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Journal articles on the topic 'CCN3'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

MacDonald, Iona J., Chien-Chung Huang, Shan-Chi Liu, Yen-You Lin, and Chih-Hsin Tang. "Targeting CCN Proteins in Rheumatoid Arthritis and Osteoarthritis." International Journal of Molecular Sciences 22, no. 9 (April 21, 2021): 4340. http://dx.doi.org/10.3390/ijms22094340.

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The CCN family of matricellular proteins (CYR61/CCN1, CTGF/CCN2, NOV/CCN3 and WISP1-2-3/CCN4-5-6) are essential players in the key pathophysiological processes of angiogenesis, wound healing and inflammation. These proteins are well recognized for their important roles in many cellular processes, including cell proliferation, adhesion, migration and differentiation, as well as the regulation of extracellular matrix differentiation. Substantial evidence implicates four of the proteins (CCN1, CCN2, CCN3 and CCN4) in the inflammatory pathologies of rheumatoid arthritis (RA) and osteoarthritis (OA). A smaller evidence base supports the involvement of CCN5 and CCN6 in the development of these diseases. This review focuses on evidence providing insights into the involvement of the CCN family in RA and OA, as well as the potential of the CCN proteins as therapeutic targets in these diseases.

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2

Brigstock, DR. "The CCN family: a new stimulus package." Journal of Endocrinology 178, no. 2 (August 1, 2003): 169–75. http://dx.doi.org/10.1677/joe.0.1780169.

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The CCN family comprises cysteine-rich 61 (CYR61/CCN1), connective tIssue growth factor (CTGF/CCN2), nephroblastoma overexpressed (NOV/CCN3), and Wnt-induced secreted proteins-1 (WISP-1/CCN4), -2 (WISP-2/CCN5) and -3 (WISP-3/CCN6). These proteins stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest and migration of multiple cell types. Many of these activities probably occur through the ability of CCN proteins to bind and activate cell surface integrins. Accumulating evidence supports a role for these factors in endocrine pathways and endocrine-related processes. To illustrate the broad role played by the CCN family in basic and clinical endocrinology, this Article highlights the relationship between CCN proteins and hormone action, skeletal growth, placental angiogenesis, IGF-binding proteins and diabetes-induced fibrosis.

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3

Wu, Qunfeng, Marda Jorgensen, Joanna Song, Junmei Zhou, Chen Liu, and Liya Pi. "Members of the Cyr61/CTGF/NOV Protein Family: Emerging Players in Hepatic Progenitor Cell Activation and Intrahepatic Cholangiocarcinoma." Gastroenterology Research and Practice 2016 (2016): 1–9. http://dx.doi.org/10.1155/2016/2313850.

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Hepatic stem/progenitor cells (HPC) reside quiescently in normal biliary trees and are activated in the form of ductular reactions during severe liver damage when the replicative ability of hepatocytes is inhibited. HPC niches are full of profibrotic stimuli favoring scarring and hepatocarcinogenesis. The Cyr61/CTGF/NOV (CCN) protein family consists of six members, CCN1/CYR61, CCN2/CTGF, CCN3/NOV, CCN4/WISP1, CCN5/WISP2, and CCN6/WISP3, which function as extracellular signaling modulators to mediate cell-matrix interaction during angiogenesis, wound healing, fibrosis, and tumorigenesis. This study investigated expression patterns of CCN proteins in HPC and cholangiocarcinoma (CCA). Mouse HPC were induced by the biliary toxin 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DDC). Differential expression patterns of CCN proteins were found in HPC from DDC damaged mice and in human CCA tumors. In addition, we utilized reporter mice that carried Ccn2/Ctgf promoter driven GFP and detected strong Ccn2/Ctgf expression in epithelial cell adhesion molecule (EpCAM)+ HPC under normal conditions and in DDC-induced liver damage. Abundant CCN2/CTGF protein was also found in cytokeratin 19 (CK19)+ human HPC that were surrounded by α-smooth muscle actin (α-SMA)+ myofibroblast cells in intrahepatic CCA tumors. These results suggest that CCN proteins, particularly CCN2/CTGF, function in HPC activation and CCA development.

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4

Mo, Fan-E., Andrew G. Muntean, Chih-Chiun Chen, Donna B. Stolz, Simon C. Watkins, and Lester F. Lau. "CYR61 (CCN1) Is Essential for Placental Development and Vascular Integrity." Molecular and Cellular Biology 22, no. 24 (December 15, 2002): 8709–20. http://dx.doi.org/10.1128/mcb.22.24.8709-8720.2002.

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ABSTRACT CYR61 (CCN1) is a member of the CCN family of secreted matricellular proteins that includes connective tissue growth factor (CCN2), NOV (CCN3), WISP-1 (CCN4), WISP-2 (CCN5), and WISP-3 (CCN6). First identified as the product of a growth factor-inducible immediate-early gene, CYR61 is an extracellular matrix-associated angiogenic inducer that functions as a ligand of integrin receptors to promote cell adhesion, migration, and proliferation. Aberrant expression of Cyr61 is associated with breast cancer, wound healing, and vascular diseases such as atherosclerosis and restenosis. To understand the functions of CYR61 during development, we have disrupted the Cyr61 gene in mice. We show here that Cyr61-null mice suffer embryonic death: ∼30% succumbed to a failure in chorioallantoic fusion, and the reminder perished due to placental vascular insufficiency and compromised vessel integrity. These findings establish CYR61 as a novel and essential regulator of vascular development. CYR61 deficiency results in a specific defect in vessel bifurcation (nonsprouting angiogenesis) at the chorioallantoic junction, leading to an undervascularization of the placenta without affecting differentiation of the labyrinthine syncytiotrophoblasts. This unique phenotype is correlated with impaired Vegf-C expression in the allantoic mesoderm, suggesting that CYR61-regulated expression of Vegf-C plays a role in vessel bifurcation. The genetic and molecular basis of vessel bifurcation is presently unknown, and these findings provide new insight into this aspect of angiogenesis.

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5

Peng, Linan, Yingying Wei, Yijia Shao, Yi Li, Na Liu, and Lihua Duan. "The Emerging Roles of CCN3 Protein in Immune-Related Diseases." Mediators of Inflammation 2021 (May 18, 2021): 1–8. http://dx.doi.org/10.1155/2021/5576059.

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The CCN proteins are a family of extracellular matrix- (ECM-) associated proteins which currently consist of six secreted proteins (CCN1-6). CCN3 protein, also known as nephroblastoma overexpressed protein (NOV), is a member of the CCN family with multiple biological functions, implicated in major cellular processes such as cell growth, migration, and differentiation. Recently, CCN3 has emerged as a critical regulator in a variety of diseases, including immune-related diseases, including rheumatology arthritis, osteoarthritis, and systemic sclerosis. In this review, we will briefly introduce the structure and function of the CCN3 protein and summarize the roles of CCN3 in immune-related diseases, which is essential to understand the functions of the CCN3 in immune-related diseases.

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6

Resovi, Andrea, Patrizia Borsotti, Tommaso Ceruti, Alice Passoni, Massimo Zucchetti, Alexander Berndt, Bruce L. Riser, Giulia Taraboletti, and Dorina Belotti. "CCN-Based Therapeutic Peptides Modify Pancreatic Ductal Adenocarcinoma Microenvironment and Decrease Tumor Growth in Combination with Chemotherapy." Cells 9, no. 4 (April 13, 2020): 952. http://dx.doi.org/10.3390/cells9040952.

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The prominent desmoplastic stroma of pancreatic ductal adenocarcinoma (PDAC) is a determinant factor in tumor progression and a major barrier to the access of chemotherapy. The PDAC microenvironment therefore appears to be a promising therapeutic target. CCN2/CTGF is a profibrotic matricellular protein, highly present in the PDAC microenvironment and associated with disease progression. Here we have investigated the therapeutic value of the CCN2-targeting BLR100 and BLR200, two modified synthetic peptides derived from active regions of CCN3, an endogenous inhibitor of CCN2. In a murine orthotopic PDAC model, the two peptides, administered as monotherapy at low doses (approximating physiological levels of CCN3), had tumor inhibitory activity that increased with the dose. The peptides affected the tumor microenvironment, inhibiting fibrosis and vessel formation and reducing necrosis. Both peptides were active in preventing ascites formation. An increased activity was obtained in combination regimens, administering BLR100 or BLR200 with the chemotherapeutic drug gemcitabine. Pharmacokinetic analysis indicated that the improved activity of the combination was not mainly determined by the substantial increase in gemcitabine delivery to tumors, suggesting other effects on the tumor microenvironment. The beneficial remodeling of the tumor stroma supports the potential value of these CCN3-derived peptides for targeting pathways regulated by CCN2 in PDAC.

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7

Perbal, B. "CCN3-mutant mice are distinct from CCN3-null mice." Journal of Cell Communication and Signaling 1, no. 3-4 (December 2007): 229–30. http://dx.doi.org/10.1007/s12079-008-0020-8.

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8

McCallum, Lynn M. R., Wanhua Lu, Susan Price, Nathalie Planque, Bernard Perbal, Andrew Pierce, Anthony Whetton, and Alexandra E. Irvine. "BCR-ABL Decreases the Expression of CCN3 Leading to Increased Clonogenic Potential and Cell Growth." Blood 106, no. 11 (November 16, 2005): 1216. http://dx.doi.org/10.1182/blood.v106.11.1216.1216.

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Abstract Chronic Myeloid Leukemia (CML) is characterized by expression of the constitutively active BCR-ABL tyrosine kinase. Previously, we have identified downregulation of the negative growth regulator, CCN3, as a result of BCR-ABL kinase activity and detected reduced CCN3 expression in human CML cell lines and primary human CML cells. We now report a reciprocal relationship of BCR-ABL and CCN3 expression and the functional consequence of expressing CCN3 in BCR-ABL+ cells. Real-time PCR was used to examine the relationship between BCR-ABL and CCN3 expression in human K562 cells. Parental K562 cells showed high expression of BCR-ABL (4.68 x104 transcripts in 5 μL of cDNA) whilst CCN3 expression was not detected. Treatment with siRNA directed against BCR-ABL (0.5 μg per106 cells) for 72 hours resulted in a 3.7 fold decrease in BCR-ABL and 6.1 fold increase in CCN3 expression (mean Ct change 1.9 ± 0.2 and 2.6 ± 0.5 for BCR-ABL and CCN3 respectively, n=3, p=0.001). Similarly, K562 cells treated with imatinib (1 micromolar) for 96 hours showed a 5.9 fold decrease in BCR-ABL expression and a 4.2 fold increase in CCN3 expression (mean Ct change 2.5 ± 0.1 and 2.1± 0.2 for BCR-ABL and CCN3 respectively, n=3, p=0.001). To investigate CCN3 function, we expressed CCN3 in BCR-ABL+ cells using Nucleofector technology (Amaxa, GmbH). K562 cells were transfected with either the pCb6+ vector (Invitrogen,UK) or pCb6+ vector containing the CCN3 construct. Cells were analysed 24 hours post-transfection by flow cytometry and also after 7 days in methyl cellulose culture to determine clonogenicity. Cell cycle analysis was performed on 20,000 events using the winMDI software. CCN3 expression in BCR-ABL+ cells resulted in an accumulation of cells in the subG0 phase of the cell cycle (mean for subG0 9.9% ± 4.6 and 21.8% ± 0.7 for the pCb6+ vector alone and pCb6+ vector containing CCN3 construct respectively). CCN3 expression significantly increased the number of cells within the subG0 area of the cell cycle (n=3, p=0.027). In addition, CCN3 expression reduced the clonogenic capacity of BCR-ABL+ cells. K562 cells transfected with the pCb6+ vector containing CCN3 construct formed significantly fewer colonies on methyl cellulose in comparison to cells that had been transfected with the pCb6+ vector alone (n=3, p=0.027). This study demonstrates a reciprocal relationship between CCN3 and BCR-ABL expression. CCN3 is known to be a negative growth regulator and increased expression of CCN3 in BCR-ABL+ cells inhibits proliferation and decreases clonogenic potential. Thus CCN3 down-regulation mediated by BCR-ABL offers growth advantage to hematopoietic cells.

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9

Ouellet, VéRonique, Matthew Dankner, Laudine Desreumaux-Communal, Estelle Schmitt, Dru Perkins, Matthew G. Annis, Veronique Barres, et al. "CCN3/NOV as a functional driver and prognostic biomarker of prostate cancer bone metastasis." Journal of Clinical Oncology 37, no. 7_suppl (March 1, 2019): 182. http://dx.doi.org/10.1200/jco.2019.37.7_suppl.182.

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182 Background: Prostate cancer commonly metastasizes to the bone, resulting in pathological fractures and poor prognosis. CCN3/NOV (Nephroblastoma overexpressed) has been implicated in promoting the formation of osteolytic prostate cancer (PC) bone metastases. The C-terminal domain of CCN3 binds growth factors, heparin sulfate proteoglycans, activates Notch signaling and promotes dimerization of CCN family members. We hypothesize that the CCN3 CT domain is required to promote osteolytic PC bone metastasis and that CCN3 represents a prognostic biomarker in primary PC tumors to predict recurrence to bone. Methods: CCN3WT and CCN3∆CT were overexpressed in LNCaP C4-2 cells. The role of CCN3 was assessed with in vitro proliferation, migration and invasion assays, and in vivo through intracardiac injection in male Nude mice (Nu/Nu). Ex vivo µCT scans were performed on bone specimens. CCN3 expression was assessed in two unique tissue microarrays (TMA) comprising over 1,500 primary prostate tumor using different anti-CCN3 antibodies with immunohistochemistry and immunohistofluorescnece, respectively. Results: While CCN3WT and CCN3∆CT had little effect in vitro on cell proliferation, migration or invasion, intracardiac injection of CCN3WT resulted in increased incidence of bone metastasis compared to empty vector control and CCN3∆CT. Ex vivo µCT revealed decreased bone mineral density in bones from mice injected with CCN3WT cells compared to control and CCN3∆CT expressing cells. In both TMAs studied, high CCN3 expression in tumor epithelium correlated with increased risk of biochemical relapse and bone metastasis at 5 years and 15 years post-resection, respectively. Conclusions: CCN3 requires its C-terminal domain for its bone metastatic function, and CCN3 is correlated with aggressive disease biology in prostate cancer. These findings point to CCN3 as a biomarker that can be useful to predict prostate cancer aggressiveness, while providing clarity on its role as a functional mediator of prostate cancer bone metastasis.

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10

Riser, Bruce L., Feridoon Najmabadi, Bernard Perbal, Jo Ann Rambow, Melisa L. Riser, Ernest Sukowski, Herman Yeger, Sarah C. Riser, and Darryl R. Peterson. "CCN3/CCN2 regulation and the fibrosis of diabetic renal disease." Journal of Cell Communication and Signaling 4, no. 1 (February 9, 2010): 39–50. http://dx.doi.org/10.1007/s12079-010-0085-z.

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11

Kuwahara, Miho, Koichi Kadoya, Sei Kondo, Shanqi Fu, Yoshiko Miyake, Ayako Ogo, Mitsuaki Ono, et al. "CCN3 (NOV) Drives Degradative Changes in Aging Articular Cartilage." International Journal of Molecular Sciences 21, no. 20 (October 13, 2020): 7556. http://dx.doi.org/10.3390/ijms21207556.

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Aging is a major risk factor of osteoarthritis, which is characterized by the degeneration of articular cartilage. CCN3, a member of the CCN family, is expressed in cartilage and has various physiological functions during chondrocyte development, differentiation, and regeneration. Here, we examine the role of CCN3 in cartilage maintenance. During aging, the expression of Ccn3 mRNA in mouse primary chondrocytes from knee cartilage increased and showed a positive correlation with p21 and p53 mRNA. Increased accumulation of CCN3 protein was confirmed. To analyze the effects of CCN3 in vitro, either primary cultured human articular chondrocytes or rat chondrosarcoma cell line (RCS) were used. Artificial senescence induced by H2O2 caused a dose-dependent increase in Ccn3 gene and CCN3 protein expression, along with enhanced expression of p21 and p53 mRNA and proteins, as well as SA-β gal activity. Overexpression of CCN3 also enhanced p21 promoter activity via p53. Accordingly, the addition of recombinant CCN3 protein to the culture increased the expression of p21 and p53 mRNAs. We have produced cartilage-specific CCN3-overexpressing transgenic mice, and found degradative changes in knee joints within two months. Inflammatory gene expression was found even in the rib chondrocytes of three-month-old transgenic mice. Similar results were observed in human knee articular chondrocytes from patients at both mRNA and protein levels. These results indicate that CCN3 is a new senescence marker of chondrocytes, and the overexpression of CCN3 in cartilage may in part promote chondrocyte senescence, leading to the degeneration of articular cartilage through the induction of p53 and p21.

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12

McCallum, Lynn, Susan Price, Nathalie Planque, Bernard Perbal, Andrew Pierce, Anthony D. Whetton, and Alexandra E. Irvine. "A novel mechanism for BCR-ABL action: stimulated secretion of CCN3 is involved in growth and differentiation regulation." Blood 108, no. 5 (September 1, 2006): 1716–23. http://dx.doi.org/10.1182/blood-2006-04-016113.

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Chronic myeloid leukemia (CML) is characterized by the presence of the constitutively active BCR-ABL protein tyrosine kinase. Using a multipotent hemopoietic cell line, FDCP-Mix, expressing BCR-ABL tyrosine kinase, we investigated the initial effects of this kinase in primitive hematopoietic stem cells. We identified down-regulation of a novel gene, CCN3, as a direct consequence of BCR-ABL kinase activity. CCN3 has been reported to function as a tumor suppressor gene in solid tumors. Northern and Western blotting plus immunocytochemical analysis confirmed CCN3 expression is decreased and is tyrosine-phosphorylated in BCR-ABL kinase active FDCP-Mix cells. Decreased cellular CCN3 correlated with increased CCN3 secretion in BCR-ABL kinase active cells. In vitro treatment of human CML cell lines with imatinib or siRNA directed against BCR-ABL significantly reduced BCR-ABL while increasing CCN3 expression. Cells from patients responding to imatinib showed a similar decrease in BCR-ABL and increase in CCN3. CML CD34+ cells treated with imatinib in vitro demonstrated increased CCN3 protein. Transfecting CCN3 into BCR-ABL+ cells inhibited proliferation and decreased clonogenic potential. CCN3 plays an important role in internal and external cell-signaling pathways. Thus, BCR-ABL can regulate protein levels by governing secretion, a novel mechanism for this tyrosine kinase.

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13

Chen, Po-Chun, Ju-Fang Liu, Yi-Chin Fong, Yuan-Lin Huang, Chia-Chia Chao, and Chih-Hsin Tang. "CCN3 Facilitates Runx2 and Osterix Expression by Inhibiting miR-608 through PI3K/Akt Signaling in Osteoblasts." International Journal of Molecular Sciences 20, no. 13 (July 5, 2019): 3300. http://dx.doi.org/10.3390/ijms20133300.

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CCN3, otherwise known as the nephroblastoma overexpressed (NOV) protein, is a cysteine-rich protein that belongs to the CCN family and regulates several cellular functions. Osteoblasts are major bone-forming cells that undergo proliferation, mineralization, renewal, and repair during the bone formation process. We have previously reported that CCN3 increases bone morphogenetic protein 4 (BMP-4) production and bone mineralization in osteoblasts, although the role of CCN3 remains unclear with regard to osteogenic transcription factors (runt-related transcription factor 2 (Runx2) and osterix). Here, we used alizarin red-S and alkaline phosphatase staining to show that CCN3 enhances osteoblast differentiation. Stimulation of osteoblasts with CCN3 increases expression of osteogenic factors such as BMPs, Runx2, and osterix. Moreover, we found that the inhibition of miR-608 expression is involved in the effects of CCN3 and that incubation of osteoblasts with CCN3 promotes focal adhesion kinase (FAK) and Akt phosphorylation. Our results indicate that CCN3 promotes the expression of Runx2 and osterix in osteoblasts by inhibiting miR-608 expression via the FAK and Akt signaling pathways.

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14

de la Vega Gallardo, Nira, Rosana Penalva, Marie Dittmer, Michelle Naughton, John Falconer, Jill Moffat, Alerie G. de la Fuente, et al. "Dynamic CCN3 expression in the murine CNS does not confer essential roles in myelination or remyelination." Proceedings of the National Academy of Sciences 117, no. 30 (July 10, 2020): 18018–28. http://dx.doi.org/10.1073/pnas.1922089117.

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CCN3 is a matricellular protein that promotes oligodendrocyte progenitor cell differentiation and myelination in vitro and ex vivo. CCN3 is therefore a candidate of interest in central nervous system (CNS) myelination and remyelination, and we sought to investigate the expression and role of CCN3 during these processes. We found CCN3 to be expressed predominantly by neurons in distinct areas of the CNS, primarily the cerebral cortex, hippocampus, amygdala, suprachiasmatic nuclei, anterior olfactory nuclei, and spinal cord gray matter. CCN3 was transiently up-regulated following demyelination in the brain of cuprizone-fed mice and spinal cord lesions of mice injected with lysolecithin. However, CCN3−/−mice did not exhibit significantly different numbers of oligodendroglia or differentiated oligodendrocytes in the healthy or remyelinating CNS, compared to WT controls. These results suggest that despite robust and dynamic expression in the CNS, CCN3 is not required for efficient myelination or remyelination in the murine CNS in vivo.

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15

Wei, Yingying, Linan Peng, Yi Li, Na Zhang, Ke Shang, Lihua Duan, Jixin Zhong, and Jie Chen. "Higher Serum CCN3 Is Associated with Disease Activity and Inflammatory Markers in Rheumatoid Arthritis." Journal of Immunology Research 2020 (May 9, 2020): 1–7. http://dx.doi.org/10.1155/2020/3891425.

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Nephroblastoma overexpressed protein (NOV/CCN3), the early discovered member of the CCN family, has recently been suggested to be involved in a number of inflammatory processes, including wound healing, alveolar epithelial cell inflammation, cancer metastasis, and macrophage foam cell formation. However, the role of CCN3 in rheumatoid arthritis (RA), a classic autoimmune and inflammatory disease, remains elusive. RA is a chronic systemic autoimmune disease that eventually leads to cartilage and bone destruction and joint dysfunction. In this study, we investigated the potential of serum CCN3 as a biomarker for RA. The serum levels of CCN3 were measured by ELISA. The clinical and laboratory parameters were collected from a clinical record system, and disease activity was determined by joint disease activity score 28 (DAS28). Our results showed that the serum levels of CCN3 were significantly increased in RA patients compared to healthy controls. Furthermore, the CCN3 level was positively correlated with DAS28 (CRP), DAS28 (ESR), and the level of anti-CCP Ab, an autoantibody highly specific for RA. Furthermore, CCN3 showed a positive correlation with inflammatory cytokine IL-6, while no significant correlation with TNF-α was observed. These data suggest that CCN3 plays an important role in the development of RA and might be a potential disease activity biomarker for RA.

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16

Leask, Andrew. "Yin and Yang: CCN3 inhibits the pro-fibrotic effects of CCN2." Journal of Cell Communication and Signaling 3, no. 2 (May 29, 2009): 161–62. http://dx.doi.org/10.1007/s12079-009-0056-4.

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17

Lu, Wanhua, Lynn McCallum, Bernard Perbal, Nourreddine Lazar, and Alexandra Irvine. "CCN3, a Novel Growth Inhibitory Factor for Chronic Myeloid Leukemia." Blood 112, no. 11 (November 16, 2008): 4230. http://dx.doi.org/10.1182/blood.v112.11.4230.4230.

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Abstract Chronic Myeloid Leukaemia (CML) is characterized by expression of the constitutively active BCR-ABL tyrosine kinase. Previously, we identified down-regulation of the negative growth regulator, CCN3, as a result of BCR-ABL kinase activity. Reduced CCN3 expression is a prominent feature in both primary human CML cells and cell lines. We now show that CCN3 is growth inhibitory and enhances imatinib induced growth inhibition. To evaluate the biological consequence of CCN3 expression in CML, K562 cells were stably transfected with a construct containing CCN3 (pCMV82-23) and growth characteristics and activation of signaling pathways were compared to cells transfected with empty vector (control). CCN3 expression was undetected by Real-time PCR in control cells whilst pCMV82-23 cells expressed 2.25 × 106 copies per 50ng of cDNA. pCMV82-23 cells showed reduced colony formation capacity (p=0.003) and reduced cell growth over a period of five days (p=0.005). Investigation of cellular signaling showed CCN3 expression resulted in significant down-regulation of three major signaling pathways and demonstrated reduced phosphorylation of ERK (p=0.002), pAKT (p=0.017) and pSTAT5 (p=0.005) compared to control cells. Protein levels for total ERK, AKT and STAT5 were unaffected by CCN3 expression. Flow cytometry showed that sustained CCN3 expression resulted in an accumulation of cells within the subG0 stage of the cell cycle (11.4% ± 3 (p=0.040)). To determine if CCN3 expression could influence sensitivity to the BCR-ABL kinase inhibitor, imatinib, pCMV82-23 cells and control cells were treated with imatinib (5uM) for 48h. Control cells treated with imatinib showed moderate growth inihibition (19.6% ± 2.5) compared to untreated control. pCMV82-23 cells showed a significant increase in the magnitude of imatinib induced growth inhibition (63.3% ± 10.5 (p=0.043)). This was associated with an increased accumulation of cells in the subG0 area of the cell cycle, 34.6% ± 5 for pCMV82-23 cells compared to control cells (21.7% ± 8) in response to imatinib treatment (p=0.006). To then determine if these effects could be reproduced using recombinant CCN3 (rCCN3), K562 cells were treated with imatinib (5uM) alone or in combination with rCCN3 (10nM) for 48h. K562 cells treated with the combination of rCCN3 and imatinib showed enhanced growth inhibition (71.8% ± 7.9) compared to cells treated with imatinib alone (81.1% ± 9.2 (p=0.008)). Loss of CCN3 is consistent with properties associated with the CML phenotype. Sustained expression of CCN3 in K562 cells restores growth control and re-establishes induction of apoptosis. Both increased expression of CCN3 or addition of the recombinant protein provide additional benefit for imatinib induced growth inhibition thus providing a novel avenue for therapeutic intervention.

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18

Fukunaga-Kalabis, Mizuho, Gabriela Martinez, Zhao-Jun Liu, Jiri Kalabis, Paul Mrass, Wolfgang Weninger, Sue M. Firth, Nathalie Planque, Bernard Perbal, and Meenhard Herlyn. "CCN3 controls 3D spatial localization of melanocytes in the human skin through DDR1." Journal of Cell Biology 175, no. 4 (November 13, 2006): 563–69. http://dx.doi.org/10.1083/jcb.200602132.

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Melanocytes reside within the basal layer of the human epidermis, where they attach to the basement membrane and replicate at a rate proportionate to that of keratinocytes, maintaining a lifelong stable ratio. In this study, we report that coculturing melanocytes with keratinocytes up-regulated CCN3, a matricellular protein that we subsequently found to be critical for the spatial localization of melanocytes to the basement membrane. CCN3 knockdown cells were dissociated either upward to the suprabasal layers of the epidermis or downward into the dermis. The overexpression of CCN3 increased adhesion to collagen type IV, the major component of the basement membrane. As the receptor responsible for CCN3-mediated melanocyte localization, we identified discoidin domain receptor 1 (DDR1), a receptor tyrosine kinase that acts as a collagen IV adhesion receptor. DDR1 knockdown decreased melanocyte adhesion to collagen IV and shifted melanocyte localization in a manner similar to CCN3 knockdown. These results demonstrate an intricate and necessary communication between keratinocytes and melanocytes in maintaining normal epidermal homeostasis.

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19

Wang, Hefei, Binbin Huang, Anli Hou, Li Xue, Baobei Wang, Jie Chen, Mengxia Li, and Jian V. Zhang. "High NOV/CCN3 expression during high-fat diet pregnancy in mice affects GLUT3 expression and the mTOR pathway." American Journal of Physiology-Endocrinology and Metabolism 320, no. 4 (April 1, 2021): E786—E796. http://dx.doi.org/10.1152/ajpendo.00230.2020.

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20

Katsube, Ken-ichi, Saki Ichikawa, Yuko Katsuki, Tasuku Kihara, Masanori Terai, Lester F. Lau, Yoshihiro Tamamura, et al. "CCN3 and bone marrow cells." Journal of Cell Communication and Signaling 3, no. 2 (June 2009): 135–45. http://dx.doi.org/10.1007/s12079-009-0059-1.

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21

Fernando, H., A. Chhabra, S. Davies, G. Watkins, H. Kynaston, R. E. Mansel, and W. G. Jiang. "Expression of the WAVE (WASP Verprolin-homologous) molecules in human breast cancer." Journal of Clinical Oncology 25, no. 18_suppl (June 20, 2007): 21061. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.21061.

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21061 Background: WAVEs (WASP Verprolin-homologous) belongs to the CCN family which comprises of nine members, the cysteine-rich 61 (Cyr61/CCN1), connective tissue growth factor (CTGF/CCN2) and nephroblastoma over-expressed (Nov/CCN3), Wnt-induced secreted proteins(WISPs)1, 2 and 3 (CCN4–6) as well as the WAVE-1,2 and 3 (also known as CCN7–9 respectively). Some members of the CCN family, such as Cyr61 and CTGF are known to stimulate mitosis, adhesion, apoptosis, extracellular matrix production, cell migration and growth arrest in cancer cells including breast cancer cells. However, there is no knowledge of the expression pattern and the function of WAVEs in human breast cancer. Here, we report the expression of WAVE-1,-2 and -3 transcripts and proteins in relation to clinical and pathological characteristics in human breast cancer. Methods: The expression of the three WAVE molecules at the mRNA and protein levels in a cohort of 122 human breast cancers and 32 normal breast tissues were analysed and correlated with the patients’ clinical outcome. The respective transcripts were quantitative determined using real time RT-PCR and distribution of the proteins were investigated by immunohistochemical methods. Results: All three WAVE proteins were detected in mammary epithelial cells and are of cytoplasmic nature. Breast cancer cells from the tissues also displayed positive staining of the WAVE proteins, with WAVE-2 staining appears weaker compared with normal epithelial cells. WAVE-1 transcripts were expressed in significantly high levels (p=0.03) in high grade breast cancers. Low levels of WAVE-2 were associated with higher TNM staging (p=0.038 in TNM3 and p=0.017 in TNM4) and were also found in patients with poor prognosis. Interesting, a marginal reduction of WAVE-3 transcripts was seen in patients who developed systemic metastasis. No other significant associations were found between the WAVE1 and WAVE3 transcripts and the breast cancer cells. Conclusions: WAVEs are widely expressed in human mammary tissues and have a differential expression in human breast cancer with WAVE2 appearing to be associated with the aggressiveness of breast tumors. No significant financial relationships to disclose.

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Zhu, Bing-Mei, Mark Wickre, Risu Na, Peter Klover, Cyril Martin, Akiko Kimura, and Lothar Hennighausen. "Stat5 Is Essential for BCR-ABL-Transformed Chronic Myeloid Leukemia (CML) Associated with Increased CCN3 Gene Expression." Blood 114, no. 22 (November 20, 2009): 3271. http://dx.doi.org/10.1182/blood.v114.22.3271.3271.

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Abstract Abstract 3271 Poster Board III-1 Introduction: Signal transducers and activators of transcription5 (Stat5) proteins are involved in many cellular processes through mediated cytokine, hormone, and growth factor signaling. But its role in disease pathogenesis has not been fully elucidated. Recently, activation of BCR-ABL has been reported to regulate a novel gene, CCN3 in cell lines and primary cells derived from chronic myeloid leukemia (CML) patients. To investigate the function of Stat5 in CML initiation and maintenance and determine the downstream target genes on Jak-Stat5 pathway, we developed a BCR-ABL - induced CML - like disease model by using retro-viral infection in Cre-mediated Stat5 knockout transgenic mice and analyzed the progress of CML. We also used Stat5 knockout (Stat5 KO) mice to perform gene profiling. Results: Our study showed that loss of Stat5 resulted in increased survival rate and remission of CML. Microarray analysis showed that CCN3 expression was down-regulated in KL cells derived from Stat5 KO mice. BCR-ABL-activated Stat5 increased expression level of CCN3 in CML cells. We further determined that Stat5 binds to CCN3 promoter region in IL-3 stimulated 32D cells and BCR-ABL-induced CML cells. Conclusions: Our study suggested that Stat5 is essential for BCR-ABL transformed CML and that CCN3 is involved in normal hematopoiesis and CML development. Further study will be necessary to uncover the function of CCN3 and more targets of Stat5 pathway in CML development and discover the therapeutic significance. Disclosures: No relevant conflicts of interest to declare.

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Yan, Xiaolang, Robert C. Baxter, Bernard Perbal, and Sue M. Firth. "The Aminoterminal Insulin-Like Growth Factor (IGF) Binding Domain of IGF Binding Protein-3 Cannot Be Functionally Substituted by the Structurally Homologous Domain of CCN3." Endocrinology 147, no. 11 (November 1, 2006): 5268–74. http://dx.doi.org/10.1210/en.2005-1568.

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IGF binding proteins (IGFBPs) are a family of structurally homologous proteins that bind IGFs with high affinities and can modulate IGF activity. The IGF binding site has been shown to comprise residues in both the aminoterminal and carboxyterminal domains. In recent years several proteins including members of the CCN (connective tissue growth factor, Cyr61, and nephroblastoma overexpressed) family were recognized as having structural homology in their aminoterminal domains to the IGFBPs. Despite their low or undetectable IGF binding ability, a proposal was made to rename them as IGFBP-related proteins. To test whether the aminoterminal domain of a CCN protein can fulfill the high-affinity IGF binding function of an IGFBP, we created a chimera in which the aminoterminal domain of IGFBP-3 was substituted with the aminoterminal domain of CCN3 (previously known as Nov). The CCN3-IGFBP-3 chimera bound IGFs and inhibited IGF activity very weakly, similar to CCN3 itself. Although structurally similar, the aminoterminal domain of CCN3 is unable to replace the aminoterminal domain of IGFBP-3 in forming a high-affinity IGF-binding site. These results argue against a direct role of CCN3 in the regulation of IGF bioavailability and indicate that the nomenclature of IGFBP-related proteins (which implies functional relationship to the classical IGFBPs) is inappropriate for CCN proteins.

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24

Smina, T. P., M. Rabeka, and Vijay Viswanathan. "Diabetic Foot Ulcer as a Cause of Significant Decline in the Renal Function Among South Indian Population With Type 2 Diabetes: Role of TGF-β1 and CCN Family Proteins." International Journal of Lower Extremity Wounds 18, no. 4 (July 15, 2019): 354–61. http://dx.doi.org/10.1177/1534734619862704.

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In the present study, a total of 428 South Indian subjects were divided into four different groups, consisting of individuals with type 2 diabetes without any other complications (T2DM), T2DM subjects with stage 2 and 3 diabetic kidney disease (CKD), T2DM subjects with grade 2 or 3 diabetic foot ulcer (DFU) and T2DM subjects having both diabetic kidney disease and diabetic foot ulcer (CKDDFU). The study was conducted ambispectively by comparing the changes in renal function among two consecutive periods, i.e., the period prior to the development of grade 2 and 3 diabetic foot ulcer (retrospectively) and after the development of DFU (prospectively). A gradual and uniform reduction of eGFR was observed throughout the study period in the subjects affected with either CKD or DFU alone. Whereas in subjects with both CKD and DFU, there was a sharp decline in the eGFR during the six months prior to the baseline, i.e., the period in which the development of ulcer and its progression to grade 2 or 3 happened. Remarkable elevations in the levels of TGF-β1 and CCN2 (CTGF), as well as a significant reduction in the level of CCN3 (NOV), were observed in the serum of CKDDFU group subjects, compared to the other groups. Increased production of TGF-β1 in response to the inflammatory stimulus from multiple sites in CKDDFU subjects caused a subsequent down-regulation of CCN3, followed by the activation of a large quantity of CCN2.

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Hoshijima, Mitsuhiro, Takako Hattori, Eriko Aoyama, Takashi Nishida, Takashi Yamashiro, and Masaharu Takigawa. "Roles of heterotypic CCN2/CTGF-CCN3/NOV and homotypic CCN2-CCN2 interactions in expression of the differentiated phenotype of chondrocytes." FEBS Journal 279, no. 19 (August 28, 2012): 3584–97. http://dx.doi.org/10.1111/j.1742-4658.2012.08717.x.

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Pasmant, Eric, Nicolas Ortonne, Laure Rittiè, Ingrid Laurendeau, Pascale Lèvy, Vladimir Lazar, Bèatrice Parfait, et al. "Differential Expression ofCCN1/CYR61,CCN3/NOV,CCN4/WISP1, andCCN5/WISP2in Neurofibromatosis Type 1 Tumorigenesis." Journal of Neuropathology & Experimental Neurology 69, no. 1 (January 2010): 60–69. http://dx.doi.org/10.1097/nen.0b013e3181c79bff.

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27

Perbal, Bernard, Monia Zuntini, Diana Zambelli, Massimo Serra, Marika Sciandra, Lara Cantiani, Enrico Lucarelli, Piero Picci, and Katia Scotlandi. "Prognostic Value of CCN3 in Osteosarcoma." Clinical Cancer Research 14, no. 3 (February 1, 2008): 701–9. http://dx.doi.org/10.1158/1078-0432.ccr-07-0806.

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28

Leask, Andrew. "CCN3: A novel function in vivo." Journal of Cell Communication and Signaling 1, no. 3-4 (December 2007): 227–28. http://dx.doi.org/10.1007/s12079-008-0019-1.

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29

Perbal, Bernard. "CCN3: Doctor Jekyll and Mister Hyde." Journal of Cell Communication and Signaling 2, no. 1-2 (June 2008): 3–7. http://dx.doi.org/10.1007/s12079-008-0028-0.

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30

Perbal, Bernard. "CCN3: the-pain-killer inside me." Journal of Cell Communication and Signaling 6, no. 2 (March 30, 2012): 117–20. http://dx.doi.org/10.1007/s12079-012-0163-5.

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31

Leask, Andrew. "CCN3: stopping that achy, breaky aorta." Journal of Cell Communication and Signaling 11, no. 1 (November 12, 2016): 93–94. http://dx.doi.org/10.1007/s12079-016-0363-5.

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32

Subramaniam, Manish Mani, Noureddine Lazar, Samuel Navarro, Bernard Perbal, and Antonio Llombart-Bosch. "Expression of CCN3 protein in human Wilms’ tumors: immunohistochemical detection of CCN3 variants using domain-specific antibodies." Virchows Archiv 452, no. 1 (December 8, 2007): 33–39. http://dx.doi.org/10.1007/s00428-007-0523-3.

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33

Leask, Andrew. "Slow train coming: an anti-CCN2 strategy reverses a model of chronic overuse muscle fibrosis." Journal of Cell Communication and Signaling 14, no. 3 (May 14, 2020): 349–50. http://dx.doi.org/10.1007/s12079-020-00568-1.

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Abstract One of the first targets proposed as an anti-fibrotic therapy was CCN2. Proof of its involvement in fibrosis was initially difficult, due to the lack of appropriate reagents and general understanding of the molecular mechanisms responsible for persistent fibrosis. As these issues have been progressively resolved over the last twenty-five years, it has become clear that CCN2 is a bone fide target for anti-fibrotic intervention. An anti-CCN2 antibody (FG-3019) is in Phase III clinical trials for idiopathic pulmonary fibrosis and pancreatic cancer, and in Phase II for Duschenne’s muscular dystrophy. An exciting paper recently published by Mary Barbe and the Popoff group has shown that FG-3019 reduces established muscle fibrosis (Barbe et al., FASEB J 34:6554–6569, 2020). Intriguingly, FG-3019 blocked the decreased expression of the anti-fibrotic protein CCN3, caused by the injury model. These important data support the notion that targeting CCN2 in the fibrotic microenvironment may reverse established fibrosis, making it the first agent currently in development to do so.

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34

Emre, Yalin, and Beat A. Imhof. "Aortic aneurysm, CCN3 may solve the problem." Journal of Thoracic Disease 8, no. 9 (September 2016): E1025—E1027. http://dx.doi.org/10.21037/jtd.2016.08.15.

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35

Faria, AdrianeReichert, JulianaElizabeth Jung, CaioCesar Silva de Catro, and Lucia de Noronha. "Reduced immunohistochemical expression of CCN3 in vitiligo." Indian Journal of Dermatology, Venereology and Leprology 84, no. 5 (2018): 558. http://dx.doi.org/10.4103/ijdvl.ijdvl_954_16.

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36

Zhang, Chao, Dustin van der Voort, Hong Shi, Rongli Zhang, Yulan Qing, Shuichi Hiraoka, Minoru Takemoto, et al. "Matricellular protein CCN3 mitigates abdominal aortic aneurysm." Journal of Clinical Investigation 126, no. 4 (March 14, 2016): 1282–99. http://dx.doi.org/10.1172/jci82337.

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Zhang, Chao, Dustin van der Voort, Hong Shi, Rongli Zhang, Yulan Qing, Shuichi Hiraoka, Minoru Takemoto, et al. "Matricellular protein CCN3 mitigates abdominal aortic aneurysm." Journal of Clinical Investigation 126, no. 5 (May 2, 2016): 2012. http://dx.doi.org/10.1172/jci87977.

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38

Leask, Andrew. "It’s a knockout: CCN3 suppresses neointimal thickening." Journal of Cell Communication and Signaling 4, no. 2 (February 24, 2010): 109–10. http://dx.doi.org/10.1007/s12079-010-0086-y.

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39

Perbal, Bernard, Noureddine Lazar, Diana Zambelli, Jose Antonio Lopez-Guerrero, Antonio Llombart-Bosch, Katia Scotlandi, and Piero Picci. "Prognostic relevance of CCN3 in Ewing sarcoma." Human Pathology 40, no. 10 (October 2009): 1479–86. http://dx.doi.org/10.1016/j.humpath.2009.05.008.

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40

Kipkeew, Friederike, Manuela Kirsch, Diana Klein, Manuela Wuelling, Elke Winterhager, and Alexandra Gellhaus. "CCN1 (CYR61) and CCN3 (NOV) signaling drives human trophoblast cells into senescence and stimulates migration properties." Cell Adhesion & Migration 10, no. 1-2 (February 12, 2016): 163–78. http://dx.doi.org/10.1080/19336918.2016.1139265.

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41

McCallum, L., and A. E. Irvine. "CCN3 – A key regulator of the hematopoietic compartment." Blood Reviews 23, no. 2 (March 2009): 79–85. http://dx.doi.org/10.1016/j.blre.2008.07.002.

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42

Sin, Wun-Chey, Mimi Tse, Nathalie Planque, Bernard Perbal, Paul D. Lampe, and Christian C. Naus. "Matricellular Protein CCN3 (NOV) Regulates Actin Cytoskeleton Reorganization." Journal of Biological Chemistry 284, no. 43 (August 25, 2009): 29935–44. http://dx.doi.org/10.1074/jbc.m109.042630.

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43

Borkham-Kamphorst, E., J. Herrmann, W. Bohr, E. van de Leur, and R. Weiskirchen. "920 ANTIFIBROTIC PROPERTIES OF NOV/CCN3 IN LIVER." Journal of Hepatology 52 (April 2010): S357. http://dx.doi.org/10.1016/s0168-8278(10)60921-x.

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44

Calhabeu, Frederico, Jérome Lafont, Gwenvael Le Dreau, Maryvonne Laurent, Chantal Kazazian, Laurent Schaeffer, Cécile Martinerie, and Catherine Dubois. "NOV/CCN3 impairs muscle cell commitment and differentiation." Experimental Cell Research 312, no. 10 (June 2006): 1876–89. http://dx.doi.org/10.1016/j.yexcr.2006.02.027.

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45

Shi, Hong, Chao Zhang, Vinay Pasupuleti, Xingjian Hu, Domenick A. Prosdocimo, Wenconghui Wu, Yulan Qing, et al. "CCN3 Regulates Macrophage Foam Cell Formation and Atherosclerosis." American Journal of Pathology 187, no. 6 (June 2017): 1230–37. http://dx.doi.org/10.1016/j.ajpath.2017.01.020.

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46

Li, C. L. "A role for CCN3 (NOV) in calcium signalling." Molecular Pathology 55, no. 4 (August 1, 2002): 250–61. http://dx.doi.org/10.1136/mp.55.4.250.

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Perbal, Bernard. "Erratum to: CCN3: the-pain-killer inside me." Journal of Cell Communication and Signaling 6, no. 3 (July 12, 2012): 185. http://dx.doi.org/10.1007/s12079-012-0167-1.

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48

Kim, Yujin, Hayoung Yang, Jeong-Ki Min, Young-Jun Park, Seung Hun Jeong, Sung-Wuk Jang, and Sungbo Shim. "CCN3 secretion is regulated by palmitoylation via ZDHHC22." Biochemical and Biophysical Research Communications 495, no. 4 (January 2018): 2573–78. http://dx.doi.org/10.1016/j.bbrc.2017.12.128.

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49

Holbourn, Kenneth P., Marc Malfois, and K. Ravi Acharya. "First Structural Glimpse of CCN3 and CCN5 Multifunctional Signaling Regulators Elucidated by Small Angle X-ray Scattering." Journal of Biological Chemistry 286, no. 25 (May 4, 2011): 22243–49. http://dx.doi.org/10.1074/jbc.m111.225755.

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50

Cario-André, Muriel, Pauline Henrot, Catherine Pain, Julien Seneschal, and Alain Taieb. "Étude de l’expression des protéines CCN2 (CTGF) et CCN3 (NOV) chez les patients atteints de sclérodermie systémique." Annales de Dermatologie et de Vénéréologie 143, no. 12 (December 2016): S431. http://dx.doi.org/10.1016/j.annder.2016.09.078.

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