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

We report on a series of three patients with an unusual syndrome of eosinophilia and myalgia associated with the oral ingestion of tryptophan that was recognized in New Mexico in October 1989. All three patients, who were women 37 to 44 years of age, had severe muscle pain, muscle weakness, mouth ulcers, and striking eosinophilia (more than 8 X 10(9) cells per liter). Other manifestations included fever, abdominal pain, dyspnea, skin rash, and elevated serum concentrations of aminotransferase and aldolase. The women had been taking tryptophan in doses of 1.2 to 2.4 g a day for three weeks to 2 1/2 years. The discontinuation of tryptophan and the initiation of glucocorticoid treatment resulted in improvement, but all three women were still symptomatic three to five months later. Tests for trichinosis and other parasites and for allergic and connective-tissues disorders were negative, and serum immunoglobulin concentrations and erythrocyte sedimentation rates were normal. A muscle biopsy in one patient and biopsies of the vagina, liver, and other abdominal organs in another revealed eosinophilic infiltration, as well as the extracellular deposition of eosinophil-granule major basic protein. All three patients had elevated serum and urinary levels of this protein and eosinophil-derived neurotoxin, indicative of eosinophil degranulation. The syndrome of eosinophilia and myalgia in association with the ingestion of tryptophan that was seen in these three patients is a newly recognized adverse effect of tryptophan ingestion. Our identification of this association in these patients led to the discovery of an epidemic of what is now called the eosinophilia-myalgia syndrome.
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PMID:Association of the eosinophilia-myalgia syndrome with the ingestion of tryptophan. 231 25

The present study examined the cellular localization of monocarboxylate transporters (MCTs), glucose transporters (GLUTs), and some glycolysis-related molecules in the murine female genital tract to demonstrate existence of lactate/pyruvate-dependent energy systems. MCT1, a major MCT subtype, was localized selectively in the ovarian granulosa, oviductal-ciliated cells, and vaginal epithelium; all localizations were associated with intense expressions of glycolytic enzymes. MCT1 was localized in the cell membrane of granulosa cells, including fine processes extending from cumulus cells toward oocytes. The cumulus cells and oocytes showed intense signals for lactate dehydrogenase (LDH)-A and -B, respectively. The basolateral membrane of oviductal-ciliated cells expressed MCT4 as well as MCT1, while adjacent non-ciliated cells contained an intense immunoreactivity for aldolase-C, a glycolytic enzyme. The expression of GLUTs in the ovary was generally weak with an intense expression of GLUT1 only in some vascular endothelia. The oviductal epithelium expressed GLUT1 and GLUT3, respectively, in the basolateral and apical membrane of non-ciliated cells. In the vagina, the basal layers of epithelium were immunolabeled for MCT1 with the entire length of cell membrane, and expressed abundantly both GLUT1 and LDH-A. The findings correspond well with the rich existence of lactate in the genital fluids and strongly suggest the active transport of lactate/pyruvate in the female reproductive tract, which provides favorable conditions for oocytes, sperms, and zygotes.
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PMID:Cellular expression of monocarboxylate transporters in the female reproductive organ of mice: implications for the genital lactate shuttle. 2136 Feb 29

Bacterial vaginosis (BV) is a polymicrobial imbalance of the vaginal microbiota associated with reproductive infections, preterm birth, and other adverse health outcomes. Sialidase activity in vaginal fluids is diagnostic of BV and sialic acid-rich components of mucus have protective and immunological roles. However, whereas mucus degradation is believed to be important in the etiology and complications associated with BV, the role(s) of sialidases and the participation of individual bacterial species in the degradation of mucus barriers in BV have not been investigated. Here we demonstrate that the BV-associated bacterium Gardnerella vaginalis uses sialidase to break down and deplete sialic acid-containing mucus components in the vagina. Biochemical evidence using purified sialoglycan substrates supports a model in which 1) G. vaginalis extracellular sialidase hydrolyzes mucosal sialoglycans, 2) liberated sialic acid (N-acetylneuraminic acid) is transported into the bacterium, a process inhibited by excess N-glycolylneuraminic acid, and 3) sialic acid catabolism is initiated by an intracellular aldolase/lyase mechanism. G. vaginalis engaged in sialoglycan foraging in vitro, in the presence of human vaginal mucus, and in vivo, in a murine vaginal model, in each case leading to depletion of sialic acids. Comparison of sialic acid levels in human vaginal specimens also demonstrated significant depletion of mucus sialic acids in women with BV compared with women with a "normal" lactobacilli-dominated microbiota. Taken together, these studies show that G. vaginalis utilizes sialidase to support the degradation, foraging, and depletion of protective host mucus barriers, and that this process of mucus barrier degradation and depletion also occurs in the clinical setting of BV.
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PMID:Degradation, foraging, and depletion of mucus sialoglycans by the vagina-adapted Actinobacterium Gardnerella vaginalis. 2347 34