Literature DB >> 15857608

Representative aminopeptidases and prolyl endopeptidase from murine macrophages: comparative activity levels in resident and elicited cells.

Renata do Amaral Olivo1, Catarina de Fátima Pereira Teixeira, Paulo Flávio Silveira.   

Abstract

Macrophages are considered the main effector cells of immune system. Under stimulation these cells are known to be activated by a process involving morphological, biochemical and functional changes. Since altered peptidase activities could be among the factors leading to the differentiation and activation of these cells, in the present work seven naphthylamide derivative substrates were employed to assess representative aminopeptidase and prolyl endopeptidase activities in resident and elicited macrophages of mice. Soluble basic aminopeptidase and prolyl endopeptidase and soluble and particulate neutral and prolyl dipeptidyl aminopeptidase IV activities were present at measurable levels while particulate prolyl endopeptidase and basic aminopeptidase, and particulate and soluble cystyl and pyroglutamyl aminopeptidases were not detectable. Kinetic parameters, chloride activation and the inhibitory effects of puromycin, bestatin, amastatin and diprotin A characterized differential properties of these peptidase activities. The observed increment (about 6-17-fold) of the soluble basic aminopeptidase and prolyl endopeptidase and soluble and particulate neutral and prolyl dipeptidyl aminopeptidase IV activities in elicited macrophages was particularly relevant, as these might contribute to an increased ability of this cell to inactivate several susceptible substrates known to be inflammatory and/or immunological mediators.

Entities:  

Mesh:

Substances:

Year:  2005        PMID: 15857608     DOI: 10.1016/j.bcp.2005.03.002

Source DB:  PubMed          Journal:  Biochem Pharmacol        ISSN: 0006-2952            Impact factor:   5.858


  6 in total

1.  Expression and activity profiles of DPP IV/CD26 and NEP/CD10 glycoproteins in the human renal cancer are tumor-type dependent.

Authors:  Adolfo Varona; Lorena Blanco; Itxaro Perez; Javier Gil; Jon Irazusta; José I López; M Luz Candenas; Francisco M Pinto; Gorka Larrinaga
Journal:  BMC Cancer       Date:  2010-05-11       Impact factor: 4.430

2.  Ang II (Angiotensin II) Conversion to Angiotensin-(1-7) in the Circulation Is POP (Prolyloligopeptidase)-Dependent and ACE2 (Angiotensin-Converting Enzyme 2)-Independent.

Authors:  Peter Serfozo; Jan Wysocki; Gvantca Gulua; Arndt Schulze; Minghao Ye; Pan Liu; Jing Jin; Michael Bader; Timo Myöhänen; J Arturo García-Horsman; Daniel Batlle
Journal:  Hypertension       Date:  2019-12-02       Impact factor: 10.190

3.  Altered Activity and Expression of Cytosolic Peptidases in Colorectal Cancer.

Authors:  Itxaro Perez; Lorena Blanco; Begoña Sanz; Peio Errarte; Usue Ariz; Maider Beitia; Ainhoa Fernández; Alberto Loizate; M Luz Candenas; Francisco M Pinto; Javier Gil; José I López; Gorka Larrinaga
Journal:  Int J Med Sci       Date:  2015-06-02       Impact factor: 3.738

4.  Methotrexate and cyclosporine treatments modify the activities of dipeptidyl peptidase IV and prolyl oligopeptidase in murine macrophages.

Authors:  R A Olivo; N G Nascimento; C F P Teixeira; P F Silveira
Journal:  Clin Dev Immunol       Date:  2008

Review 5.  The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis.

Authors:  Yannick Waumans; Lesley Baerts; Kaat Kehoe; Anne-Marie Lambeir; Ingrid De Meester
Journal:  Front Immunol       Date:  2015-08-07       Impact factor: 7.561

6.  Prolyl endopeptidase activity is correlated with colorectal cancer prognosis.

Authors:  Gorka Larrinaga; Itxaro Perez; Lorena Blanco; Begoña Sanz; Peio Errarte; Maider Beitia; María C Etxezarraga; Alberto Loizate; Javier Gil; Jon Irazusta; José I López
Journal:  Int J Med Sci       Date:  2014-01-10       Impact factor: 3.738

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.