Chapter 304 - Carboxypeptidase M

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  • Downregulation of kinin B1 receptor function by B2 receptor heterodimerization and signaling

    2015, Cellular Signalling
    Citation Excerpt :

    The kB2R is selectively activated by the peptides bradykinin (BK) or kallidin (KD; Lys-BK) cleaved from kininogen precursors by plasma or tissue kallikrein [1,2]. BK or KD is inactivated as kB2R agonists by removal of their C-terminal Arg by plasma carboxypeptidase (CP) N [3,4] or membrane CPM [5–7] but the metabolites generated, des-Arg9-BK (DABK) or des-Arg10-KD (DAKD), are instead specific agonists of the kB1R [2,8,9]. Typically, the kB2R is constitutively expressed in a variety of cell types in contrast to the kB1R whose expression is induced by injury or inflammation [1,2].

  • Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor

    2013, Journal of Biological Chemistry
    Citation Excerpt :

    They are distinguished from the CPA/B (M14A) subfamily by the lack of a propeptide activation sequence and the presence of an additional C-terminal domain consisting of a seven-stranded β barrel with topological similarity to the plasma protein transthyretin (2, 6, 7). CPM is an ectoenzyme anchored to the plasma membrane of cells by a glycosylphosphatidylinositol (GPI) anchor (8, 9) and is widely distributed in the body, for example in lung and placental microvilli, kidney, blood vessels, intestine, brain, and peripheral nerves and can be found in soluble form in various body fluids (1, 10, 11). CPM has a strict specificity, cleaving only C-terminal Arg or Lys residues (12), and although >60 endogenous human peptides or proteins have been identified as potential CPM substrates, only 22 have been tested and shown to have altered activity after C-terminal cleavage (10).

  • Targeted proteomic response to coffee consumption

    2020, European Journal of Nutrition
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