scholarly journals Crystal Structures of HIV-1 Tat-derived Nonapeptides Tat-(1–9) and Trp2-Tat-(1–9) Bound to the Active Site of Dipeptidyl-peptidase IV (CD26)

2005 ◽  
Vol 280 (15) ◽  
pp. 14911-14917 ◽  
Author(s):  
Wilhelm Andreas Weihofen ◽  
Jianguo Liu ◽  
Werner Reutter ◽  
Wolfram Saenger ◽  
Hua Fan
Keyword(s):  
Crystal Structures ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Hiv 1

scholarly journals Crystal Structures of Human Dipeptidyl Peptidase IV in its Apo and Diprotin B-complexed Forms

2007 ◽  
Vol 39 (5) ◽  
pp. 335-343 ◽  
Author(s):  
Hajime HIRAMATSU ◽  
Kiyoshi KYONO ◽  
Atsushi YAMAMOTO ◽  
Kazuhiko SAEKI ◽  
Hideaki SHIMA ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv

Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist

Blood ◽  
2000 ◽  
Vol 96 (5) ◽  
pp. 1674-1680 ◽  
Author(s):  
Paul Proost ◽  
Patricia Menten ◽  
Sofie Struyf ◽  
Evemie Schutyser ◽  
Ingrid De Meester ◽  
...  
Keyword(s):  
Mononuclear Cells ◽  
Specific Activity ◽  
High Capacity ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Surface Glycoprotein ◽  
Peripheral Blood Mononuclear ◽  
Dpp Iv ◽  
Stromal Cell Derived Factor ◽  
Hiv 1

Abstract Chemokines are proinflammatory cytokines that play a role in leukocyte migration and activation. Recent reports showed that RANTES (regulated on activation normal T-cell expressed and secreted chemokine), eotaxin, macrophage-derived chemokine (MDC), and stromal cell–derived factor-1 (SDF-1) are NH2-terminally truncated by the lymphocyte surface glycoprotein and protease CD26/dipeptidyl peptidase IV (CD26/DPP IV). Removal of the NH2-terminal dipeptide resulted in impaired inflammatory properties of RANTES, eotaxin, MDC, and SDF-1. The potential CD26/DPP IV substrate macrophage inflammatory protein–1β (MIP-1β) and the related chemokine, LD78α (ie, one of the MIP-1α isoforms), were not affected by this protease. However, CD26/DPP IV cleaved LD78β, a most potent CCR5 binding chemokine and inhibitor of macrophage tropic human immunodeficiency virus–1 (HIV-1) infection, into LD78β(3-70). Naturally truncated LD78β(3-70), but not truncated MIP-1β, was recovered as an abundant chemokine form from peripheral blood mononuclear cells. In contrast to all other chemokines processed by CD26/DPP IV, LD78β(3-70) had increased chemotactic activity in comparison to intact LD78β. With a minimal effective concentration of 30 pmol/L, LD78β(3-70) became the most efficient monocyte chemoattractant. LD78β(3-70) retained its high capacity to induce an intracellular calcium increase in CCR5-transfected cells. Moreover, on CCR1 transfectants, truncated LD78β(3-70) was 30-fold more potent than intact LD78β. Thus, CD26/DPP IV can exert not only a negative but also a positive feedback during inflammation by increasing the specific activity of LD78β. CD26/DPP IV–cleaved LD78β(3-70) is the most potent CCR1 and CCR5 agonist that retains strong anti–HIV-1 activity, indicating the importance of the chemokine-protease interaction in normal and pathologic conditions.

Decreased Dipeptidyl Peptidase IV Enzyme Activity of Plasma Soluble CD26 and Its Inverse Correlation with HIV-1 RNA in HIV-1 Infected Individuals

1999 ◽  
Vol 91 (3) ◽  
pp. 283-295 ◽  
Author(s):  
Osamu Hosono ◽  
Toshio Homma ◽  
Hiroshi Kobayashi ◽  
Yasuhiko Munakata ◽  
Yoshihisa Nojima ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Inverse Correlation ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Hiv 1

A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site

2013 ◽  
Vol 434 (2) ◽  
pp. 191-196 ◽  
Author(s):  
Mika Nabeno ◽  
Fumihiko Akahoshi ◽  
Hiroyuki Kishida ◽  
Ikuko Miyaguchi ◽  
Yoshihito Tanaka ◽  
...  
Keyword(s):  
Comparative Study ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Binding Modes ◽  
Dipeptidyl Peptidase Iv Inhibitors

Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site

2007 ◽  
Vol 17 (6) ◽  
pp. 1765-1768 ◽  
Author(s):  
Scott M. Sheehan ◽  
Hans-Juergen Mest ◽  
Brian M. Watson ◽  
Valentine J. Klimkowski ◽  
David E. Timm ◽  
...  
Keyword(s):  
Conformational Change ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Dipeptidyl Peptidase Iv Inhibitors

An active-site mutation (Gly633 .fwdarw. Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum

Biochemistry ◽  
1992 ◽  
Vol 31 (47) ◽  
pp. 11921-11927 ◽  
Author(s):  
Emiko Tsuji ◽  
Yoshio Misumi ◽  
Toshiyuki Fujiwara ◽  
Noboru Takami ◽  
Shigenori Ogata ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Mutation ◽  
Rapid Degradation
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