Literature DB >> 1639752

Subcellular distribution of glycolyltransferases in rodent liver and their significance in special reference to the synthesis of N-glycolyneuraminic acid.

J Vamecq1, N Mestdagh, J P Henichart, J Poupaert.   

Abstract

The enzymic synthesis, transfer, and utilization of glycolyl-CoA (i.e. 2-hydroxyacetyl-CoA) have been studied in rat and mouse livers. On the one hand, these tissues contain the enzyme activities allowing the synthesis of glycolyl-CoA from fatty acids (palmitate omega-hydroxylase, omega-hydroxypalmitoyl-CoA synthetase, and mitochondrial beta-oxidation of omega-hydroxypalmitoyl-CoA) and 3-hydroxypyruvic acid (oxidation by intact mitochondria). On the other hand, three types of glycolyltransferase activities can be demonstrated in rodent livers, depending on either carnitine, glucosamine, or glucosamine-6-phosphate. The subcellular distributions of these glycolyltransferase activities are similar to those of the corresponding acetyltransferase counterparts. Concerning carnitine glycolytransferase, the activity is widely distributed in the subcellular fractions, pointing out its occurrence in most cell compartments. By contrast, the glucosamine and glucosamine-6-phosphate glycolytransferase activities were located preferentially in the microsomal fraction. The condensation between glycolyl-CoA and glucosamine (or glucosamine-6-phosphate) raises the interesting question of the nature and the role of the resulting glycolylglucosamine molecule, especially in an alternative N-glycolylneuraminic acid synthesis pathway.

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Year:  1992        PMID: 1639752     DOI: 10.1093/oxfordjournals.jbchem.a123800

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  8 in total

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2.  A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence.

Authors:  H H Chou; H Takematsu; S Diaz; J Iber; E Nickerson; K L Wright; E A Muchmore; D L Nelson; S T Warren; A Varki
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-29       Impact factor: 11.205

Review 3.  NGcGM3 ganglioside: a privileged target for cancer vaccines.

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Journal:  Clin Dev Immunol       Date:  2010-10-27

Review 4.  Involvement of a non-human sialic Acid in human cancer.

Authors:  Annie N Samraj; Heinz Läubli; Nissi Varki; Ajit Varki
Journal:  Front Oncol       Date:  2014-02-19       Impact factor: 6.244

5.  Tumor Trp53 status and genotype affect the bone marrow microenvironment in acute myeloid leukemia.

Authors:  Rodrigo Jacamo; R Eric Davis; Xiaoyang Ling; Sonali Sonnylal; Zhiqiang Wang; Wencai Ma; Min Zhang; Peter Ruvolo; Vivian Ruvolo; Rui-Yu Wang; Teresa McQueen; Scott Lowe; Johannes Zuber; Steven M Kornblau; Marina Konopleva; Michael Andreeff
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6.  Antitumor effects of the GM3(Neu5Gc) ganglioside-specific humanized antibody 14F7hT against Cmah-transfected cancer cells.

Authors:  Denise Dorvignit; Kayluz F Boligan; Ernesto Relova-Hernández; Marilyn Clavell; Armando López; Mayrel Labrada; Hans-Uwe Simon; Alejandro López-Requena; Circe Mesa; Stephan von Gunten
Journal:  Sci Rep       Date:  2019-07-09       Impact factor: 4.379

Review 7.  Loss of N-glycolylneuraminic acid in humans: Mechanisms, consequences, and implications for hominid evolution.

Authors:  A Varki
Journal:  Am J Phys Anthropol       Date:  2001       Impact factor: 2.868

Review 8.  From "Serum Sickness" to "Xenosialitis": Past, Present, and Future Significance of the Non-human Sialic Acid Neu5Gc.

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  8 in total

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