Expression and function of periostin-like factor in vascular smooth muscle cells

Litvin, Judith; Chen, Xing; Keleman, Sheri; Zhu, Shimei; Autieri, Michael V.

doi:10.1152/ajpcell.00153.2006

Cited by 19 publications

(17 citation statements)

References 32 publications

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“…We also confirmed the localization of periostin in the Golgi. It is noteworthy that a subcellular localization of periostin has also been indicated (50,51), while secreted periostin is detected in the cell culture medium (9). Many secretory proteins are synthesized as inactive precursors in the ER and are usually cleaved at sites composed of single or paired basic amino acid residues by members of the subtilisin/kexin-like proprotein convertase family (52).…”

Section: Confined Tibial Periostitis Both In Periostinmentioning

confidence: 99%

Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

Kii

Nishiyama

et al. 2010

Journal of Biological Chemistry

246

247

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Extracellular matrix (ECM) underlies a complicated multicellular architecture that is subjected to significant forces from mechanical environment. Although various components of the ECM have been enumerated, mechanisms that evolve the sophisticated ECM architecture remain to be addressed. Here we show that periostin, a matricellular protein, promotes incorporation of tenascin-C into the ECM and organizes a meshwork architecture of the ECM. We found that both periostin null mice and tenascin-C null mice exhibited a similar phenotype, confined tibial periostitis, which possibly corresponds to medial tibial stress syndrome in human sports injuries. Periostin possessed adjacent domains that bind to tenascin-C and the other ECM protein: fibronectin and type I collagen, respectively. These adjacent domains functioned as a bridge between tenascin-C and the ECM, which increased deposition of tenascin-C on the ECM. The deposition of hexabrachions of tenascin-C may stabilize bifurcations of the ECM fibrils, which is integrated into the extracellular meshwork architecture. This study suggests a role for periostin in adaptation of the ECM architecture in the mechanical environment.

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Section: Confined Tibial Periostitis Both In Periostinmentioning

confidence: 99%

Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

Kii

Nishiyama

et al. 2010

Journal of Biological Chemistry

246

247

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“…These two proteins are single gene products and differ in their COOH terminal region [2, 8, 9]. Neither PLF nor Periostin are expressed in most adult tissues under normal conditions, but is expressed under conditions of mechanical overload or injury and repair of the musculoskeletal system, and in disease of the cardiovascular system [9–21]. Both isoforms are induced in adult tissues and cells under adverse conditions such as hypoxia, UV exposure, serum starvation, abnormal cell growth and pressure or volume and mechanical overload.…”

Section: Introductionmentioning

confidence: 99%

Periostin-like-factor and Periostin in an animal model of work-related musculoskeletal disorder

Rani

Barbe

Barr

et al. 2009

Bone

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Work-related musculoskeletal disorders (WMSDs), also known as overuse injuries, account for a substantial proportion of work injuries and workers’ compensation claims in the United States. However, the pathophysiological mechanisms underlying WMSDs are not well understood, especially the early events in their development. In this study we used an animal model of upper extremity WMSD, in which rats perform a voluntary repetitive reaching and pulling task for a food reward. This innovative model provides us an opportunity to investigate the role of molecules which may be used either as markers of early diagnosis of these disorders, and/or could be targeted for therapeutic purposes in the future. Periostin-Like-Factor (PLF), and Periostin were examined in this study. Both belong to a family of vitamin K-dependent gamma carboxylated proteins characterized by the presence of conserved Fasciclin domains and not detected in adult tissues except under conditions of chronic overload, injury, stress or pathology. The spatial and temporal pattern of PLF and Periostin localization was examined by immunohistochemistry and western blot analysis in the radius and ulna of animals performing a high repetition, high force task for up to 12 weeks and in controls. We found that PLF was present primarily in the cellular periosteum, articular cartilage, osteoblasts, osteocytes and osteoclasts at weeks 3 and 6 in all distal bone sites examined. This increase coincided with a transient increase in serum osteocalcin in week 6, indicative of adaptive bone formation at this time point. PLF immunoexpression decreased in the distal periosteum and metaphysis by week 12, coincided temporally with an increase in serum Trap5b, thinning of the growth plate and reduced cortical thickness. In contrast to PLF, once Periostin was induced by task performance, it continued to be present at a uniformly high level between 3 and 12 weeks in the trabeculae, fibrous and cellular periosteum, osteoblasts and osteocytes. In general, the data suggest that PLF is located in tissues during the early adaptive stage of remodeling but not during the pathological phase and therefore might be a marker of early adaptive remodeling.

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“…Alternative splicing at the C‐terminal end yields four different isoforms in mouse and human (as referenced in National Center for Biotechnology Information database). However, the function(s) and tissue localization of these isoforms remain unknown 4–7…”

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confidence: 99%

AP2 adaptor complex mediates bile salt export pump internalization and modulates its hepatocanalicular expression and transport function

et al. 2012

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The bile salt export pump (BSEP) mediates the biliary excretion of bile salts and its dysfunction induces intrahepatic cholestasis. Reduced canalicular expression of BSEP resulting from the promotion of its internalization is one of the causes of this disease state. However, the molecular mechanism underlying BSEP internalization from the canalicular membrane (CM) remains unknown. We have shown previously that 4-phenylbutyrate (4PBA), a drug used for ornithine transcarbamylase deficiency (OTCD), inhibited internalization and subsequent degradation of cell-surface-resident BSEP. The current study found that 4PBA treatment decreased significantly the expression of aand l2-adaptin, both of which are subunits of the AP2 adaptor complex (AP2) that mediates clathrin-dependent endocytosis, in liver specimens from rats and patients with OTCD, and that BSEP has potential AP2 recognition motifs in its cytosolic region. Based on this, the role of AP2 in BSEP internalization was explored further. In vitro analysis with 33FLAG-human BSEP-expressing HeLa cells and human sandwich-culture hepatocytes indicates that the impairment of AP2 function by RNA interference targeting of a-adaptin inhibits BSEP internalization from the plasma membrane and increases its cell-surface expression and transport function. Studies using immunostaining, coimmunoprecipitation, glutathione S-transferase pulldown assay, and time-lapse imaging show that AP2 interacts with BSEP at the CM through a tyrosine motif at the carboxyl terminus of BSEP and mediates BSEP internalization from the CM of hepatocytes. Conclusion: AP2 mediates the internalization and subsequent degradation of CMresident BSEP through direct interaction with BSEP and thereby modulates the canalicular expression and transport function of BSEP. This information should be useful for understanding the pathogenesis of severe liver diseases associated with intrahepatic cholestasis. (HEPATOLOGY 2012;55:1889-1900

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Expression and function of periostin-like factor in vascular smooth muscle cells

Cited by 19 publications

References 32 publications

Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

Incorporation of Tenascin-C into the Extracellular Matrix by Periostin Underlies an Extracellular Meshwork Architecture

Periostin-like-factor and Periostin in an animal model of work-related musculoskeletal disorder

AP2 adaptor complex mediates bile salt export pump internalization and modulates its hepatocanalicular expression and transport function

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