Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The presence of gastricsin in bovine abomasal juice has been reported previously, but its exact site of origin has not yet been established. Specific polyclonal antibodies were used in the peroxidase-antiperoxidase method or the protein A/gold technique to label cells producing progastricsin. This immunocytolocalization was correlated with that of pepsinogen and prochymosin using specific polyclonal antibodies against those zymogens. The present study clearly established that progastricsin was located exclusively in chief, mucous neck, transitional mucous neck/chief, foveolar epithelial and surface epithelial cells of the calf fundic mucosa. Furthermore, progastricsin was found to be colocalized with pepsinogen and prochymosin in the same secretory granules of these cells. Progastricsin was not observed in parietal, gastric endocrine and undifferentiated neck cells.
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PMID:Cellular and subcellular localization of progastricsin in calf fundic mucosa: colocalization with pepsinogen and prochymosin. 202 33

The aspartic proteinase cathepsin D was purified from human spleen and localised in various formalin fixed paraffin embedded human tissues using the peroxidase-antiperoxidase (PAP) technique. Cathepsin D was shown not only in macrophages but also in other connective tissue cells, and in epithelium. It was present in spleen (littoral cells and cells within Malpighian bodies), liver (hepatocytes and Kupffer cells), lung (alveolar macrophages and bronchial epithelium), brain (neurones), lymph nodes (histiocytes in germinal centres, sinusoid lining cells) and stomach (parietal and mucous neck cells). Cathepsin D was also found in carcinomas of bronchus, stomach, colon, kidney, breast, ovary, bladder and pancreas, both in neoplastic epithelium and in stromal cells, but was seldom present in connective tissue neoplasms. A group of malignant lymphomas also contained the enzyme within scattered cells. The distribution of cathepsin D seems to be much wider than that of the structurally related aspartic proteinases pepsin, gastricsin, and renin.
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PMID:Immunolocalization of cathepsin D in normal and neoplastic human tissues. 354 65

An immunoperoxidase (peroxidase-antiperoxidase) method was used to localise the gastric acid proteinase gastricsin in prostate. The enzyme was present, probably as zymogen, in acinar lining cells in 66 (69%) of 96 cases of benign prostatic enlargement; other normal tissues from male genital tract were negative. It was also present in the tumour cells in 21 (39%) of 54 cases of prostatic adenocarcinoma. The findings support the suggestion that the prostate is the source of the gastricsin of normal seminal fluid. It is not yet clear whether its presence in prostatic carcinomas will be of diagnostic use.
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PMID:Gastricsin in the benign and malignant prostate. 392 77