Involvement of stress-activated protein kinase/c-Jun N-terminal kinase in endothelin-1-induced heat shock protein 27 in osteoblasts

Tokuda, Harukuni; Niwa, Masayuki; Ito, Hidenori; Oiso, Yutaka; Kato, Kenji; Kozawa, Osamu

doi:10.1530/eje.0.1490239

Cited by 12 publications

(9 citation statements)

References 28 publications

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“…The compounds PD98059 (ERK inhibitor; Maiti et al, 2008), SB203580 (p38 inhibitor; Maiti et al, 2008), and SP600125 (JNK Inhibitor – SP600125; Tokuda et al, 2003) were obtained from Cell Signaling Technologies (Hertfordshire, UK) and used in the concentration range of 3–30 μM as based on published data (Gallicchio et al, 2009). In selected experiments the ERK inhibitor (10 μM) was tested against peptide Ac2-26 validating blockade of phosphor-ERK accumulation by Western blotting using a described methodology (Hayhoe et al, 2006).…”

Section: Methodsmentioning

confidence: 99%

Annexin A1 N-Terminal Derived Peptide Ac2-26 Exerts Chemokinetic Effects on Human Neutrophils

Dalli¹,

Montero‐Melendez²,

McArthur³

et al. 2012

Front. Pharmacol.

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It is postulated that peptides derived from the N-terminal region of Annexin A1, a glucocorticoid-regulated 37-kDa protein, could act as biomimetics of the parent protein. However, recent evidence, amongst which the ability to interact with distinct receptors other then that described for Annexin A1, suggest that these peptides might fulfill other functions at variance to those reported for the parent protein. Here we tested the ability of peptide Ac2-26 to induce chemotaxis of human neutrophils, showing that this peptide can elicit responses comparable to those produced by the canonical activator formyl-Met-Leu-Phe (or FMLP). However, whilst disruption of the chemical gradient abolished the FMLP response, addition of peptide Ac2-26 in the top well of the chemotaxis chamber did not affect (10 μM) or augmented (at 30 μM) the neutrophil locomotion to the bottom well, as elicited by 10 μM peptide Ac2-26. Intriguingly, the sole addition of peptide Ac2-26 in the top wells produced a marked migration of neutrophils. A similar behavior was observed when human primary monocytes were used. Thus, peptide Ac2-26 is a genuine chemokinetic agent toward human blood leukocytes. Neutralization strategies indicated that engagement of either the GPCR termed FPR1 or its cognate receptor FPR2/ALX was sufficient to sustain peptide Ac2-26 induced neutrophil migration. Similarly, application of pharmacological inhibitors showed that cell locomotion to peptide Ac2-26 was mediated primarily by the ERK, but not the JNK and p38 pathways. In conclusion, we report here novel in vitro properties for peptide Ac2-26, promoting neutrophil and monocyte chemokinesis; a process that may contribute to accelerate the resolution phase of inflammation. We postulate that the generation of Annexin A1 N-terminal peptides at the site of inflammation may expedite the egress of migrated leukocytes thus promoting the return to homeostasis.

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Section: Methodsmentioning

confidence: 99%

Annexin A1 N-Terminal Derived Peptide Ac2-26 Exerts Chemokinetic Effects on Human Neutrophils

Dalli¹,

Montero‐Melendez²,

McArthur³

et al. 2012

Front. Pharmacol.

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“…Protein samples were mixed with an equal volume of 2Â SDS sample buffer, boiled for 10 min, and subjected to 8% SDS-PAGE and Western blot analysis as described previously [Tokuda et al, 2003]. The nitrocellulose membrane was blocked with 5% milk, Tris-buffered saline (TBS)-0.2% Tween-20 (TTBS) for 2 h, and incubated with primary antibody (0.5 mg/ml) for 2 h. The blot was then washed three-times in TTBS and incubated with 0.1 mg/ml of HRPconjugated goat anti-rabbit IgG secondary antibody (Pierce) for 2 h at room temperature.…”

Section: Western Blot Analysismentioning

confidence: 99%

Expression and function of periostin‐isoforms in bone

Litvin

Selim

Montgomery

et al. 2004

J of Cellular Biochemistry

156

194

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Periostin was originally identified in MC3T3-E1 osteoblast-like cells. We have identified an isoform of periostin referred to as periostin-like-factor (PLF). It is homologous to other proteins such as fasciclin I (fas I), MPB70, betaIG-H3, and Algal-CAMs. All of these proteins are implicated in regulating cell adhesion. PLF and the other isoforms of periostin differ in their C-terminal sequences. PLF and periostin differ in two specific regions, between 673 and 699 amino acids (aa) and 785-812 aa. Periostin isoforms are expressed in vivo and in vitro during the stages of osteoblast differentiation and maturation. Their mRNAs are present in pre-osteoblast cells as detected by in situ hybridization, and the proteins are between 86 and 93 kD in size as determined by Western blot analysis. Antisense oligonucleotides and antibodies directed against the isoforms of periostin were used to block the activity of these proteins. In both cases, the levels of osteoblast-specific-differentiation markers were markedly reduced suggesting a role for these proteins in osteoblast differentiation.

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“…HSPs are multifunctional proteins involved in a variety of cellular activities such as antiapoptotic self-protection in response to cytotoxic environments Cooper et al 2000), tissue regeneration (Hebb et al 2006;Laplante et al 1998), actin stabilization (Russotti et al 1997), and differentiation by regulating caspase activity and stabilizing proteins associated with differentiation (Lanneau et al 2007). In particular, HSP27 is involved in bone physiology through upregulation of TGF-β (Hatakeyama et al 2002) and estrogen (Cooper and Uoshima 1994) which can increase bone mass, endothelin-1 (Tokuda et al 2003), and prostaglandins (Kozawa et al 2001). HSP47 is a procollagen-binding protein expressed in the endoplasmic reticulum (Nagata 1998) and involved in the biosynthesis of type I collagen (Dafforn et al 2001), a major bone extracellular matrix protein.…”

Section: Introductionmentioning

confidence: 99%

Response of preosteoblasts to thermal stress conditioning and osteoinductive growth factors

Chung

Rylander

2012

Cell Stress and Chaperones

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Conditioning protocols involving mechanical stress independently or with chemical cues such as growth factors (GFs) possess significant potential to enhance bone regeneration. However, utilization of thermal stress conditioning alone or with GFs for bone therapy has been under-investigated. In this study, a preosteoblast cell line (MC3T3-E1) was exposed to treatment with water bath heating (44°C, 4 and 8 min) and osteoinductive GFs (bone morphogenetic protein-2 and transforming growth factor-β1) individually or in combination to investigate whether these stimuli could promote induction of bone-related markers, an angiogenic factor, and heat shock proteins (HSPs). Cells remained viable when heating durations were less than 20 min at 40ºC, 16 min at 42ºC, and 10 min at 44ºC. Increasing heating duration at 44°C, promoted gene expression of HSPs, osteocalcin (OCN), and osteopontin (OPN) at 8 h post-heating (PH). Heating in combination with GFs caused the greatest gene induction of osteoprotegerin (OPG; 6.9- and 1.6-fold induction compared to sham-treated and GF only treated groups, respectively) and vascular endothelial growth factor (VEGF; 16.0- and 1.6-fold compared to sham and GF-only treated groups, respectively) at 8 h PH. Both heating and GFs independently suppressed the matrix metalloproteinase-9 (MMP-9) gene. GF treatment caused a more significant decrease in MMP-9 protein secretion to non-detectable levels compared to heating alone at 72 h PH. Secretion of OCN, OPN, and OPG increased with the addition of GFs but diminished with heating as measured by ELISA at 72 h PH. These results suggest that conditioning protocols utilizing heating and GFs individually or in combination can induce HSPs, bone-related proteins, and VEGF while also causing downregulation of osteoclastic activity, potentially providing a promising bone therapeutic strategy.

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Involvement of stress-activated protein kinase/c-Jun N-terminal kinase in endothelin-1-induced heat shock protein 27 in osteoblasts

Cited by 12 publications

References 28 publications

Annexin A1 N-Terminal Derived Peptide Ac2-26 Exerts Chemokinetic Effects on Human Neutrophils

Annexin A1 N-Terminal Derived Peptide Ac2-26 Exerts Chemokinetic Effects on Human Neutrophils

Expression and function of periostin‐isoforms in bone

Response of preosteoblasts to thermal stress conditioning and osteoinductive growth factors

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