Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells.

Kumamoto, Kenshi; Stewart, T.A.; Johnson, A.; Erdös, Ervin G.

doi:10.1172/jci110015

Cited by 71 publications

(42 citation statements)

References 21 publications

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“…With longer peptides (e.g., the deca-and nonapeptides angiotensin I and bradykinin), this activity at neutrality is relatively high. Many of the physical and enzymatic characteristics of deamidase are close or identical to those reported for cathepsin A (41,45,46).…”

Section: Discussionsupporting

confidence: 64%

“…Of the three serine peptidases, which were relatively more active by one to two orders of magnitude than the metallopeptidases (Table 1), dipeptidyl peptidase IV (or CD26; [10][11][12] and prolylcarboxypeptidase (13,41) cleave peptides preferentially after a proline residue. Dipeptidyl peptidase IV is a membrane-bound serine peptidase active above neutral pH (10)(11)(12) that inactivates many peptides and hormones (42).…”

Section: Discussionmentioning

confidence: 99%

“…Its presence was demonstrated in cell lines HL-60 (43) and U937 (44), but not in human alveolar macrophages. Prolylcarboxypeptidase (or angiotensinase C) is a lysosomal enzyme with a pH optimum at acid pH (13,41), but it inactivates its natural substrate, angiotensin II, at Prot-Phe" bond even at neutral pH (Table 1).…”

Section: Discussionmentioning

confidence: 99%

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Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages.

Jackman¹,

Tan²,

Schraufnagel³

et al. 1995

Am J Respir Cell Mol Biol

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Alveolar macrophages protect the lungs against noxious agents. Proteases and peptidases are essential for this defense and many metabolic activities. Human alveolar macrophages were evaluated for the presence of six important peptidases. Deamidase, a serine peptidase identical with the lysosomal protective protein and possibly with cathepsin A, had high specific activity in alveolar macrophages and is also present in cultured mouse J774A.1 and human U937 cells, used for the sake of comparison. In fractionated J774A cells, most of the deamidase activity was in the lysosomal fraction and in the final supernatant. Deamidase in human alveolar macrophages, obtained by bronchoalveolar lavage from 23 patients, cleaved dansyl-Phe-Leu-Arg at a rate of 2.26 mumol/h/mg protein and hydrolyzed the chemotactic peptide N-f-Met-Leu-Phe even faster, at a rate of 53.1 mumol/h/mg protein, the highest activity for this enzyme with any of the cells we tested. Rabbit antiserum, elicited with the recombinant partial sequence of the enzyme, immunoprecipitated 77-88% of the macrophage deamidase. In immunocytochemistry, this antiserum localized deamidase within the human macrophages. The enzyme was inhibited by diisopropylfluorophosphate (DFP; 1 mM) and by ebelactone B (10 microM), noncompetitively. The mRNA of deamidase was detected in mouse macrophages by Northern blot; the two protein chains of deamidase were shown in human macrophages by Western blot. In addition, two other serine peptidases were also highly active in macrophages: dipeptidyl peptidase IV (1.38 mumol/h/mg protein) and prolylcarboxypeptidase (0.72 mumol/h/mg protein). The activity of plasma membrane zinc metallopeptidases, neutral endopeptidase 24.11 and carboxypeptidase M, in contrast, was low or absent (angiotensin I converting enzyme; kininase II).(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionsupporting

confidence: 64%

Section: Discussionmentioning

confidence: 99%

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Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages.

Jackman¹,

Tan²,

Schraufnagel³

et al. 1995

Am J Respir Cell Mol Biol

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“…This purification enabled us to produce specific antibodies against PRCP and for the first time establish a sensitive immunoassay for the measurement of PRCP in various body fluids. Earlier assays of PRCP have been based on enzymatic activity (15,16 ). In this study we measured PRCP in plasma obtained from 3 different cohorts, i.e., from a group of young healthy individuals, from a cohort of patients admitted to the emergency room with chest pain, and from the PIVUS community-based cohort of more than one thousand men and women of mean age 70 years (17 ).…”

Section: Discussionmentioning

confidence: 99%

Plasma Prolylcarboxypeptidase (Angiotensinase C) Is Increased in Obesity and Diabetes Mellitus and Related to Cardiovascular Dysfunction

Lind²,

Zhao

et al. 2012

Clinical Chemistry

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BACKGROUND: Prolylcarboxypeptidase (PRCP) (angiotensinase C) has 3 major targets, angiotensin II, prekallikrein, and ␣-melanocyte stimulating hormone [1][2][3][4][5][6][7][8][9][10][11][12][13] . The truncation of the latter leads to loss in appetite regulation and obesity in experimental animals. The objectives of this study were to purify PRCP from a native source, establish a sensitive immunoassay for PRCP, and relate plasma PRCP concentrations to signs and symptoms of obesity, diabetes mellitus, and cardiovascular dysfunction.

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“…PRCP also was associated with endothelial cell matrix [32]. Although originally purified from lysosomes, PRCP is a membrane protein since it is constitutively expressed on endothelial cell membranes where it is functional and upon gene trap targeting it was interrupted along with other membrane proteins by homing with a CD4 membrane signal [3,31,[33][34][35]. More recent cell biology studies since PRCP was first described as a lysosomal protease suggest that lysosomal compartments in all eukaryotic cells are the endomembrane system that is intimately involved in the export of internal constituents [36].…”

Section: Activation Of the Plasma Kallikrein/kinin Systemmentioning

confidence: 99%

Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system

Schmaier

2008

International Immunopharmacology

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The plasma kallikrein/kinin system that consists of the proteins factor XII, prekallikrein, and high molecular weight kininogen was first recognized as a surface-activated coagulation system arising when blood or plasma interacts with artificial surfaces. Although surface-activated contact activation occurs in vivo when various negatively charged surfaces become exposed, including a developing platelet thrombus, a physiologic, non-injury mechanism for activation, regulation, and function of this system has been elusive. Recent investigations have shown that there is a physiologic pathway for assembly and activation of this system independent of factor XII. Gene deficient mice of the bradykinin B2 receptor and factor XII have been recognized to have reduced risk for arterial thrombosis. This plasma proteolytic system influences arterial thrombosis independent of influencing hemostasis. Thus, the plasma kallikrein/kinin system has two mechanisms for its activation: one that is dependent and another independent of factor XII. Better understanding of this system may lead to insight into mechanisms for arterial thrombosis, independent of hemostasis.

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Prolylcarboxypeptidase (angiotensinase C) in human lung and cultured cells.

Cited by 71 publications

References 21 publications

Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages.

Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages.

Plasma Prolylcarboxypeptidase (Angiotensinase C) Is Increased in Obesity and Diabetes Mellitus and Related to Cardiovascular Dysfunction

Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system

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