Localization of an N-Domain Region of Angiotensin-Converting Enzyme Involved in the Regulation of Ectodomain Shedding Using Monoclonal Antibodies

2005 ◽  
Vol 4 (2) ◽  
pp. 258-267 ◽  
Author(s):  
Irina V. Balyasnikova ◽  
Zenda L. Woodman ◽  
Ronald F. Albrecht ◽  
Ramanathan Natesh ◽  
K. Ravi Acharya ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Angiotensin Converting Enzyme ◽  
Ectodomain Shedding ◽  
Converting Enzyme

Immunohistochemical study of angiotensin-converting enzyme in human tissues using monoclonal antibodies

1987 ◽  
Vol 87 (5) ◽  
pp. 487-490 ◽  
Author(s):  
S. M. Danilov ◽  
A. I. Faerman ◽  
O. Yu. Printseva ◽  
A. V. Martynov ◽  
I. Yu. Sakharov ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Angiotensin Converting Enzyme ◽  
Immunohistochemical Study ◽  
Human Tissues ◽  
Converting Enzyme

scholarly journals The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein

2004 ◽  
Vol 271 (12) ◽  
pp. 2539-2547 ◽  
Author(s):  
Tobias M. J. Allinson ◽  
Edward T. Parkin ◽  
Thomas P. Condon ◽  
Sylva L. U. Schwager ◽  
Edward D. Sturrock ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Ectodomain Shedding ◽  
Converting Enzyme

Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding

2001 ◽  
Vol 358 (1) ◽  
pp. 185-192 ◽  
Author(s):  
Susan PANG ◽  
Anthony J. CHUBB ◽  
Sylva L. U. SCHWAGER ◽  
Mario R. W. EHLERS ◽  
Edward D. STURROCK ◽  
...  
Keyword(s):  
Cell Surface ◽  
Angiotensin Converting Enzyme ◽  
Active Form ◽  
Ectodomain Shedding ◽  
Converting Enzyme ◽  
Critical Determinant ◽  
Terminal Domain ◽  
Cytosolic Domains ◽  
Identical Manner ◽  
Substrate Proteins

Angiotensin-converting enzyme (ACE) is one of a growing number of integral membrane proteins that is shed from the cell surface through proteolytic cleavage by a secretase. To investigate the requirements for ectodomain shedding, we replaced the glycosylphosphatidylinositol addition sequence in membrane dipeptidase (MDP) - a membrane protein that is not shed - with the juxtamembrane stalk, transmembrane (TM) and cytosolic domains of ACE. The resulting construct, MDP–STMACE, was targeted to the cell surface in a glycosylated and enzymically active form, and was shed into the medium. The site of cleavage in MDP–STMACE was identified by MS as the Arg374-Ser375 bond, corresponding to the Arg1203-Ser1204 secretase cleavage site in somatic ACE. The release of MDP–STMACE and ACE from the cells was inhibited in an identical manner by batimastat and two other hydroxamic acid-based zinc metallosecretase inhibitors. In contrast, a construct lacking the juxtamembrane stalk, MDP–TMACE, although expressed at the cell surface in an enzymically active form, was not shed, implying that the juxtamembrane stalk is the critical determinant of shedding. However, an additional construct, ACEΔC, in which the N-terminal domain of somatic ACE was fused to the stalk, TM and cytosolic domains, was also not shed, despite the presence of a cleavable stalk, implying that in contrast with the C-terminal domain, the N-terminal domain lacks a signal required for shedding. These data are discussed in the context of two classes of secretases that differ in their requirements for recognition of substrate proteins.

Monoclonal Antibodies 1B3 and 5C8 as Probes for Monitoring the Integrity of the C-Terminal End of Soluble Angiotensin-Converting Enzyme

Hybridoma ◽  
2005 ◽  
Vol 24 (1) ◽  
pp. 14-26 ◽  
Author(s):  
Irina V. Balyasnikova ◽  
Zhu-Li Sun ◽  
Folker E. Franke ◽  
Yulia V. Berestetskaya ◽  
Antony J. Chubb ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Angiotensin Converting Enzyme ◽  
Converting Enzyme
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