Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzymatic activities unique to the glyoxylate cycle of higher plants and certain lower invertebrates, isocitrate lyase and malate synthase, have been demonstrated in homogenates prepared from human liver. Human liver can also carry out cyanide-insensitive fatty acid oxidation from palmitate. Utilizing light microscopic immunocytochemistry with an antibody produced against Euglena malate synthase, this enzyme localizes in numerous ovoid granules in human hepatocytes. Also, immunocytochemistry using antibodies produced against rat fatty acyl-CoA oxidase showed that this enzyme was localized in similar structures. With routine cytochemistry, catalase was seen in identical granular bodies. Both catalase and fatty acyl-CoA oxidase are peroxisomal enzymes. The presence of malate synthase in liver homogenates was further confirmed by Western blot analysis. These data suggest that the human liver may be capable of utilizing the carbon backbone of fatty acids for carbohydrate synthesis since the glyoxylate cycle in lower organisms subserves this anabolic function.
Anat Rec 1992 Dec
PMID:Evidence for the glyoxylate cycle in human liver. 145 49

Information regarding the presence of the glyoxylate cycle in chick liver was sought. This metabolic pathway has long been thought to be absent from vertebrate tissues. Previous studies in other tissues have shown that, when present, this pathway is sensitive to vitamin-D. Thus, the effect of long-term vitamin-D deficiency and subsequent vitamin-D replacement on liver structure was studied by light microscopy. In addition, specific biochemical assays for the presence of glyoxylate cycle enzymes were performed. Light microscopy of lipid extracted tissues, light microscopic histochemistry, and quantitative histochemistry showed that the hepatocytes from vitamin-D-deficient animals contained primarily lipid. Hepatocytes from normal and vitamin-D-replete livers contained primarily carbohydrate as judged by their staining with periodic acid-Schiff (PAS). Also, malate synthase positive peroxisomes were seen in hepatocytes from normal and vitamin-D-treated chicks. Structures positive for this glyoxylate cycle enzyme were rarely seen in the hepatocytes from vitamin-D-deficient animals. Biochemical analyses showed the presence of the two unique glyoxylate cycle enzymes, isocitrate lyase and malate synthase, in chick hepatocytes. The activity of these enzymes was markedly increased in the vitamin-D-replete livers. In addition, chick hepatocytes demonstrated the capacity to oxidize fatty acid in the presence of cyanide. This activity, which is characteristic of peroxisomal B-oxidation rather than mitochondrial, was stimulated by vitamin-D treatment. Lastly, incubation of chick liver in the presence of a fatty acid substrate (palmitate) led to higher tissue glycogen content. The latter was further increased in liver from vitamin-D-replete animals. These data show the presence of glyoxylate cycle enzymes in a higher vertebrate and indicate that this tissue is endowed with the capacity to convert lipid to carbohydrate.
Anat Rec 1990 Jul
PMID:Identification of glyoxylate cycle enzymes in chick liver--the effect of vitamin D3: cytochemistry and biochemistry. 216 96

Peroxisomes were identified in chondrocytes from all zones of the mammalian epiphyseal growth plate by using light microscopic techniques for the cytochemical demonstration of catalase, the marker enzyme for these organelles. Additional cytochemistry showed the presence of malate-synthase-positive structures within the chondrocytes. The latter enzyme, also associated with peroxisomes, is unique to the glyoxylate shunt, a metabolic pathway thought to be absent in vertebrate tissues. The glyoxylate cycle allows the net conversion of lipid to carbohydrate, i.e., gluconeogenesis. Biochemical studies on growth plate cartilage indicate that this tissue has the capacity to carry out cyanide-insensitive B-oxidation of fatty acids. The latter takes place in a nonmitochondrial compartment, most likely the peroxisomal compartment. Additionally, both of the unique enzymes associated with the glyoxylate cycle, i.e., isocitrate lyase and malate synthase, were also identified in a cell-free homogenate of this cartilage. These studies indicate that cartilage, a poorly vascularized tissue characterized by its low oxygen tension and anaerobic glycolysis, may have the capacity to convert lipid to carbohydrate, i.e., gluconeogenesis via the glyoxylate pathway. In this way, cartilage may be unique among mammalian tissues.
Anat Rec 1989 Apr
PMID:Glyoxylate cycle in the epiphyseal growth plate: isocitrate lyase and malate synthase identified in mammalian cartilage. 271 49