Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence.

Oldberg, Åke; Franzén, Ahnders; Heinegård, Dick

doi:10.1073/pnas.83.23.8819

Cited by 997 publications

(644 citation statements)

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“…OPN is a phosphoglycoprotein originally isolated from bone extracellular matrix [29]. It is synthesized by a variety of immune and nonimmune cells including macrophages, lymphocytes, fibroblasts, osteoclasts, epithelial cells, endothelial cells, and smooth muscle cells [30].…”

Section: Discussionmentioning

confidence: 99%

Biochemical markers of bone turnover in diagnosis of myeloma bone disease

Dizdar¹,

Barışta²,

Kalyoncu³

et al. 2006

American J Hematol

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This study was designed to explore the value of markers of bone turnover, macrophage inflammatory protein-1a (MIP-1a), and osteopontin (OPN) in the diagnosis of myeloma bone disease. Twenty-five patients with newly diagnosed and untreated multiple myeloma (MM), and 22 age-, sex-, and bone mineral density-matched control subjects were enrolled. Levels of MIP-1a, OPN, carboxy-terminal telopeptide of Type-1 collagen (C-telopeptide or Ctx), deoxypyridinoline (DPD), Type-1 collagen propeptide (T1Pro), and bone-specific alkaline phosphatase (BALP) were assessed in both groups. Twenty-two of the patients had bone involvement documented by skeletal surveys and lumbar spinal magnetic resonance imaging. Levels of serum Ctx, OPN, MIP-1a, and urine DPD were significantly higher in MM patients with bone disease than in controls (P < 0.01). Serum Ctx levels were elevated in 90.9% of patients with MM and 40.9% of controls (P < 0.001). Urine DPD levels were elevated in 90.4% of the patients and 31.8% of the controls (P < 0.001). The serum OPN and MIP-1a levels of the patients were significantly correlated with b2-microglobulin and lactate dehydrogenase levels (P < 0.05). Our study indicates that Ctx and DPD are sensitive markers of bone disease in MM, and higher than normal values suggest presence of bone disease rather than benign osteoporosis in MM. The utility of OPN and MIP-1a needs to be further investigated. Am. J. Hematol. 82:185-191, 2007. V V C 2006 Wiley-Liss, Inc.

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Section: Discussionmentioning

confidence: 99%

Biochemical markers of bone turnover in diagnosis of myeloma bone disease

Dizdar¹,

Barışta²,

Kalyoncu³

et al. 2006

American J Hematol

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“…Here, we have shown that FGD1 is required for effective transport of cargo proteins from the Golgi complex to the plasma membrane in general, whereas in osteoblasts it regulates the secretion of PC-I, osteocalcin, osteonectin, and osteopontin. All of these proteins have fundamental roles in the generation of mineralized extracellular matrix during bone development (Lian et al, 1978;Termine et al, 1981;Oldberg et al, 1986;Leblond, 1989), and therefore their aberrant transport through a lack of FGD1 are likely to contribute to the FGDY manifestations.…”

Section: Discussionmentioning

confidence: 99%

“…All of these proteins are soluble (i.e., reside in the lumen of secretory compartments), and therefore they have a topology different from that of VSVG (which is a transmembrane protein). Moreover, they are of different sizes, being either relatively small (osteocalcin, osteonectin, and ostopontin; Lian et al, 1978;Termine et al, 1981;Oldberg et al, 1986) or forming large supramolecular aggregates within early compartments of the secretory pathway (PC-I; Leblond, 1989). All of these proteins have fundamental roles in bone morphogenesis.…”

Section: Fgd1 Is Required For Transport Of Bone Proteins In Osteoblastsmentioning

confidence: 99%

Faciogenital Dysplasia Protein (FGD1) Regulates Export of Cargo Proteins from the Golgi Complex via Cdc42 Activation

Egorov

Capestrano

Vorontsova

et al. 2009

MBoC

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Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY). FGD1 encodes a guanine nucleotide exchange factor that specifically activates the GTPase Cdc42. In turn, Cdc42 is an important regulator of membrane trafficking, although little is known about FGD1 involvement in this process. During development, FGD1 is highly expressed during bone growth and mineralization, and therefore a lack of the functional protein leads to a severe phenotype. Whether the secretion of proteins, which is a process essential for bone formation, is altered by mutations in FGD1 is of great interest. We initially show here that FGD1 is preferentially associated with the trans-Golgi network (TGN), suggesting its involvement in export of proteins from the Golgi. Indeed, expression of a dominant-negative FGD1 mutant and RNA interference of FGD1 both resulted in a reduction in post-Golgi transport of various cargoes (including bone-specific proteins in osteoblasts). Live-cell imaging reveals that formation of post-Golgi transport intermediates directed to the cell surface is inhibited in FGD1-deficient cells, apparently due to an impairment of TGN membrane extension along microtubules. These effects depend on FGD1 regulation of Cdc42 activation and its association with the Golgi membranes, and they may contribute to FGDY pathogenesis.

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“…It is a sialic acid-rich phosphorylated glycoprotein originally isolated from the bone. The opn gene contains a Gly-Arg-Gly-Asp-Ser (GRGDS) -encoding motif that promotes cell attachment via avb3 integrin (Oldberg et al, 1986) and CD44 (Weber et al, 1996). Opn has been suggested to play important roles in the process of neoplastic metastasis (Brown et al, 1994;Oates et al, 1996) by enhancement of cell attachment through Opn receptors.…”

Section: Introductionmentioning

confidence: 99%