نتایج جستجو برای: Dipeptidyl Peptidase-IV

تعداد نتایج: 187377  

Journal: :The Biochemical journal 2006
Jais R Bjelke Jesper Christensen Per F Nielsen Sven Branner Anders B Kanstrup Nicolai Wagtmann Hanne B Rasmussen

Dipeptidyl peptidases 8 and 9 have been identified as gene members of the S9b family of dipeptidyl peptidases. In the present paper, we report the characterization of recombinant dipeptidyl peptidases 8 and 9 using the baculovirus expression system. We have found that only the full-length variants of the two proteins can be expressed as active peptidases, which are 882 and 892 amino acids in le...

Journal: :Hypertension 2008
James Brian Byrd Karine Touzin Saba Sile James V Gainer Chang Yu John Nadeau Albert Adam Nancy J Brown

Angioedema is a potentially life-threatening adverse effect of angiotensin-converting enzyme inhibitors. Bradykinin and substance P, substrates of angiotensin-converting enzyme, increase vascular permeability and cause tissue edema in animals. Studies indicate that amino-terminal degradation of these peptides, by aminopeptidase P and dipeptidyl peptidase IV, may be impaired in individuals with ...

2001
Stefan Brocke Andreas Steinbrecher Dirk Reinhold Laura Quigley Ameer Gado Nancy Tresser Leonid Izikson Ilona Born Jürgen Faust Klaus Neubert Roland Martin Siegfried Ansorge

Journal: :European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies 1992
G Vanhoof I De Meester M van Sande S Scharpé A Yaron

The proline-specific peptidases, aminopeptidase P (EC 3.4.11.9) and dipeptidyl peptidase IV (EC 3.4.14.5), were measured in human tissue homogenates and physiological fluids. All tissues examined contained measurable aminopeptidase P and dipeptidyl peptidase IV activities. High specific activities for both enzymes under study were found in benign prostatic hypertrophy. Normal prostate and prost...

Journal: :European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies 1991
R Mentlein R Staves H Rix-Matzen H R Tinneberg

Dipeptidyl peptidase IV (CD 26 leukocyte differentiation antigen) is an enzymic surface marker of a human T lymphocyte subpopulation which has been shown to be associated with their capacity to produce large amounts of interleukin 2 and proliferate strongly in response to mitogenic stimulation. The peptidase activity on the surface of purified human peripheral mononuclear cells was determined s...

Journal: :Hypertension 2012
Edwin K Jackson Stanton J Kochanek Delbert G Gillespie

The purpose of this study was to investigate the role of dipeptidyl peptidase IV in regulating the effects of 2 of its substrates, neuropeptide Y(1-36) and peptide YY(1-36), on proliferation of and collagen production by preglomerular vascular smooth muscle and glomerular mesangial cells from spontaneously hypertensive and normotensive rats. In cells from hypertensive rats, neuropeptide Y(1-36)...

Journal: :Infection and immunity 1997
A Beauvais M Monod J Wyniger J P Debeaupuis E Grouzmann N Brakch J Svab A G Hovanessian J P Latgé

A dipeptidyl-peptidase IV was purified from the culture medium of the human-pathogenic fungus Aspergillus fumigatus. The enzyme has an apparent molecular mass of 95 kDa and contained approximately 10 kDa of N-linked carbohydrate. This glycoprotein is antigenic and has all characteristics of the class IV dipeptidyl-peptidases: removal of Xaa-Pro and to a lesser extent Xaa-Ala dipeptides from the...

2012
Eleonore Fröhlich Elke Maier Richard Wahl

BACKGROUND To understand the role of proteases involved in human thyroid cancer progression and tissue invasion, thyrocytes from other species could potentially be used provided their characteristics are similar. It is not known whether dipeptidyl peptidase IV and aminopeptidase N activities, which are overexpressed in human thyroid cancer, are, as in human, also absent in normal thyrocytes of ...

1999
Roger H. ERICKSON James R. GUM Craig D. LOTTERMAN James W. HICKS Roy S. LAI Young S. KIM

Hepatocyte nuclear factor 1 was identified as the transcription factor binding to a 20 bp (®150 to ®131) region of the gene for human dipeptidyl peptidase IV, which has been shown to be important for the expression of dipeptidyl peptidase IV in the human intestinal and hepatic epithelial cell lines Caco-2 and HepG2. Functional analysis of the hepatocyte nuclear factor 1 site was performed with ...

Journal: :Clinical science 1983
M T Abbs A J Kenny

A microvillar fraction was prepared from human kidney cortex. This fraction was seven to 10 times enriched in aminopeptidases N and A, gamma-glutamyltransferase, dipeptidyl peptidase IV, neutral endopeptidase and alkaline phosphatase. Dipeptidyl peptidase IV activity of human renal microvilli could be inhibited by di-isopropylphosphorofluoridate and neutral endopeptidase activity by phosphorami...

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