Yasuharu Takada

Comparative evaluation of sialylated carbohydrate antigens, KL‐6, CA19‐9 and SLX as serum markers for interstitial pneumonia

Abstract We compared diagnostic values of three serum carbohydrate antigens, KL‐6, CA19‐9 and SLX to discriminate interstitial pneumonia (IP) from alveolar pneumonia and healthy volunteers. Subjects consisted of 13 patients with idiopathic pulmonary fibrosis and 10 associated with collagen vascular diseases, 12 patients with sarcoidosis and 70 controls (52 healthy volunteers and 18 patients with alveolar pneumonia). Cut‐off values were determined at the level at which the diagnostic accuracy became the highest for each marker, 449 U/mL for KL‐6, 26 U/mL for CA19‐9 and 41 U/mL for SLX. The sensitivity, the specificity and the diagnostic accuracy were 74.3% (26/35), 98.6% (69/70) and 90.5% (95/105) in KL‐6, 42.9% (15/35), 94.3% (66/70) and 77.1% (81/105) in CA19‐9, and 20.0% (7/35) and 95.7% (67/70) and 70.5% (74/105) in SLX, respectively. Receiver operating characteristic curves revealed that KL‐6 was far superior to both CA19‐9 and SLX. These results suggest that KL‐6 is the best marker for interstitial pneumonia among these carbohydrate antigens.

The immunocytochemical detection of angiotensin-converting enzyme in alveolar macrophages from patients with sarcoidosis

Angiotensin-converting enzyme (ACE) was detected in alveolar macrophages obtained by bronchoalveolar lavage (BAL), but not in lymphocytes and other cells, by immunofluorescence using anti-human ACE antibody. The enzyme was localized on the surface of plasma membrane and cytoplasmic processes of alveolar macrophages, as demonstrated by immunoelectron microscopy. The immunocytochemical staining for ACE in alveolar macrophages from patients with sarcoidosis was intense, which was consistent with the result that ACE activity in BAL cells from patients with sarcoidosis was significantly higher than in cells from normal subjects and from patients with nonsarcoid lung diseases.

Correlation between angiotensin-converting enzyme activity and histologic patterns in benign prostatic hypertrophy tissue.

Abstract Angiongensin converting enzyme (ACE) activities in 46 benign prostatic hypertrophy (BPH) tissues from 23 patients were compared with respect to histologic patterns, i.e., cystic, adenomatous and fibromuscular components. There was a good correlation between the enzyme activity and the percentage of cystic component in the tissue. On immunofluorescent study using antiserum against purified human kidney ACE, human prostatic ACE in tissues from BPH was mainly located in tubular epithelial cells and cystic lumens.

Angiotensin converting enzyme. A possible histologic indicator for human renal cell carcinoma.

Angiotensin converting enzyme (ACE) was studied in specimens of human renal cell carcinoma by indirect immunofluorescence using rabbit antibody to human kidney ACE and fluorescein‐labeled goat antibody to rabbit immunoglobulin. ACE was demonstrated in the cells of all renal cell carcinomas from 10 patients and in the cultured cells set up from 4 of them, but not in any cells of 12 extrarenal carcinomas of prostate, lung, and alimentary tract. These results suggest that immunohistologic detection of ACE is of value in the histologic diagnosis of renal cell carcinoma.

Direct radioimmunoassay of angiotensin-converting enzyme in sera from patients with pulmonary diseases

The concentration of angiotensin-converting enzyme (ACE) was measured in the sera of 47 normal subjects and 108 patients with various pulmonary diseases by radioimmunoassay (RIA) using antiserum to human kidney ACE and homogeneous human kidney ACE as a tracer. The immunologic identity of ACE in the sera from a normal subject and a patient with active sarcoidosis was demonstrated by parallel logit-log transformation of displacement curves in the RIA. The activity and the enzyme concentration in normal and clinical samples correlated well (r=0.78,P<0.001). The mean concentration of ACE in normal serum was 320.9±105.2 ng/ml (mean ±1 SD, n=47). Serum ACE concentration in patients with active sarcoidosis (823.4±209.7, n=13) and in patients with silicosis (569.5±183.8, n=21) was significantly higher than in normals, and the ACE activity in the serum of both groups increased parallel to the concentration. In contrast, patients with active pulmonary tuberculosis (508.5±159.4, n=11) and with lung cancer (481.1±169.5, n=12) had significantly higher serum ACE concentrations (P<0.005) although the serum ACE activity did not increase. The specific activity of both groups (40.4±7.0 and 39.6±7.1 µmol/min/mg, respectively) was lower than that of normal subjects (50.0±12.8). A low ACE activity and a normal ACE concentration in patients with diffuse panbronchiolitis (n=8) and chronic bronchitis (n=6) resulted in a significantly low specific activity (37.4±13.0 and 36.2±7.3, respectively).

Angiotensin Converting Enzyme in Sarcoidosis and in Silicosis

Angiotensin converting enzyme (ACE) activities of bronchoalveolar lavage fluid (BALF) and serum in patients with sarcoidosis and with silicosis were measured. Serum ACE was measured by enzymic assay and radioimmunoassay. There was a close relationship between ACE activity and content (r = 0.78). Serum ACE activities in patients with active sarcoidosis (37.5 +/- 11.1 nmol/min/ml, mean +/- SD) and with silicosis (25.5 +/- 9.3) were significantly elevated from the control (18.6 +/- 6.0). BALF ACE activities in the control, patients with active sarcoidosis and with silicosis were 0.23 +/- 0.19 nmol/min/ml, 0.94 +/- 0.97 and 0.38 +/- 0.05, respectively. BALF ACE in patients with active sarcoidosis and with silicosis were significantly different from the control. When BALF ACE was corrected by the cell count of alveolar macrophage (per 10(6) cells), activity was significantly different from control only in the patients with sarcoidosis. Moreover, only the alveolar macrophages in sarcoidosis were stained by immunofluorescence and immunocytochemistry using rabbit antihuman ACE antibody. Induction of ACE in alveolar macrophage might have an important role for the activity or progression of sarcoidosis.

Production of angiotensin-converting enzyme in rat epididymis

Summary:  Unilateral ductuli efferentia testis of immature rat were severed in order to interrupt the continuity between testis and epididymis and angiotensin‐converting enzyme (ACE) activities were measured 5 weeks after the operation. The epididymal ACE on the operated side increased to nearly the same level as that on the contralateral side, but the testicular ACE activity on the operated side was markedly lower than that on the contralateral side.

Immunohistologic Characterization of Angiotensin Converting Enzyme in the Human Kidney Using Monoclonal and Polyclonal Antibodies

Angiotensin converting enzyme (ACE; EC 3.4.15.1), or kininase II, plays an important role in the regulation of blood pressure by converting angiotensin I to the vasopressor angiotensin II, and by inactivating the depressor substance bradykinin (Erdos, 1976). The enzyme is mainly localized on the luminal surface of vascular endothelial cells of the lung or other tissues (Caldwell et al.,1976; Ryan et al., 1976; Takada et al., 1982). In addition to the endothelial localization, the enzyme is present on other types of cells including epithelial cells of renal proximal tubule, small intestine and testis, and neuroepithelial cells of the brain (Caldwell et al.,1976; Ryan et al.,1976; Takada et al., 1982; Defendini et al.,1983). Recent studies have demonstrated that testis of the rabbit and brain of the rat contain isoforms of ACE (El-Dorry et al., 1982; Strittmatter et al., 1985). Recently, we have developed monoclonal antibodies against human kidney ACE. In the present study, we examined the binding specificity of monoclonal antibody to ACE in the human kidney and lung by immunofluoresent method in comparison with that of the polyclonal antibody against human kidney ACE.

Biochemistry of Human Converting Enzyme

Angiotensin converting enzyme (ACE, EC 3.4.15.1) was purified to homogeneity from human kidney and its specific antibody was raised in the rabbit. The antibody cross-reacted equally with human enzymes from kidney, lung, intestine, plasma and urine. Immunofluorescent and immunoelectron microscopic observation indicated that the enzyme was located on the plasma membrane and micropinocytic vesicles at the luminal site of vascular endothelium in the lung. It was also present on the brush border, intercellular and basal infolding membranes of proximal tubular epithelium, but was not detected on the distal tubular epithelium or vascular endothelium in the kidney. ACE was demonstrated immunocytologically in human alveolar macrophages and renal carcinoma tissues. The carcinoma tissue contained a possible isoenzyme of ACE differing in part immunologically from the enzyme of normal kidney.

[Hepatopulmonary syndrome: clinical report of two cases].

症例1は57歳,女性.労作時呼吸困難を主訴に受診. PaO250.6Torrと低酸素血症を認めた.症例2は68歳,女性.肝細胞癌の治療目的にて入院中に労作時息切れが出現. PaO255.3Torrと低酸素血症を認めた.両症例とも基礎疾患として肝硬変症を認めること,ガス交換異常を伴う低酸素血症を認めること,マルチスライスCT (MSCT)にて肺内末梢血管拡張を認めることから肝肺症候群と診断した.