymatic capabilities. This article examines, in detail, our current understanding of the biological involvement of this unique enzyme family and their overall potential as therapeutic targets.
Yu
Denise M T
DM
AW Morrow Gastroenterology and Liver Centre, Royal Prince Alfred Hospital, University of Sydney, Sydney, Australia.
Yao
Tsun-Wen
TW
Chowdhury
Sumaiya
S
Nadvi
Naveed A
NA
Osborne
Brenna
B
Church
W Bret
WB
McCaughan
Geoffrey W
GW
Gorrell
Mark D
MD
D000818:Animals; D014408:Biomarkers, Tumor / Q000145:classification; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D004195:Disease Models, Animal; D016503:Drug Delivery Systems; D006801:Humans; D008958:Models, Molecular; D009369:Neoplasms / Q000188:drug therapy / Q000201:enzymology* / Q000235:genetics* / Q000276:immunology
D014408:Biomarkers, Tumor; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases