| Literature DB >> 15016448 |
Fanny Jardinaud1, Ghasal Banisadr, Florence Noble, Stéphane Mélik-Parsadaniantz, Huixiong Chen, Christophe Dugave, Hervé Laplace, William Rostène, Marie-Claude Fournié-Zaluski, Bernard P Roques, Théodora Popovici.
Abstract
Aminopeptidase N (APN), which is widely distributed in mammalian tissues, is able to cleave numerous regulatory peptides. The selective inhibitor of APN, [(125)I] RB129, has been used to study the distribution of this exopeptidase during rat prenatal development and adult life by in vitro whole-body autoradiography. In the central nervous system, APN shows a weak labeling compared to the major part of the non-nervous tissues in the embryo and in the adult. APN is progressively expressed in kidney, intestine, heart, lung, sensory organs, eye, and thymus. In organs such as the liver, the cartilages and the bones, altered levels of APN expression are observed during the development, or in the embryo compared to the adult, suggesting a role of APN during the liver haematopoiesis and bone growth. At this time, all the physiological functions of APN are still incompletely known, however its developmental pattern of expression strongly suggests a function of modulation of this enzyme during the development, next in physiological and/or pathological situations in adult. In this way, APN could represent a new therapeutic target in pathological processes, such as tumoral proliferation and/or angiogenesis associated with cancer development, where an increase in the level of this enzyme has been observed.Entities:
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Year: 2004 PMID: 15016448 DOI: 10.1016/j.biochi.2003.12.004
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079