نتایج جستجو برای: mannose 1 phosphate guanyltransferas

تعداد نتایج: 2826486  

Journal: :Journal of immunology 2008
Akira Abe Robert Kelly Jessica Kollmeyer Miki Hiraoka Ye Lu James A Shayman

Macrophages have long been known to secrete a Phospholipase A(2) with an acidic pH optimum in response to phagocytic stimuli. However, the enzyme or enzymes responsible for this activity have not been identified. We report that mouse alveolar macrophages release lysosomal phospholipase A(2) (LPLA(2)) into the medium of cultured cells following stimulation with zymosan. The release of the enzyme...

2015
Mukesh Meena Vishal Prasad Andleeb Zehra Vijai K. Gupta Ram S. Upadhyay

Numerous plants and fungi produce mannitol, which may serve as an osmolyte or metabolic store; furthermore, mannitol also acts as a powerful quencher of reactive oxygen species (ROS). Some phytopathogenic fungi use mannitol to stifle ROS-mediated plant resistance. Mannitol is essential in pathogenesis to balance cell reinforcements produced by both plants and animals. Mannitol likewise serves a...

Journal: :The Journal of biological chemistry 1981
A R Robbins R Myerowitz R J Youle G J Murray D M Neville

The localization of acid hydrolases was examined in Chinese hamster ovary cells with defective mannose 6-phosphate receptors; these mutants had been shown to exhibit reduced uptake and altered binding of exogenously added acid hydrolase (Robbins, A. R., Myerowitz, R., Youle, R. J., Murray, G. J., and Neville, D. M., Jr. (1981) J. Biol. Chem. 256, 10618-10622). Cells were grown in the presence o...

2017
Valentina Citro Chiara Cimmaruta Ludovica Liguori Gaetano Viscido Maria Vittoria Cubellis Giuseppina Andreotti

The most frequent disorder of glycosylation, PMM2-CDG, is caused by a deficiency of phosphomannomutase activity. In humans two paralogous enzymes exist, both of them require mannose 1,6-bis-phosphate or glucose 1,6-bis-phosphate as activators, but only phospho-mannomutase1 hydrolyzes bis-phosphate hexoses. Mutations in the gene encoding phosphomannomutase2 are responsible for PMM2-CDG. Although...

Journal: :The Journal of biological chemistry 1993
L A Bach S Hsieh K Sakano H Fujiwara J F Perdue M M Rechler

A family of six specific insulin-like growth factor binding proteins (IGFBPs) modulates the biological actions of the insulin-like growth factors, IGF-I and IGF-II. In the present study, we determined the binding affinity of purified human IGFBPs 1-6 for recombinant human IGF-II mutants whose binding to IGF-I, IGF-II/mannose 6-phosphate, and insulin receptors was previously reported (Sakano, K....

Journal: :Acta crystallographica. Section D, Biological crystallography 2004
Michael K Swan Thomas Hansen Peter Schönheit Christopher Davies

Phosphoglucose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) shows virtually no sequence similarity to its counterparts from bacterial and eukaryotic sources and belongs to a unique group within the PGI superfamily. Whereas conventional PGIs show strict substrate specificity for glucose 6-phosphate and fructose 6-phosphate, PaPGI/PMI can also catalyse the isomerization of m...

Journal: :The Journal of biological chemistry 1977
A Heifetz A D Elbein

A particulate fraction from porcine aorta catalyzed the incorporation of N-acetylglucosamine (GlcNAc) from UDP-[3H]GlcNAc into both GlcNAc-pyrophosphorylpolyprenol and GlcNAc-GlcNAc-pyrophosphorylpolyprenol. This transfer utilized endogenous lipid and required a divalent cation. Mn2+ was the best metal ion and was optimum at 2.3 mM. This same particulate fraction was previously shown to transfe...

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