Purification of a Novel Serine Proteinase Inhibitor from the Skeletal Muscle of White Croaker (Argyrosomus argentatus)

Cao, Min‐Jie; Osatomi, Kiyoshi; Matsuda, Ryozo; Ohkubo, Makoto; Hara, Kenji; Ishihara, Tadashi

doi:10.1006/bbrc.2000.2803

Cited by 61 publications

(50 citation statements)

References 12 publications

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“…Molecular cloning and sequencing have identified PGI as an autocrine motility factor (AMF) found to be a major cell motility-stimulating factor associated with cancer development and progression (7)(8)(9). PGI was found to be a neuroleukin that promotes growth of embryonic spinal and sensory neurons (10), a maturation factor mediating differentiation of human myeloid leukemia cells (11), sperm antigen-36 (12), and a myofibril-bound serine proteinase inhibitor (13). Of note, aberrations in PGI expressions or activities due to mutations or deletions in PGI are of significant clinical importance because mutations in PGI lead to hereditary nonspherocytic hemolytic anemia disease (14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Funasaka

Yanagawa

et al. 2007

Cancer Research

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Phosphoglucose isomerase (PGI) is one of the glycolytic enzymes and is a multifunctional enzyme that functions in glucose metabolism inside the cell while acting as a cytokine outside the cell, with properties that include autocrine motility factor (AMF) regulating tumor cell motility. Although there are many studies indicating that PGI/AMF has been implicated in progression of metastasis, no direct studies of the significance of exogenous PGI/AMF on tumor progression have been reported. Here, we report on the mesenchymal-toepithelial transition (MET), which is the reverse phenomenon of the epithelial-to-mesenchymal transition that is associated with loss of cell polarity, loss of epithelia markers, and enhancement of cell motility essential for tumor cell invasion and metastasis. Mesenchymal human fibrosarcoma HT1080 cells, which have naturally high levels of endogenous and exogenous PGI/AMF, were stably transfected with PGI

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Section: Introductionmentioning

confidence: 99%

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Funasaka

Yanagawa

et al. 2007

Cancer Research

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“…[2][3][4]. Other functions of PGI/AMF are as T cell lymphokine (e.g., neuroleukin) that supports the survival of spinal and sensory neurons (5), maturation factor that differentiates myeloid leukemic cells to terminal monocytic cells (6), sperm antigen-36 (7), and myofibril-bound serine proteinase inhibitor (8). In addition, PGI/ AMF is an antigen of arthritis diseases (9) and is detected in rheumatoid synovial fluid (10).…”

Section: Introductionmentioning

confidence: 99%

Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Activities by the Poly(ADP-Ribose) Polymerase Family-14

et al. 2007

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“…These proteins promote antibody secretion by mononuclear cells, tumor cell motility, and differentiation of leukemia cells and a promyelocytic cell line (HL-60 cells), respectively. More recently, PGI has also been identified as the antigen involved in rheumatoid arthritis of a mouse line (13), as a specific inhibitor toward myofibril-bound serine proteinase (14), and as the surface antigen involved in sperm agglutination (15). Because very little is known about how PGI is precisely involved in these various biological processes, this moonlighting protein (16) has been the subject of intense investigations.…”

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confidence: 99%

The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho- d -arabinonohydroxamic acid

Arsenieva

Hardré

Salmon

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

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Phosphoglucose isomerase (EC 5.3.1.9) catalyzes the second step in glycolysis, the reversible isomerization of D-glucose 6-phosphate to D-fructose 6-phosphate. The reaction mechanism involves acid-base catalysis with proton transfer and proceeds through a cis-enediol(ate) intermediate. 5-Phospho-D-arabinonohydroxamic acid (5PAH) is a synthetic small molecule that resembles the reaction intermediate, differing only in that it has a nitrogen atom in place of C1. Hence, 5PAH is the best inhibitor of the isomerization reaction reported to date with a Ki of 2 ؋ 10 ؊7 M. Here we report the crystal structure of rabbit phosphoglucose isomerase complexed with 5PAH at 1.9 Å resolution. The interaction of 5PAH with amino acid residues in the enzyme active site supports a model of the catalytic mechanism in which Glu-357 transfers a proton between C1 and C2 and Arg-272 helps stabilize the intermediate. It also suggests a mechanism for proton transfer between O1 and O2. P hosphoglucose isomerase (PGI; EC 5.3.1.9) is a cytosolic glycolytic enzyme that catalyzes the reversible isomerization of D-glucose 6-phosphate (G6P) to D-fructose 6-phosphate (F6P). In addition to isomerase activity, PGI has been shown to display anomerase activity between pyranose anomers of G6P (1), between furanose anomers of F6P (2), and between those of D-mannose 6-phosphate (3), as well as C-2-epimerase activity on G6P (4). It also has roles in protein glycosylation, gluconeogenesis, and the pentose phosphate pathway (5). This central role in the metabolism of phosphorylated sugars explains the strong impact of PGI deficiency in humans (6, 7), as well as the interest as a therapeutic target in parasite metabolism (8). The PGI polypeptide chain, or perhaps a variation thereof, also has extracellular roles as neuroleukin, autocrine motility factor, and differentiation and maturation mediator (9-12). These proteins promote antibody secretion by mononuclear cells, tumor cell motility, and differentiation of leukemia cells and a promyelocytic cell line (HL-60 cells), respectively. More recently, PGI has also been identified as the antigen involved in rheumatoid arthritis of a mouse line (13), as a specific inhibitor toward myofibril-bound serine proteinase (14), and as the surface antigen involved in sperm agglutination (15). Because very little is known about how PGI is precisely involved in these various biological processes, this moonlighting protein (16) has been the subject of intense investigations.Biochemical characterization of PGI began over 50 years ago and includes inhibitor studies (1,(17)(18)(19)(20)(21)(22)(23)(24)(25), labeling studies (26-32), solvent exchange (33, 34), mutagenesis (35,36), and pH profile studies (20,37). A proposed multistep catalytic mechanism includes a ring-opening step followed by an isomerization step. The isomerization step proceeds via general acid-base catalysis with proton transfer. In the G6P to F6P direction, abstraction of the proton from C2 by an active site amino acid residue yields a 1,2-cis-enediol(ate) in...

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Purification of a Novel Serine Proteinase Inhibitor from the Skeletal Muscle of White Croaker (Argyrosomus argentatus)

Cited by 61 publications

References 12 publications

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Down-Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Results in Mesenchymal-to-Epithelial Transition of Human Lung Fibrosarcoma Cells

Regulation of Phosphoglucose Isomerase/Autocrine Motility Factor Activities by the Poly(ADP-Ribose) Polymerase Family-14

The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho- d -arabinonohydroxamic acid

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