Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan

Kaul, Sunil C.; Sugihara, Takashi; Yoshida, Akira; Nomura, Hitoshi; Wadhwa, Renu

doi:10.1038/sj.onc.1203696

Cited by 34 publications

(28 citation statements)

References 39 publications

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“…sequences in collagens, especially type IV and V collagens. The possible involvement of the P3H genes in human tumourigenesis was explored because ectopic expression of P3H1 was reported to cause growth arrest in fibroblasts (Kaul et al, 2000). There are three P3H proteins encoded in the human genome, P3H1, P3H2 and P3H3.…”

Section: Discussionmentioning

confidence: 99%

The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer

et al. 2009

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Expression of P3H2 (Leprel1) and P3H3 (Leprel2) but not P3H1 (Leprecan) is down-regulated in breast cancer by aberrant CpG methylation in the 5 0 regulatory sequences of each gene. Methylation of P3H2 appears specific to breast cancer as no methylation was detected in a range of cell lines from other epithelial cancers or from primary brain tumours or malignant melanoma. Methylation in P3H2, but not P3H3, was strongly associated with oestrogen-receptor-positive breast cancers, whereas methylation in P3H3 was associated with higher tumour grade and Nottingham Prognostic Index. Ectopic expression of P3H2 and P3H3 in cell lines with silencing of the endogenous gene results in suppression of colony growth. This is the first demonstration of epigenetic inactivation of prolyl hydroxylases in human cancer, implying that this gene family represents a novel class of tumour suppressors. The restriction of silencing in P3H2 to breast carcinomas, and its association with oestrogen-receptor-positive cases, suggests that P3H2 may be a breast-cancer-specific tumour suppressor.

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Section: Discussionmentioning

confidence: 99%

The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer

et al. 2009

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“…1A). The two different transcripts are thought to represent a long form and an alternatively spliced shorter form, both of which have previously been found to be associated with certain human tissues and transformed cells (Kaul et al, 2000). P3H1 expression was not detected in skeletal muscle by northern blot analysis with either the 3'UTR probe or with an internal probe (see Methods).…”

Section: Northern Blot Analysis Of P3h1 P3h2 and P3h3 Expression In mentioning

confidence: 99%

Expression of Prolyl 3-hydroxylase Genes in Embryonic and Adult Mouse Tissues

Vranka

Stadler

Bächinger

2009

Cell Struct. Funct.

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ABSTRACT. Collagen requires hydroxylation of its proline residues to achieve proper assembly, structure, and function. Prolyl 4-hydroxylase catalyzes formation of 4-hydroxyproline, which is essential for collagen triple helix formation and stability. Prolyl 3-hydroxylase catalyzes formation of 3-hydroxyproline, which is far less abundant in collagens and whose function remains unclear. Recently mutations in prolyl 3-hydroxylase 1 have been associated with osteogenesis imperfecta, yet the temporal and spatial expression patterns of the prolyl 3-hydroxylase family members during development and in adult tissues remain undefined. By northern blot analysis distinct differences in transcript sizes of the three prolyl 3-hydroxylase genes were detected. Quantitative RTPCR demonstrated tissue-specific differences in prolyl 3-hydroxylase expression, most notable of which were high levels of prolyl 3-hydroxylase 2 in kidney and prolyl 3-hydroxylase 1 expression in embryonic tissues. Finally, in situ hybridization was used to assess spatio-temporal distribution of three prolyl 3-hydroxylases at embryonic days 11-15. Importantly, prolyl 3-hydroxylase 1 was expressed within cartilage condensations of the vertebral bodies and in the aortic arch of the developing heart, whereas prolyl 3-hydroxylase 2 was expressed in developing lens capsule. The prolyl 3-hydroxylase 3 gene showed more generalized expression overlapping somewhat with the other two genes. This report characterizes expression of the three prolyl 3-hydroxylase genes in embryonic and adult mice. Overall these data demonstrate tissue specific prolyl 3-hydroxylase gene expression in both fetal and adult tissues indicating a developmental role for prolyl 3-hydroxylase activity.

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“…Interestingly, the initial screen of ES cells demonstrated that message was present for a wide variety of PG core proteins, including many that have been shown to have tightly regulated spatiotemporal distribution in vivo. These include HSPG syndecan 3 and chondroitin sulfate proteoglycans (CSPGs) testican [24] and leprecan [25]. However, the CSPG NG2, often used as a neural-specific marker [26], was found only in the day 7 cells (both GFP-positive and GFP-negative).…”

Section: Differential Changes In Gene Expressionmentioning

confidence: 99%

Essential Alterations of Heparan Sulfate During the Differentiation of Embryonic Stem Cells to Sox1-Enhanced Green Fluorescent Protein-Expressing Neural Progenitor Cells

et al. 2007

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Embryonic stem (ES) cells can be cultured in conditions thateither maintain pluripotency or allow differentiation to the three embryonic germ layers. Heparan sulfate (HS), a highly polymorphic glycosaminoglycan, is a critical cell surface coreceptor in embryogenesis, and in this paper we describe its structural transition from an unusually low-sulfated variant in ES cells to a more highly sulfated form in fluorescence-activated cell sorting-purified neural progenitor cells. The characteristic domain structure of HS was retained during this transformation. However, qualitative variations in surface sulfation patterns between ES and differentiated cells were revealed using HS epitope-specific antibodies and the HS-binding growth factor fibroblast growth factor 2 (FGF-2). Expression profiles of the HS modification enzymes indicated that both "early" (N-sulfotransferases) and "late" (6O-and 3O-sulfotransferases) sulfotransferases contributed to the alterations in sulfation patterning. An HS-null ES line was used to demonstrate the necessity for HS in neural differentiation. HS is a coreceptor for many of the protein effectors implicated in pluripotency and differentiation (e.g., members of the FGF family, bone morphogenic proteins, and fibronectin). We suggest that the stage-specific activities of these proteins are finely regulated by dynamic changes in sulfation motifs in HS chains.

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Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan

Cited by 34 publications

References 39 publications

The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer

The prolyl 3-hydroxylases P3H2 and P3H3 are novel targets for epigenetic silencing in breast cancer

Expression of Prolyl 3-hydroxylase Genes in Embryonic and Adult Mouse Tissues

Essential Alterations of Heparan Sulfate During the Differentiation of Embryonic Stem Cells to Sox1-Enhanced Green Fluorescent Protein-Expressing Neural Progenitor Cells

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