Prolyl Hydroxylase

Cardinale, George J.; Udenfriend, Sidney

doi:10.1002/9780470122860.ch6

Cited by 108 publications

(30 citation statements)

References 210 publications

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“…Both types of BMSC expressed several markers of those usually present, and considered typical, on MSC, whereas they were negative for surface receptors expressed on leukocytes. Importantly, the polygon-shaped BMSC, differently from the spindle-shaped BMSC, were intracytoplasmic positive for expression of the enzyme 4-prolyl-hydroxylase, which is involved in the hydroxylation of collagen and other protein with collagen-like amino acid sequences (60). Although both these BMSC types were sensitive to NK cell-mediated lysis, only the spindle-shaped BMSC were able to differentiate into adipocytes or osteoblasts under appropriate culture conditions (not shown), suggesting that within this cell population, some cells with a differentiating potential similar to that of MSC are present.…”

Section: Discussionmentioning

confidence: 96%

Interaction between Human NK Cells and Bone Marrow Stromal Cells Induces NK Cell Triggering: Role of NKp30 and NKG2D Receptors

Poggi¹,

Prevosto²,

Massaro³

et al. 2005

The Journal of Immunology

148

121

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In this study we have analyzed the interaction between in vitro cultured bone marrow stromal cells (BMSC) and NK cells. Ex vivo-isolated NK cells neoexpressed the activation Ag CD69 and released IFN-γ and TNF-α upon binding with BMSC. Production of these proinflammatory cytokines was dependent on ligation of ICAM1 expressed on BMSC and its receptor LFA1 on NK cells. Furthermore, the NKp30, among natural cytotoxicity receptors, appeared to be primarily involved in triggering NK cells upon interaction with BMSC. Unexpectedly, autologous IL-2-activated NK cells killed BMSC. Again, LFA1/ICAM1 interaction plays a key role in NK/BMSC interaction; this interaction is followed by a strong intracellular calcium increase in NK cells. More importantly, NKG2D/MHC-I-related stress-inducible molecule A and/or NKG2D/UL-16 binding protein 3 engagement is responsible for the delivery of a lethal hit. It appears that HLA-I molecules do not protect BMSC from NK cell-mediated injury. Thus, NK cells, activated upon binding with BMSC, may regulate BMSC survival.

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Section: Discussionmentioning

confidence: 96%

Interaction between Human NK Cells and Bone Marrow Stromal Cells Induces NK Cell Triggering: Role of NKp30 and NKG2D Receptors

Poggi¹,

Prevosto²,

Massaro³

et al. 2005

The Journal of Immunology

148

121

View full text Add to dashboard Cite

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“…About 3-6% of total tissue protein in the body is collagen, and the functional properties of skin depend on the integrity of collagen in the dermis. Changes in collagen expression occur during wound healing, new bone development, and aging [24]. Therefore, the control of collagen metabolism might be useful for a variety of therapeutic and cosmetic applications.…”

Section: Introductionmentioning

confidence: 99%

Effect of Porcine Placental Extract on Collagen Production in Human Skin Fibroblasts In Vitro

Yoshikawa

Takano²,

Ishigaki³

et al. 2013

Gynecol Obstet (Sunnyvale)

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Placental Extract (PE) has been used as a folk remedy in Asian countries. Human PE is clinically used for the treatment of skin wrinkles because it promotes skin regeneration. In this study, we found that Porcine PE (PPE) promoted collagen production in Normal Human Dermal Fibroblasts (NHDFs). Treatment of NHDFs with PPE at concentrations of 12.5-100 μg/mL enhanced their proliferation and secretion of procollagen C peptide. We also found that expression of intracellular Matrix Metalloproteinase-9 (MMP-9) in PPE-treated NHDFs was decreased in a dose-dependent manner. These results indicate that PPE might affect facial wrinkling partly by enhancing fibroblast proliferation and collagen secretion while inhibiting MMP-9 expression in NHDFs.

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“…Although many reports have utilized ascorbate as a stimulator for highrate secretion (13) or as an inducer of synchronized procollagen trafficking (6,7), the mechanism for the enhanced procollagen biosynthesis upon such stimulation has remained unclear. In response to increased traffic loads, regulated coordination of de novo biosynthesis must occur depending on the levels of undelivered cargos.…”

mentioning

confidence: 99%

Enhancement of Procollagen Biosynthesis by p180 through Augmented Ribosome Association on the Endoplasmic Reticulum in Response to Stimulated Secretion

Ueno

Tanaka

Kaneko

et al. 2010

Journal of Biological Chemistry

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A coiled-coil microtubule-bundling protein, p180, was originally reported as a ribosome-binding protein on the rough endoplasmic reticulum (ER) and is highly expressed in secretory tissues. Recently, we reported a novel role for p180 in the transGolgi network (TGN) expansion following stimulated collagen secretion. Here, we show that p180 plays a key role in procollagen biosynthesis and secretion in diploid fibroblasts. Depletion of p180 caused marked reductions of secreted collagens without significant loss of the ER membrane or mRNA. Metabolic labeling experiments revealed that the procollagen biosynthetic activity was markedly affected following p180 depletion. Moreover, loss of p180 perturbs ascorbate-stimulated de novo biosynthesis mainly in the membrane fraction with a preferential secretion defect of large proteins. At the EM level, one of the most prominent morphological features of p180-depleted cells was insufficient ribosome association on the ER membranes. In contrast, the ER of control cells was studded with numerous ribosomes, which were further enhanced by ascorbate. Similarly biochemical analysis confirmed that levels of membrane-bound ribosomes were altered in a p180-dependent manner. Taken together, our data suggest that p180 plays crucial roles in enhancing collagen biosynthesis at the entry site of the secretory compartments by a novel mechanism that mainly involves facilitating ribosome association on the ER. Entry of proteins into the secretory pathway via the rough endoplasmic reticulum (ER)3 is essential for intracellular transport of proteins to secretory compartments within the cell and finally to the extracellular milieu. In tissues with high secretory activity, such as the pancreas, the secretory apparatus is highly developed. One of the morphological hallmarks in such tissues is drastic proliferation of rough ER membranes that are densely occupied by ribosomes, whereas the rough ER in other tissues forms a loose network of tubular cisternae sparsely studded with ribosomes (1). However, the molecular basis for the biogenesis and proliferation of the rough ER in secretory tissues is largely unknown (1, 2).Collagen is one of the major components of the extracellular matrix (ECM) in connective tissues such as skin, tendon, and bone. It is synthesized on the ER membrane as a precursor form, i.e. procollagen, and secreted by professional secretory cells including fibroblasts. Fully consistent with the normal secretory pathway, procollagen is cotranslationally translocated into the lumen of the ER. Much interest has been focused on the mechanisms of its folding and trimerization processes in the ER, such as the hydroxylation enzymes for proline and lysine residues (reviewed in Refs. 3 and 4)). Recently, there has been considerable interest in the intracellular trafficking mechanism of procollagen as a representative model for supramolecular cargos (5-7). In addition, the regulation of procollagen biosynthesis has been intensively studied at the transcriptional level (8, 9) as well as at the...

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Prolyl Hydroxylase

Cited by 108 publications

References 210 publications

Interaction between Human NK Cells and Bone Marrow Stromal Cells Induces NK Cell Triggering: Role of NKp30 and NKG2D Receptors

Interaction between Human NK Cells and Bone Marrow Stromal Cells Induces NK Cell Triggering: Role of NKp30 and NKG2D Receptors

Effect of Porcine Placental Extract on Collagen Production in Human Skin Fibroblasts In Vitro

Enhancement of Procollagen Biosynthesis by p180 through Augmented Ribosome Association on the Endoplasmic Reticulum in Response to Stimulated Secretion

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