Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone

Ito, Shinya; Nagata, Kazuhiro

doi:10.1016/j.semcdb.2016.11.005

Cited by 197 publications

(159 citation statements)

References 97 publications

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“…It is difficult to reconcile these data with a dedicated role in the transport of large cargo. That said, some further support for a direct role of TANGO1 in procollagen export comes from experiments looking at the procollagen-specific chaperone Hsp47 (Ito and Nagata 2017; Nagata et al 1986). TANGO1 binds directly to Hsp47 (Ishikawa et al 2016).…”

Section: Efficient Assembly Of the Copii Coat As A Prerequisite For Pmentioning

confidence: 99%

“…Hsp47 interacts with the SH3 domain of TANGO1 and can bind to both monomeric (Hosokawa and Nagata 2000) and trimeric procollagens, with a higher affinity for the latter (Fig. 2, step 1), thus acting as a cargo adapter with no specificity for particular procollagen types (Ito and Nagata 2017; Koide et al 1999; Tasab et al 2000). …”

Section: Efficient Assembly Of the Copii Coat As A Prerequisite For Pmentioning

confidence: 99%

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COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

McCaughey

Stephens

2018

Histochem Cell Biol

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The export of newly synthesized proteins from the endoplasmic reticulum is fundamental to the ongoing maintenance of cell and tissue structure and function. After co-translational translocation into the ER, proteins destined for downstream intracellular compartments or secretion from the cell are sorted and packaged into transport vesicles by the COPII coat protein complex. The fundamental discovery and characterization of the pathway has now been augmented by a greater understanding of the role of COPII in diverse aspects of cell function. We now have a deep understanding of how COPII contributes to the trafficking of diverse cargoes including extracellular matrix molecules, developmental signalling proteins, and key metabolic factors such as lipoproteins. Structural and functional studies have shown that the COPII coat is both highly flexible and subject to multiple modes of regulation. This has led to new discoveries defining roles of COPII in development, autophagy, and tissue organization. Many of these newly emerging features of the canonical COPII pathway are placed in a context of procollagen secretion because of the fundamental interest in how a coat complex that typically generates 80-nm transport vesicles can package a cargo reported to be over 300 nm. Here we review the current understanding of COPII and assess the current consensus on its role in packaging diverse cargo proteins.

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Section: Efficient Assembly Of the Copii Coat As A Prerequisite For Pmentioning

confidence: 99%

Section: Efficient Assembly Of the Copii Coat As A Prerequisite For Pmentioning

confidence: 99%

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

McCaughey

Stephens

2018

Histochem Cell Biol

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“…Serpin, found in our assay, may represent uterine serpins, most probably involved in the inhibition of an immune response of the mother against the fetus or can participate in placental transportation while extracellular serpins are inhibitors of proteases. Another member of the serpin family, HSP 47, is crucial for collagen folding; however, it does not exert serine protease inhibitory activity …”

Section: Resultsmentioning

confidence: 99%

Identification of protein patterns in bovine placenta at early‐mid pregnancy – Pilot studies

Ner‐Kluza

Wawrzykowski

Franczyk

et al. 2019

Rapid Comm Mass Spectrometry

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Rationale Placenta is a crucial tissue for an appropriate development of the fetus and the course of pregnancy. Its composition and structure change dynamically along pregnancy but the full pattern of these changes is not fully described in cows yet. The aim of the present study was to detect qualitative and quantitative protein profiles of bovine placenta during early‐mid pregnancy at the time of placental formation. Methods Placental tissues from healthy cows (n = 3) in early pregnancy (3–5 months) were collected at the slaughterhouse. Maternal and fetal parts were manually divided prior to homogenization. Further analysis was done in triplicates on the maternal and fetal parts separately and subjected to one‐dimensional (1D) electrophoretic separation, followed by identification of peptide maps by nanospray liquid chromatography/tandem mass spectrometry (nanoLC/MS/MS). Proteins were identified by use of the MASCOT software with the SwissProt database. Results Proteomic analysis showed more than 4000 differentially expressed proteins in maternal and fetal parts of placenta. Each part expressed around 900 proteins, of which ca. 90 were common. The identified proteins were analyzed in accordance to molecular function and their participation in biological processes. Conclusions The obtained results provide new insight into the knowledge about biochemical characteristics of placenta (new proteins) and serve for further studies on the possible markers of physiological/pathological pregnancy or function of placenta. Moreover, our data can be a good starting point for further studies on the processes underlying the attachment of placenta.

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“…The latter may also have a role to play in hyaluronic acid metabolism, as it is a HABP. Serpin H1 (Hsp47) is a collagen‐specific chaperone and the slight decline in its levels is uncertain but expression kinetics may have a role to play as previously discussed .…”

Section: Discussionmentioning

confidence: 99%

Bio‐derived hydroxystearic acid ameliorates skin age spots and conspicuous pores

Schütz

Rawlings²,

Wandeler

et al. 2019

Intern J of Cosmetic Sci

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IntroductionWe report on the preparation and efficacy of 10‐hydroxystearic acid (HSA) that improves facial age spots and conspicuous pores.MethodsThe hydration of oleic acid into HSA was catalyzed by the oleate hydratase from Escherichia coli. Following treatment with HSA, collagen type I and type III was assessed in primary human dermal fibroblasts together with collagen type III, p53 protein levels and sunburn cells (SBC) after UVB irradiation (1 J cm−2) by immunohistochemistry on human ex vivo skin. UVB‐induced expression of matrix metalloprotease‐1 (MMP‐1) was determined from full thickness skin by RT‐qPCR. Modification of the fibroblast secretome by HSA was studied by mass‐spectrometry‐based proteomics. In a full‐face, double blind, vehicle‐controlled trial HSA was assessed for its effects on conspicuous facial pore size and degree of pigmentation of age spots in Caucasian women over an 8‐week period.ResultsHSA was obtained in enantiomeric pure, high yield (≥80%). Collagen type I and type III levels were dose‐dependently increased (96% and 244%; P < 0.01) in vitro and collagen type III in ex vivo skin by +57% (P < 0.01) by HSA. HSA also inhibited UVB‐induced MMP‐1 gene expression (83%; P < 0.01) and mitigated SBC induction (−34% vs. vehicle control) and reduced significantly UV‐induced p53 up‐regulation (−46% vs. vehicle control; P < 0.01) in irradiated skin. HSA modified the fibroblast secretome with significant increases in proteins associated with the WNT pathway that could reduce melanogenesis and proteins that could modify dermal fibroblast activity and keratinocyte differentiation to account for the alleviation of conspicuous pores. Docking studies in silico and EC50 determination in reporter gene assays (EC50 5.5 × 10−6 M) identified HSA as a peroxisomal proliferator activated receptor‐α (PPARα) agonist. Clinically, HSA showed a statistically significant decrease of surface and volume of skin pores (P < 0.05) after 8 weeks of application and age spots became significantly less pigmented than the surrounding skin (contrast, P < 0.05) after 4 weeks.ConclusionHSA acts as a PPARα agonist to reduce the signs of age spots and conspicuous pores by significantly modulating the expression of p53, SBC, MMP‐1 and collagen together with major changes in secreted proteins that modify keratinocyte, melanocyte and fibroblast cell behavior.

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Biology of Hsp47 (Serpin H1), a collagen-specific molecular chaperone

Cited by 197 publications

References 97 publications

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

Identification of protein patterns in bovine placenta at early‐mid pregnancy – Pilot studies

Bio‐derived hydroxystearic acid ameliorates skin age spots and conspicuous pores

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