Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three aldolase isoenzymes; aldolase A, B and C were found in various human tissues including gastric mucosa, by means of substrate specificities (the fuctose-1, 6-diphosphate aldolase/fructose-1-phosphate aldolase activity ratio) and electrophoresis. The basic pattern of aldolase isoenzyme in man consisted of nine active bands, which were designated as I, II, III, IV, V, VI, VII, VIII and IX band from anode side respectively. The I band corresponded to aldolase C, V to aldolase A and IX to aldolase B. The II, III and IV band are hybrid molecules composed of subunit of aldolase A and C, and the VI, VII and VIII of subunit of aldolase A and B. The V band was present in all tissues, while IX was detected in the liver, kidney and stomach. The I, II, III and IV band were found in all tissues except for muscle. These findings were extremely different from those in other species. In normal gastric mucosa, active bands were composed of I, II, III, IV, V, VIII and IX band, while in gastric cancerous tissue, I, II, III, VIII and IX band were absent or markedly decreased in activity. In contrast, the V band increased. In fetal gastric mucosa, they showed the same pattern as cancerous. In extract of cancerous tissues, the FDP/F1P activity ratio was 20.5+/-2.2, as compared with 7.2+/-0.1 in normal gastric mucosa. In serum of patients with gastric cancer, the FDP/F1P activity ratio was 9.7+/-1.2, while it was 2.9+/-0.4 in normal human serum. These results suggest that the elevation in serum of the FDP/F1P ratio in gastric cancer is due to increase in muscle type isoenzyme (aldolase A) which is derived from cancerous tissue. Furthermore, the analysis of serum aldolase isoenzyme will save for cancer diagnosis.
 ...
PMID:[The distribution of the aldolase isoenzymes in various human tissues and the anomaly in cancerous tissues -especially in gastric cancer- (author's transl)]. 124 Aug 53

A 54-yr-old man was admitted to Hokkaido University Hospital, complaining of fever, multiple arthralgia, edematous erythema and face and muscular weakness of extremities during the last 2 months. He was diagnosed as dermatomyositis by acceleration of ESR, elevation of GOT, GPT, CPK, aldolase, moderate increases of collagen fibers in biopsy specimen of skin and his clinical signs. Although stools were positive for occult blood, the routine radiographic examination failed to detect the bleeding site in the upper GI. tract. However, in the double contrast picture of the stomach, a very fine abnormal linear shadow was observed at the upper corpus of the lesser curvature. This linear shadow was a margin of the tumor, retrospectively. About 4 months later, abnormal pain occurred and a mass was palpable in the left lumbar region, suggesting a pancreatic tumor. He was operated on excising the tumor, but was performed only exploratory laparotomy because of the presence of intra-abdominal metastases. Death occurred 40 days after the operation and necropsy was done. The gross anatomical findings of the abdomen showed a stomach tumor as large as an infant's head and its metastases to pancreas, lymph nodes, and greater and lesser omentum. Esophageal mucosa including esophagocardiac junction was intact. Histological examination of the intragastric tumor revealed a typical squamous cell carcinoma with keratinization. According to the absence of the components of adenocarcinoma and squamous metaplastic gastric mucosa of non-cancerous areas in the stomach, it seemed likely to be a heterotopic squamous cell carcinoma. It was unknown about the precedence between the stomach cancer and dermatomyositis. There have been 11 cases of primary pure squamous cell carcinoma in the world literature since 1968, but this is the first case report of coexistence of these two diseases.
 ...
PMID:[A case report of a primary pure squamous cell carcinoma of the stomach associated with dermatomyositis (author's transl)]. 726 22

We studied the alteration of aldolase isozymes in the serum and tissues of patients with cancer and other diseases using radioimmunoassays specific for aldolase A, B, and C subunits. Aldolase B was predominantly found in adult liver, where aldolase A and C were distinctly low. Aldolase A and B showed almost the same concentration in fetal liver, while in neonatal liver aldolase B protein concentrations were much higher than aldolase A. In contrast, aldolase A was the predominant isozyme found in hepatoma and gastric cancer tissues, whereas aldolase B was distinctly low in hepatoma tissues, and extremely low in gastric cancer tissues. These results suggest that the aldolase A is a more fetal type of liver isozyme than the aldolase B and C, and aldolase B is a more differentiated type of liver isozyme than aldolase A and C. Serum FDP aldolase activities were elevated in half of patients with liver diseases, all patients with muscle diseases and a few patients with cancer. Serum aldolase A levels were elevated in patients with muscle diseases and cancer, but not elevated in patients with liver diseases. In contrast, serum aldolase B levels were elevated in patients with liver disease, but not elevated in patients with muscle diseases and other diseases without liver injury. Serum aldolase B levels showed a trend to decrease in cancer patients with normal GPT levels. Serum aldolase A/B ratios were significantly increased in cancer patients with normal GPT levels, whereas they showed the decreased levels in patients with liver diseases.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Alteration of aldolase isozymes in serum and tissues of patients with cancer and other diseases. 804 42

Aimed at identification and structural characterization of novel putative therapeutic targets in H. pylori, the etiological agent of numerous gastrointestinal diseases including peptic ulcer and gastric cancer, the present study comprised of three phases. First, through subtractive analysis of metabolic pathways of Helicobacter pylori HPAG1 and human, as documented in the KEGG database, 11 pathogen-specific pathways were identified. Next, all proteins involved in these pathogen-specific pathways were scrutinized in search of promising targets and the study yielded 25 candidate target proteins that are likely to be essential for the pathogen viability, but have no homolog in human. The lipopolysaccharide (LPS) biosynthesis pathway was found to be the largest contributor (nine proteins) to this list of candidate proteins. Considering the importance of LPS in H. pylori virulence, 3D structural models of three predicted target enzymes of this pathway, namely 2-dehydro-3-deoxy-phosphooctonate aldolase, UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase and Phosphoheptose isomerase, were then built up using the homology modeling approaches. Binding site analysis and docking of the known biological substrate PEP to 2-dehydro-3-deoxyphosphooctonate aldolase revealed the potential binding pocket present in the single monomeric form of the enzyme and identified 11 amino acid residues that might play the key roles in this protein-ligand interaction.
 ...
PMID:In silico quest for putative drug targets in Helicobacter pylori HPAG1: molecular modeling of candidate enzymes from lipopolysaccharide biosynthesis pathway. 2185 May 71