Two Candidate Downstream Target Genes for E2A-HLF

Kurosawa, Hidemitsu; Goi, Kumiko; Inukai, Takeshi; Inaba, Toshiya; Chang, Kun-San; Shinjyo, Tetsuharu; Rakestraw, Karen M.; Naeve, Clayton W.; Look, A. Thomas

doi:10.1182/blood.v93.1.321

Cited by 43 publications

(12 citation statements)

References 57 publications

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“…1 a ). Combined with data from previous reports,1, 2 SRPX2 mRNA appears to be widely observed in normal tissues, with particularly high levels detected in the placenta and lung.…”

Section: Resultssupporting

confidence: 75%

“…Although the meaning of SRPX2 overexpression in gastric cancer is unclear, a real‐time RT‐PCR analysis of clinical samples showed that SRPX2 expression is associated with a poor prognosis in patients with gastric cancer. SRPX2 was first identified as a downstream molecule of E2F‐HLF in pro‐B acute leukemia with t(17;19) (q23;p13) and has since been reported to contribute to malignant phenotypes 1 . E2F‐HLF ‐positive leukemia is characterized by a poor outcome with bone invasion, hypercalcemia and intravascular coagulation 24.…”

Section: Discussionmentioning

confidence: 99%

“…SRPX2 (Sushi repeat containing protein, X‐linked 2) was first identified as SRPUL (Sushi repeat protein upregulated in leukemia) by Kurosawa et al 1 The E2A‐HLF fusion gene causes B‐cell precursor acute lymphoblastic leukemia, which is characterized by an unusual paraneoplastic syndrome comprising intravascular coagulation and hypercalcemia; one of the target genes of E2A‐HLF is SRPX2 . Apart from the possible involvement of this gene in malignant diseases, a disease‐causing mutation (p.N327S) in SRPX2 resulting in a gain‐of‐glycosylation aberration in the secreted mutant protein, and the mutation actually leads to rolandic epilepsy with oral and speech dyspraxia and with mental retardation in the French family 2.…”

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confidence: 99%

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SRPX2 is overexpressed in gastric cancer and promotes cellular migration and adhesion

Tanaka

Arao

Maegawa

et al. 2008

Intl Journal of Cancer

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SRPX2 (Sushi repeat containing protein, X-linked 2) was first identified as a downstream molecule of the E2A-HLF fusion gene in t(17;19)-positive leukemia cells and the biological function of this gene remains unknown. We found that SRPX2 is overexpressed in gastric cancer and the expression and clinical features showed that high mRNA expression levels were observed in patients with unfavorable outcomes using real-time RT-PCR. The cellular distribution of SRPX2 protein showed the secretion of SRPX2 into extracellular regions and its localization in the cytoplasm. The introduction of the SRPX2 gene into HEK293 cells did not modulate the cellular proliferative activity but did enhance the cellular migration activity, as shown using migration and scratch assays. The conditioned-medium obtained from SRPX2-overexpressing cells increased the cellular migration activity of a gastric cancer cell line, SNU-16. In addition, SRPX2 protein remarkably enhanced the cellular adhesion of SNU-16 and HSC-39 and increased the phosphorylation levels of focal adhesion kinase (FAK), as shown using western blotting, suggesting that SRPX2 enhances cellular migration and adhesion through FAK signaling. In conclusion, the overexpression of SRPX2 enhances cellular migration and adhesion in gastric cancer cells. Here, we report that the biological functions of SRPX2 include cellular migration and adhesion to cancer cells.

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“…1 a ). Combined with data from previous reports,1, 2 SRPX2 mRNA appears to be widely observed in normal tissues, with particularly high levels detected in the placenta and lung.…”

Section: Resultssupporting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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SRPX2 is overexpressed in gastric cancer and promotes cellular migration and adhesion

Tanaka

Arao

Maegawa

et al. 2008

Intl Journal of Cancer

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“…It was described as a downstream target gene for E2A-HLF fusion gene. 5 The SRPX2 protein consists of 465 amino acid residues, including one DUF4174 domain, three sushi repeat domains, and one hyaline repeat (HYR) domain (GenBank NP-055282). Some of the initial studies have shown that SRPX2 plays a crucial role in the development of the cerebral language center.…”

Section: Introductionmentioning

confidence: 99%

High SRPX2 protein expression predicts unfavorable clinical outcome in patients with prostate cancer

Zhang¹,

Li²,

Fan³

et al. 2018

OTT

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BackgroundSushi repeat-containing protein X-linked 2 (SRPX2) is overexpressed in a variety of different tumor tissues and correlated with poor prognosis in patients. Little research focuses on the role of SRPX2 expression in prostate cancer (PCa), and the clinicopathological significance of the protein expression in this tumor is relatively unknown. However, our previous transcriptome data from those cancer stem-like cells indicated the role of SRPX2 in PCa.Materials and methodsIn this study, RT-PCR and Western blotting were firstly used to examine the SRPX2 expression in three PCa cell lines including LNCaP, DU145, and PC3, and then SRPX2 protein expression was immunohistochemically investigated and statistically analyzed in a series of 106 paraffin-embedded PCa tissue specimens.ResultsSignificantly lower levels of SRPX2 expression were verified in the LNCaP cells, compared with the expression in the aggressive DU145 and PC3 cells, in both mRNA and protein levels. Immunohistochemically, there were variable SRPX2 protein expressions in the clinical samples. Moreover, high levels of SRPX2 expression in the PCa tissues were significantly associated with Gleason score (P=0.008), lymph node metastasis (P=0.009), and distant metastasis (P=0.021). Furthermore, higher levels of SRPX2 expression in the PCa tissues were significantly associated with shorter overall survival (OS) (P<0.001).ConclusionOur results demonstrate that SRPX2 is highly expressed in aggressive PCa cells in vitro, and its protein expression in PCa is significantly associated with malignant clinical features and shorter OS, strongly indicating its prognostic value in prostate cancers.

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“…Annexin VIII expression has also been described in a number of pathological states. Annexin VIII expression is up‐regulated in acute promyelocytic lymphocyte (APL) (29,30) and also in pro‐B leukemia cell lines (31) . It has been proposed that annexin VIII may have a role in the coagulopathies associated with these disorders and may play a role in the hypercalcemia, which is associated with pro‐B leukemia (30) .…”

Section: Discussionmentioning

confidence: 99%

Annexin VIII Is Differentially Expressed by Chondrocytes in the Mammalian Growth Plate During Endochondral Ossification and in Osteoarthritic Cartilage

White

Watson

Newman

et al. 2002

Journal of Bone and Mineral Research

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Endochondral ossification is the developmental process that leads to the formation and coordinated longitudinal growth of the majority of the vertebrate skeleton. Central to this process is chondrocyte differentiation occurring in the growth plate that lies at the junction between the epiphyseal cartilage and the bone. To identify novel factors involved in this differentiation process, suppression subtractive hybridization was performed to amplify preferentially cDNAs uniquely expressed in fetal bovine growth plate chondrocytes as opposed to epiphyseal chondrocytes. The subtracted product was used to screen a fetal bovine chondrocyte cDNA library. One of the cDNA clones identified encoded the bovine orthologue of annexin VIII, a protein not previously described in the growth plate. Northern and Western blotting confirmed that annexin VIII was expressed by growth plate chondrocytes and not by epiphyseal chondrocytes. Immunohistochemistry of the fetal bovine growth plate identified a gradient of increasing annexin VIII protein from the proliferative to the hypertrophic zone. Immunofluorescence localized annexin VIII largely to the chondrocyte cell membrane. In a preliminary study, we examined the distribution of annexin VIII in normal and osteoarthritic (OA) articular cartilage. In OA cartilage, the protein was located in a subset of mid-to deep zone chondrocytes and in the matrix surrounding these cells; no annexin VIII was detected in normal articular cartilage. Thus annexin VIII is a marker for chondrocyte differentiation during normal endochondral ossification and may act as a marker for cells undergoing inappropriate differentiation in OA. (J Bone Miner Res 2002;17:1851-1858)

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Two Candidate Downstream Target Genes for E2A-HLF

Cited by 43 publications

References 57 publications

SRPX2 is overexpressed in gastric cancer and promotes cellular migration and adhesion

SRPX2 is overexpressed in gastric cancer and promotes cellular migration and adhesion

High SRPX2 protein expression predicts unfavorable clinical outcome in patients with prostate cancer

Annexin VIII Is Differentially Expressed by Chondrocytes in the Mammalian Growth Plate During Endochondral Ossification and in Osteoarthritic Cartilage

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