Purification, characterization and developmental expression of chick (Gallus domesticus) liver PSP protein+

Nordin, H; Matsumoto, Mitsuharu; Suzuki, Kaoru; Kaneki, K.; Natori, Yasuo; Kishi, Kazushi; Oka, Tatsuzo

doi:10.1016/s1096-4959(00)00308-0

Cited by 12 publications

(6 citation statements)

References 9 publications

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“…A natural calpain activator protein has been isolated from the bovine brain and when characterized was found to be very similar to goat liver UK114 (16). Biological studies of its function suggest that it may play a role in cellular differentiation and development because levels are significantly increased during differentiation from human monocytes to macrophages (17) and during the development process of rat kidney, rat brain, pig liver, and chick liver (11,(18)(19)(20). Furthermore, expression of PSP depends on the proliferation states of the cell and overexpression of PSP reduces cell proliferation of normal rat kidney epithelial NRK-52E cells (21,22).…”

Section: Introductionmentioning

confidence: 99%

Decreased Expression of UK114 Is Related to the Differentiation Status of Human Hepatocellular Carcinoma

Chong

Huang²,

et al. 2008

Cancer Epidemiology, Biomarkers &Amp; Prevention

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Previous studies have identified that the expression of UK114 is tissue specific and the protein has been found to be most abundant in liver and kidney. However, the expression of UK114 in human hepatocellular carcinoma and its relationship to differentiation and transformation of hepatocellular carcinoma have not been studied. In this study, the expression of UK114 in human hepatocellular carcinoma was examined by Northern and Western blot analyses. We found that UK114 was significantly down-regulated in most of hepatocellular carcinoma tissues compared with adjacent nontumor tissues (72.7%) at both mRNA and protein levels. We looked into the possibility that this decreased expression of UK114 in the hepatocellular carcinoma tissues may play a role in the differentiation or tumorigenicity of hepatocellular carcinoma. Immunohistochemical staining showed that the reduced expression of UK114 in hepatocellular carcinoma tissues was correlated with the tumor differentiation status as graded by the Edmondson-Steiner classification. On the other hand, overexpression of UK114 was not able to suppress the proliferation of human hepatoma cells and tumorigenicity in nude mice. These results suggest that UK114 does not seem to act as a tumor suppressor gene; however, it may useful as a biomarker that will assist in the grading of the differentiation status of hepatocellular carcinoma samples. (Cancer Epidemiol Biomarkers Prev 2008;17(3):535 -42)

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Section: Introductionmentioning

confidence: 99%

Decreased Expression of UK114 Is Related to the Differentiation Status of Human Hepatocellular Carcinoma

Chong

Huang²,

et al. 2008

Cancer Epidemiology, Biomarkers &Amp; Prevention

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“…Perchloric acid‐soluble protein (PSP) was originally isolated from rat liver (RL‐PSP) [1]. Subsequently, we isolated and characterized PSP from rat kidney (RK‐PSP) [2], rat brain (RB‐PSP) [3], rat lung (RLu‐PSP) [4], chick liver (CL‐PSP) [5] and pig liver (PL‐PSP) [6]. Proteins homologous to PSP were also characterized in mice (Hrp 12) [7], goats (UK‐114) [8] and humans (p14.5) [9].…”

Section: Introductionmentioning

confidence: 99%

Perchloric acid‐soluble protein regulates cell proliferation and differentiation in the spinal cord of chick embryos

et al. 2005

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The role of perchloric acid-soluble protein (PSP) was investigated in chick embryos. Fluorescently labeled anti-chick liver (CL)-PSP IgG was injected into the yolk sac in ovo at embryonic day 3, and became localized in neuroepithelial cells. Within 12 h, morphological changes were observed in 37.5% of anti-CL-PSP IgG-injected embryos, and the neuroepithelial cells formed a wavy line. No significant changes were observed in embryos injected with non-immune IgG or PBS. Increased expression of PCNA and decreased expression of neuronal class III b-tubulin were observed in the spinal cord after anti-CL-PSP IgG injection. These results suggest that PSP controls the proliferation and differentiation of neuroepithelial cells in chick embryos.

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“…Perchloric acid–soluble protein (PSP) was initially isolated from the rat liver as a translational inhibitor (Oka et al 1995). Subsequently, it was also found in various other species, including humans (Schmiedeknecht et al 1996), mice (Samuel et al 1997), goats (Ceciliani et al 1996), Escherichia coli (Colombo et al 1998), chicks (Nordin et al 2001), Saccharomyces cerevisiae (Kim et al 2001), pigs (Kaneki et al 2003b), and so on. Since its gene (a member of the YER057c/YJGF family) is highly conserved during evolution, PSP may play important roles in the cell.…”

mentioning

confidence: 97%

“…Since its gene (a member of the YER057c/YJGF family) is highly conserved during evolution, PSP may play important roles in the cell. In mammals, PSP has been reported to be associated with various functions, including ribonuclease activity (Morishita et al 1999; Sawasaki et al 2001), fatty acid‐binding activity (Sasagawa et al 1999), differentiation‐dependent expression (Oka et al 1995; Asagi et al 1998; Nordin et al 2001; Suzuki et al 2001; Kaneki et al 2003a), and repression of proliferation (Kanouchi et al 2001). However, the precise biological function of PSP has not yet been elucidated.…”

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confidence: 99%

Nuclear transfer of perchloric acid–soluble protein by endoplasmic reticulum stressors

Kanouchi

Matsumoto

Taga³

et al. 2005

Protein Science

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Perchloric acid-soluble protein (PSP) is highly conserved during evolution from bacteria to mammals. Although PSP has been recognized as an inhibitor of translation and proliferation in vitro, its precise biological role has not yet been elucidated. Since we previously found similar distributions for PSP and the endoplasmic reticulum (ER) and Golgi complex, the intracellular distribution of PSP was analyzed in more detail. Immunofluorescence studies indicated that PSP co-localized with the ER and Golgi complex, since the distribution pattern of PSP was well matched to both of these organelles. An immunoelectron microscopic study revealed PSP was located not only in the cytosol but also on the surface of the outer ER membrane. Since PSP was present on the ER, we speculated that it may be associated with ER function. Therefore, we analyzed whether or not the ER stress response, which is one of the ER functions, affected PSP expression. The results showed that various ER stressors (thapsigargin, A23187, tunicamycin, brefeldin A, and cisplatin) provoked a dramatic change in the localization of PSP from outside of the nucleus to inside the nucleus within 3 h. Moreover, the ER stressors induced PSP expression. These results suggest that PSP is involved in the cellular response to ER stressors, and that the change in localization of PSP from the ER to the nucleus may be associated with ER stress responses.Keywords: perchloric acid; soluble protein; m-calpain; endoplasmic reticulum; ER stress; thapsigargin Perchloric acid-soluble protein (PSP) was initially isolated from the rat liver as a translational inhibitor (Oka et al. 1995). Subsequently, it was also found in various other species, including humans (Schmiedeknecht et al. (Kaneki et al. 2003b), and so on. Since its gene (a member of the YER057c/YJGF family) is highly conserved during evolution, PSP may play important roles in the cell. In mammals, PSP has been reported to be associated with various functions, including ribonuclease activity (Morishita et al. 1999;Sawasaki et al. 2001), fatty acid-binding activity (Sasagawa et al. 1999), differentiation-dependent expression (Oka et al. 1995;Asagi et al. 1998;Nordin et al. 2001;Suzuki et al. 2001;Kaneki et al. 2003a), and repression of proliferation . However, the precise biological function of PSP has not yet been elucidated. Reprint requests to: Hiroaki Kanouchi, Department of Biochemistry, Kawasaki Medical School, 577 Matsushima, Kurashiki-city, Okayama, 701-0192, Japan; e-mail: kanouchihiroaki@mac.com; fax: +81-86-462-1199.Abbreviations: PSP, perchloric acid-soluble protein; ER, endoplasmic reticulum; GRP78, 78 kDa glucose regulated protein/BiP; D-PSP, Dorosophia ortholog PSP.Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi

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Purification, characterization and developmental expression of chick (Gallus domesticus) liver PSP protein+

Cited by 12 publications

References 9 publications

Decreased Expression of UK114 Is Related to the Differentiation Status of Human Hepatocellular Carcinoma

Decreased Expression of UK114 Is Related to the Differentiation Status of Human Hepatocellular Carcinoma

Perchloric acid‐soluble protein regulates cell proliferation and differentiation in the spinal cord of chick embryos

Nuclear transfer of perchloric acid–soluble protein by endoplasmic reticulum stressors

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