Hematopoietic growth factor inducible neurokinin-1 type: a transmembrane protein that is similar to neurokinin 1 interacts with substance P

Bandari, Persis; Qian, Jing; Yehia, Ghassan; Joshi, Deval D.; Maloof, Paul; Potian, Julius A.; Oh, Hyun Sook; Gascón, Pedro; Harrison, Jonathan S.; Rameshwar, Pranela

doi:10.1016/s0167-0115(02)00288-4

Cited by 53 publications

(66 citation statements)

References 36 publications

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“…It is also referred to as osteoactivin, hematopoietic growth factor-inducible neurokinin 1, and the dendritic cell-associated heparin sulfate proteoglycan-dependent integrin ligand (18)(19)(20)(21). Gpnmb has been implicated in regulation of both adaptive and innate immunity (22)(23)(24).…”

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confidence: 99%

Lysosomal Stress in Obese Adipose Tissue Macrophages Contributes to MITF-Dependent Gpnmb Induction

et al. 2014

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In obesity, adipose tissue (AT) contains crown-like structures where macrophages surround nonviable adipocytes. To understand how AT macrophages (ATMs) contribute to development of insulin resistance, we examined their character in more detail. In silico analysis of F2 mouse populations revealed significant correlation between adipose glycoprotein nonmetastatic melanoma protein B (Gpnmb) expression and body weight. In obese mice and obese individuals, Gpnmb expression was induced in ATMs. Cultured RAW264.7 cells were used to obtain insight into the mechanism of Gpnmb regulation. Gpnmb was potently induced by lysosomal stress inducers, including palmitate and chloroquine, or Torin1, an inhibitor of mammalian target of rapamycin complex 1 (mTORC1). These stimuli also provoked microphthalmia transcription factor (MITF) translocation to the nucleus, and knockdown of MITF by short hairpin RNA indicated its absolute requirement for Gpnmb induction. In agreement with our in vitro data, reduced mTORC1 activity was observed in isolated ATMs from obese mice, which coincided with increased nuclear MITF localization and Gpnmb transcription. Aberrant nutrient sensing provokes lysosomal stress, resulting in attenuated mTORC1 activity and enhanced MITF-dependent Gpnmb induction. Our data identify Gpnmb as a novel marker for obesity-induced ATM infiltration and potentiator of interleukin-4 responses and point toward a crucial role for MITF in driving part of the ATM phenotype.

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confidence: 99%

Lysosomal Stress in Obese Adipose Tissue Macrophages Contributes to MITF-Dependent Gpnmb Induction

et al. 2014

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“…The initial identification of OA emerged from studies using an animal model of osteopetrosis, in which it is overexpressed (Safadi et al, 2001; Owen et al, 2003; Selim 2009). Other groups have identified the same protein in different species and have designated different names such as glycoprotein nmb in melanoma cell lines (Weterman et al, 1995; Okamoto et al, 2005; Kuan et al, 2006; Tse et al, 2006; Pollack et al, 2007) and melanocytes (Anderson et al, 2002, 2006), dendritic cell heparin sulfate proteoglycan integrin dependent ligand in dendritic and T-cells (Shikano et al, 2001; Chung et al, 2007), and human hematopoietic growth factor inducible neurokinin in tumor cells (Bandari et al, 2003). In osteoblasts, OA exists as a 65-kDa transmembrane protein and a 115-kDa secreted glycoprotein (Safadi et al, 2001).…”

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confidence: 99%

“…The osteoinductive effects of BMP-2 are dependent on OA (Abdelmagid et al, 2007). OA has the ability to regulate cell proliferation, adhesion, differentiation and synthesis of ECM proteins in various cell types (Adema et al, 1994; Jager et al, 2000; Anderson et al, 2001, 2002, 2006; Safadi et al, 2001; Bandari et al, 2003; Onaga et al, 2003; Ott et al, 2003; Safadi et al, 2003; Yasumoto et al, 2004; Boissy et al, 2005; Ogawa et al, 2005; Okamoto et al, 2005; Brunberg et al, 2006; Hoashi et al, 2006; Abe et al, 2007; Helip-Wooley et al, 2007; Nakamura et al, 2007; Ripoll et al, 2007). OA messenger ribonucleic acid (mRNA) and protein are expressed by human and rodent osteoblasts (Safadi et al, 2001; Owen et al, 2003).…”

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confidence: 99%

Comparison of bone morphogenetic protein‐2 and osteoactivin for mesenchymal cell differentiation: Effects of bolus and continuous administration

Arosarena¹,

Carpio-Cano²,

Cadena³

et al. 2011

Journal Cellular Physiology

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Current osteoinductive protein therapy utilizes bolus administration of large doses of bone morphogenetic proteins (BMPs), which is costly, and may not replicate normal bone healing. The limited in vivo biologic activity of BMPs requires the investigation of growth factors that may enhance this activity. In this study, we utilized the C3H10T1/2 murine mesenchymal stem cell line to test the hypotheses that osteoactivin (OA) has comparable osteoinductive effects to bone morphogenetic protein-2 (BMP-2), and that sustained administration of either growth factor would result in increased osteoblastic differentiation as compared to bolus administration. Sustained release biodegradable hydrogels were designed, and C3H10T1/2 cells were grown on hydrogels loaded with BMP-2 or OA. Controls were grown on unloaded hydrogels, and positive controls were exposed to bolus growth factor administration. Cells were harvested at several time points to assess osteoblastic differentiation. Alkaline phosphatase (ALP) staining and activity, and gene expression of ALP and osteocalcin were assessed. Treatment with OA or BMP-2 resulted in comparable effects on osteoblastic marker expression. However, cells grown on hydrogels demonstrated osteoblastic differentiation that was not as robust as cells treated with bolus administration. This study shows that OA has comparable effects to BMP-2 on osteoblastic differentiation using both bolus administration and continuous release, and that bolus administration of OA has a more profound effect than administration using hydrogels for sustained release. This study will lead to a better understanding of appropriate delivery methods of osteogenic growth factors like OA for repair of fractures and segmental bone defects.

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“…4 The Gpnmb gene has high homology to Pmel-17 and qnr-71 genes that are important in melanocyte differentiation and melanosome formation (21,22). The OA/Gpnmb protein is a type I trans-membrane glycoprotein of 562 amino acids that has been assigned several names in other species, such as DC-HIL (dendritic cell heparan sulfate proteoglycan integrin-dependent ligand) in mouse dendritic cells (23), GPNMB (glycoprotein nmb) in human melanoma cell lines and melanocytes (24), and HGFIN (hematopoietic growth factor-inducible neurokinin) in human tumor cells (25). The importance of OA/Gpnmb in osteogenesis emerged from several of our previous reports in which we tested the effects of OA/Gpnmb, using several approaches, on mesenchymal stem cells and osteoblast differentiation and function (26 -28).…”

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confidence: 99%

Mutation in Osteoactivin Promotes Receptor Activator of NFκB Ligand (RANKL)-mediated Osteoclast Differentiation and Survival but Inhibits Osteoclast Function

Abdelmagid

Sondag

Moussa

et al. 2015

Journal of Biological Chemistry

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Background:The importance of osteoactivin has emerged from its role in osteogenesis. Results: Loss-of-function mutation of osteoactivin stimulates osteoclast differentiation and survival, with a defect in bone resorption. Conclusion: Osteoactivin acts as a negative regulator of osteoclastogenesis and a positive regulator of osteoclast function. Significance: This study helps to identify the possible mechanisms and targets of osteoactivin during osteoclast differentiation with impact on bone remodeling.

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Hematopoietic growth factor inducible neurokinin-1 type: a transmembrane protein that is similar to neurokinin 1 interacts with substance P

Cited by 53 publications

References 36 publications

Lysosomal Stress in Obese Adipose Tissue Macrophages Contributes to MITF-Dependent Gpnmb Induction

Lysosomal Stress in Obese Adipose Tissue Macrophages Contributes to MITF-Dependent Gpnmb Induction

Comparison of bone morphogenetic protein‐2 and osteoactivin for mesenchymal cell differentiation: Effects of bolus and continuous administration

Mutation in Osteoactivin Promotes Receptor Activator of NFκB Ligand (RANKL)-mediated Osteoclast Differentiation and Survival but Inhibits Osteoclast Function

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