Literature DB >> 2908057

Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A ('angiotensin converting enzyme'), is a marker for a set of striatal efferent fibres.

K Barnes1, R Matsas, N M Hooper, A J Turner, A J Kenny.   

Abstract

Endopeptidase-24.11 (sometimes referred to as 'enkephalinase') is a key cell-surface enzyme in the metabolism of neuropeptides. A previous immunohistochemical study mapped the enzyme in pig brain and indicated a striosomal ordering of the enzyme within the striatum. This point has now been confirmed by staining adjacent sections for acetylcholinesterase (by histochemistry) and endopeptidase-24.11 (by an immunoperoxidase method). While there were some general similarities in the mapping of these two hydrolases, e.g. in the caudate-putamen, globus pallidus, olfactory tubercle, substantia nigra and striatonigral tract, there were differences in intensity and in the microscopic distribution, e.g. as in striosomes for which acetylcholinesterase was diminished. Two other membrane peptidases, peptidyl dipeptidase A ('angiotensin converting enzyme') and aminopeptidase N, were also mapped by the same immunohistochemical method. Peptidyl dipeptidase A had some similarities with endopeptidase-24.11, e.g. in its concentration within the striatal nuclei, but clear differences were also apparent, in particular the absence of staining of the former in the globus pallidus and olfactory tubercle. Immunostaining for aminopeptidase N, in contrast to the other peptidases, was observed as a diffuse staining throughout the gray matter. At the microscopic level, two important differences were that staining for aminopeptidase N and peptidyl dipeptidase A was very intense throughout the vasculature of the brain and that striatal efferent bundles of unmyelinated fibres staining positively for endopeptidase-24.11 were depleted of the other two peptidases. All three peptidases were identified in the pia mater. Thus, endopeptidase-24.11, unlike peptidyl dipeptidase A and aminopeptidase N, is a marker for a set of striatal efferent fibres in pig brain.

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Year:  1988        PMID: 2908057     DOI: 10.1016/0306-4522(88)90184-4

Source DB:  PubMed          Journal:  Neuroscience        ISSN: 0306-4522            Impact factor:   3.590


  9 in total

1.  Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine.

Authors:  H Terashima; N W Bunnett
Journal:  J Gastroenterol       Date:  1995-12       Impact factor: 7.527

Review 2.  The endothelin system and endothelin-converting enzyme in the brain: molecular and cellular studies.

Authors:  K Barnes; A J Turner
Journal:  Neurochem Res       Date:  1997-08       Impact factor: 3.996

3.  A comparison of the zinc contents and substrate specificities of the endothelial and testicular forms of porcine angiotensin converting enzyme and the preparation of isoenzyme-specific antisera.

Authors:  T A Williams; K Barnes; A J Kenny; A J Turner; N M Hooper
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

4.  Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse.

Authors:  K Barnes; J Ingram; A J Kenny
Journal:  Biochem J       Date:  1989-12-01       Impact factor: 3.857

5.  Membrane peptidases in the pig choroid plexus and on other cell surfaces in contact with the cerebrospinal fluid.

Authors:  A Bourne; K Barnes; B A Taylor; A J Turner; A J Kenny
Journal:  Biochem J       Date:  1989-04-01       Impact factor: 3.857

6.  The Alzheimer's amyloid-degrading peptidase, neprilysin: can we control it?

Authors:  N N Nalivaeva; N D Belyaev; I A Zhuravin; A J Turner
Journal:  Int J Alzheimers Dis       Date:  2012-07-26

7.  The anti-inflammatory Annexin A1 induces the clearance and degradation of the amyloid-β peptide.

Authors:  Miriam Ries; Rodrigo Loiola; Urvi N Shah; Steve M Gentleman; Egle Solito; Magdalena Sastre
Journal:  J Neuroinflammation       Date:  2016-09-02       Impact factor: 8.322

Review 8.  Neprilysin expression and functions in development, ageing and disease.

Authors:  N N Nalivaeva; I A Zhuravin; A J Turner
Journal:  Mech Ageing Dev       Date:  2020-09-26       Impact factor: 5.432

9.  Mutations in MME cause an autosomal-recessive Charcot-Marie-Tooth disease type 2.

Authors:  Yujiro Higuchi; Akihiro Hashiguchi; Junhui Yuan; Akiko Yoshimura; Jun Mitsui; Hiroyuki Ishiura; Masaki Tanaka; Satoshi Ishihara; Hajime Tanabe; Satoshi Nozuma; Yuji Okamoto; Eiji Matsuura; Ryuichi Ohkubo; Saeko Inamizu; Wataru Shiraishi; Ryo Yamasaki; Yasumasa Ohyagi; Jun-ichi Kira; Yasushi Oya; Hayato Yabe; Noriko Nishikawa; Shinsuke Tobisawa; Nozomu Matsuda; Masayuki Masuda; Chiharu Kugimoto; Kazuhiro Fukushima; Satoshi Yano; Jun Yoshimura; Koichiro Doi; Masanori Nakagawa; Shinichi Morishita; Shoji Tsuji; Hiroshi Takashima
Journal:  Ann Neurol       Date:  2016-03-17       Impact factor: 10.422

  9 in total

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