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Journal articles on the topic 'Prolyl hydroxylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Bhute, Vijesh J., James Harte, Jack W. Houghton, and Patrick H. Maxwell. "Mannose Binding Lectin Is Hydroxylated by Collagen Prolyl-4-hydroxylase and Inhibited by Some PHD Inhibitors." Kidney360 1, no. 6 (2020): 447–57. http://dx.doi.org/10.34067/kid.0000092020.

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BackgroundMannose-binding lectin (MBL) is an important component of innate immune defense. MBL undergoes oligomerization to generate high mol weight (HMW) forms which act as pattern recognition molecules to detect and opsonize various microorganisms. Several post-translational modifications including prolyl hydroxylation are known to affect the oligomerization of MBL. Yet, the enzyme(s) which hydroxylate proline in the collagen-like domain residues have not been identified and the significance of prolyl hydroxylation is incompletely understood.MethodsTo investigate post-translational modificat

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2

Horita, Shoichiro, John Scotti, Michael McDonough, et al. "Crystal structures of 2OG oxygenases involved in ribosomal protein hydroxylation." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C304. http://dx.doi.org/10.1107/s2053273314096958.

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Post-translational modifications play diverse biological functions. Hydroxylation of collagen proteins has long been a recognised post-translational modification in eukaryotes. In the case of collagen, hydroxylation of prolyl residues, by 2-oxoglutarate and iron dependent enzymes (2OG oxygenases), in collagen proteins allows for the stabilisation of the collagen triple helix structure through conformational restraint and through the addition of a hydrogen bond donor. Additionally, hydroxylation of lysine side chains of collagen is required for cross-linking collagen (and possibly other protein

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3

Markolovic, Suzana, Sarah E. Wilkins, and Christopher J. Schofield. "Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases." Journal of Biological Chemistry 290, no. 34 (2015): 20712–22. http://dx.doi.org/10.1074/jbc.r115.662627.

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The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen biosynthesis. 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible factors that play important roles in the adaptive response to hypoxia. Subsequently, they have been shown to catalyze N-demethylation (via hydroxylation) of Nϵ-methylated histone lysyl residues, as well as hydroxylation of multiple other residues. Recent work has identified roles for 2OG oxygenases in the modification of translation-a

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4

Rappu, Pekka, Antti M. Salo, Johanna Myllyharju, and Jyrki Heino. "Role of prolyl hydroxylation in the molecular interactions of collagens." Essays in Biochemistry 63, no. 3 (2019): 325–35. http://dx.doi.org/10.1042/ebc20180053.

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Abstract Co- and post-translational hydroxylation of proline residues is critical for the stability of the triple helical collagen structure. In this review, we summarise the biology of collagen prolyl 4-hydroxylases and collagen prolyl 3-hydroxylases, the enzymes responsible for proline hydroxylation. Furthermore, we describe the potential roles of hydroxyproline residues in the complex interplay between collagens and other proteins, especially integrin and discoidin domain receptor type cell adhesion receptors. Qualitative and quantitative regulation of collagen hydroxylation may have remark

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5

Ono, Masaya, Junichi Matsubara, Kazufumi Honda та ін. "Prolyl 4-Hydroxylation of α-Fibrinogen". Journal of Biological Chemistry 284, № 42 (2009): 29041–49. http://dx.doi.org/10.1074/jbc.m109.041749.

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6

Narayanan, A. S., D. F. Meyers, and R. C. Page. "Mononuclear cell supernatants inhibit prolyl hydroxylation." FEBS Letters 179, no. 2 (1985): 229–32. http://dx.doi.org/10.1016/0014-5793(85)80524-x.

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7

Franklin, T. J., and M. Hitchen. "Inhibition of collagen hydroxylation by 2,7,8-trihydroxyanthraquinone in embryonic-chick tendon cells." Biochemical Journal 261, no. 1 (1989): 127–30. http://dx.doi.org/10.1042/bj2610127.

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Prolyl 4-hydroxylase (EC 1.14.11.2) is an essential enzyme in the post-translational modification of collagen. Inhibitors of this enzyme are of potential interest for the treatment of diseases involving excessive deposition of collagen. 2,7,8-Trihydroxyanthraquinone (THA) is an effective inhibitor of prolyl 4-hydroxylase by virtue of its ability to compete with the co-substrate 2-oxoglutarate (Ki = 40.3 microM). Using a simple and reproducible assay for collagen hydroxylation, we show that THA inhibits the hydroxylation of collagen in embryonic-chick tendon cells in short-term culture, with an

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8

FRANKLIN, Trevor J., William P. MORRIS, Philip N. EDWARDS, Michael S. LARGE, and Robert STEPHENSON. "Inhibition of prolyl 4-hydroxylase in vitro and in vivo by members of a novel series of phenanthrolinones." Biochemical Journal 353, no. 2 (2001): 333–38. http://dx.doi.org/10.1042/bj3530333.

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Examples of a novel series of phenanthrolinones are shown to be potent competitive inhibitors of avian prolyl 4-hydroxylase, and of collagen hydroxylation, in embryonic chick tendon cells and human foreskin fibroblasts in vitro and in the oestradiol-stimulated rat uterus in vivo. Two compounds, Compound 1 (1,4-dihydrophenanthrolin-4-one-3-carboxylic acid) and Compound 5 [8-(N-butyl-N-ethylcarbamoyl)-1,4-dihydrophenathrolin-4-one-3-carboxylic acid], with comparable potencies in vivo, were chosen to investigate the effect of the inhibition of the hydroxylation of newly synthesized uterine collag

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9

Luo, Weibo, Benjamin Lin, Yingfei Wang, et al. "PHD3-mediated prolyl hydroxylation of nonmuscle actin impairs polymerization and cell motility." Molecular Biology of the Cell 25, no. 18 (2014): 2788–96. http://dx.doi.org/10.1091/mbc.e14-02-0775.

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Actin filaments play an essential role in cell movement, and many posttranslational modifications regulate actin filament assembly. Here we report that prolyl hydroxylase 3 (PHD3) interacts with nonmuscle actin in human cells and catalyzes hydroxylation of actin at proline residues 307 and 322. Blocking PHD3 expression or catalytic activity by short hairpin RNA knockdown or pharmacological inhibition, respectively, decreased actin prolyl hydroxylation. PHD3 knockdown increased filamentous F-actin assembly, which was reversed by PHD3 overexpression. PHD3 knockdown increased cell velocity and mi

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10

Flashman, Emily, Sarah L. Davies, Kar Kheng Yeoh, and Christopher J. Schofield. "Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents." Biochemical Journal 427, no. 1 (2010): 135–42. http://dx.doi.org/10.1042/bj20091609.

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The HIF (hypoxia-inducible factor) hydroxylases [PHDs or EGLNs (prolyl hydroxylases), which in humans are PHD isoforms 1–3, and FIH (factor inhibiting HIF)] regulate HIF levels and activity. These enzymes are Fe(II)/2-oxoglutarate-dependent oxygenases, many of which are stimulated by ascorbate. We have investigated the ascorbate dependence of PHD2-catalysed hydroxylation of two prolyl hydroxylation sites in human HIF-1α, and of FIH-catalysed hydroxylation of asparaginyl hydroxylation sites in HIF-1α and in a consensus ankyrin repeat domain peptide. The initial rate and extent of hydroxylation

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11

Qi, Hank H., Pat P. Ongusaha, Johanna Myllyharju, et al. "Prolyl 4-hydroxylation regulates Argonaute 2 stability." Nature 455, no. 7211 (2008): 421–24. http://dx.doi.org/10.1038/nature07186.

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12

Schmelzer, Christian E. H., Marcus B. M. Nagel, Szymon Dziomba, Yulia Merkher, Sarit S. Sivan, and Andrea Heinz. "Prolyl hydroxylation in elastin is not random." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 10 (2016): 2169–77. http://dx.doi.org/10.1016/j.bbagen.2016.05.013.

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13

Wang, Shike, Kuo-Hao Lee, Nathalia Victoria Araujo, Chang-Guo Zhan, Vivek M. Rangnekar, and Ren Xu. "Develop a High-Throughput Screening Method to Identify C-P4H1 (Collagen Prolyl 4-Hydroxylase 1) Inhibitors from FDA-Approved Chemicals." International Journal of Molecular Sciences 21, no. 18 (2020): 6613. http://dx.doi.org/10.3390/ijms21186613.

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Collagen prolyl 4-hydroxylase 1 (C-P4H1) is an α-ketoglutarate (α-KG)-dependent dioxygenase that catalyzes 4-hydroxylation of proline on collagen. C-P4H1-induced prolyl hydroxylation is required for proper collagen deposition and cancer metastasis. Therefore, targeting C-P4H1 is considered a potential therapeutic strategy for collagen-related cancer progression and metastasis. However, no C-P4H1 inhibitors are available for clinical testing, and the high content assay is currently not available for C-P4H1 inhibitor screening. In the present study, we developed a high-throughput screening assay

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14

Zagórska, Anna, and Józef Dulak. "HIF-1: the knowns and unknowns of hypoxia sensing." Acta Biochimica Polonica 51, no. 3 (2004): 563–85. http://dx.doi.org/10.18388/abp.2004_3545.

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Hypoxia-inducible factor-1 (HIF-1) is a transcriptional activator that functions as a master regulator of cellular and systemic oxygen homeostasis. It consists of two constitutively produced subunits: HIF-1alpha and HIF-1beta. Under normoxic conditions HIF-1alpha undergoes hydroxylation at specific prolyl residues which leads to an immediate ubiquitination and subsequent proteasomal degradation of the alpha subunit. Additionally, hydroxylation of an asparaginyl residue blocks the transcriptional activity of HIF-1 due to inhibition of its interaction with co-activators. In contrast, under hypox

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15

Aviner, Ranen, Kathy H. Li, Judith Frydman, and Raul Andino. "Cotranslational prolyl hydroxylation is essential for flavivirus biogenesis." Nature 596, no. 7873 (2021): 558–64. http://dx.doi.org/10.1038/s41586-021-03851-2.

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16

Pappalardi, Melissa B., Dean E. McNulty, John D. Martin, et al. "Biochemical characterization of human HIF hydroxylases using HIF protein substrates that contain all three hydroxylation sites." Biochemical Journal 436, no. 2 (2011): 363–69. http://dx.doi.org/10.1042/bj20101201.

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The HIF (hypoxia-inducible factor) plays a central regulatory role in oxygen homoeostasis. HIF proteins are regulated by three Fe(II)- and α-KG (α-ketoglutarate)-dependent prolyl hydroxylase enzymes [PHD (prolyl hydroxylase domain) isoenzymes 1–3 or PHD1, PHD2 and PHD3] and one asparaginyl hydroxylase [FIH (factor inhibiting HIF)]. The prolyl hydroxylases control the abundance of HIF through oxygen-dependent hydroxylation of specific proline residues in HIF proteins, triggering subsequent ubiquitination and proteasomal degradation. FIH inhibits the HIF transcription activation through asparagi

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17

Kapitsinou, Pinelopi P., Jonathan Jaffe, Mark Michael, et al. "Preischemic targeting of HIF prolyl hydroxylation inhibits fibrosis associated with acute kidney injury." American Journal of Physiology-Renal Physiology 302, no. 9 (2012): F1172—F1179. http://dx.doi.org/10.1152/ajprenal.00667.2011.

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Acute kidney injury (AKI) due to ischemia is an important contributor to the progression of chronic kidney disease (CKD). Key mediators of cellular adaptation to hypoxia are oxygen-sensitive hypoxia-inducible factors (HIF), which are regulated by prolyl-4-hydroxylase domain (PHD)-containing dioxygenases. While activation of HIF protects from ischemic cell death, HIF has been shown to promote fibrosis in experimental models of CKD. The impact of HIF activation on AKI-induced fibrosis has not been defined. Here, we investigated the role of pharmacologic HIF activation in AKI-associated fibrosis

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18

Barth, Sandra, Jutta Nesper, Philippe A. Hasgall, et al. "The Peptidyl Prolyl cis/trans Isomerase FKBP38 Determines Hypoxia-Inducible Transcription Factor Prolyl-4-Hydroxylase PHD2 Protein Stability." Molecular and Cellular Biology 27, no. 10 (2007): 3758–68. http://dx.doi.org/10.1128/mcb.01324-06.

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ABSTRACT The heterodimeric hypoxia-inducible transcription factors (HIFs) are central regulators of the response to low oxygenation. HIF-α subunits are constitutively expressed but rapidly degraded under normoxic conditions. Oxygen-dependent hydroxylation of two conserved prolyl residues by prolyl-4-hydroxylase domain-containing enzymes (PHDs) targets HIF-α for proteasomal destruction. We identified the peptidyl prolyl cis/trans isomerase FK506-binding protein 38 (FKBP38) as a novel interactor of PHD2. Yeast two-hybrid, glutathione S-transferase pull-down, coimmunoprecipitation, colocalization

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19

Myllylä, R., D. D. Kaska, and K. I. Kivirikko. "The catalytic mechanism of the hydroxylation reaction of peptidyl proline and lysine does not require protein disulphide-isomerase activity." Biochemical Journal 263, no. 2 (1989): 609–11. http://dx.doi.org/10.1042/bj2630609.

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Prolyl 4-hydroxylase, an alpha 2 beta 2 tetramer, catalyses the formation of 4-hydroxyproline in collagens. The beta subunit is known to be identical with the enzyme protein disulphide-isomerase and to possess disulphide-isomerase activity even when present in the prolyl 4-hydroxylase tetramer. We here report that lysyl hydroxylase, a homodimer, and algal prolyl 4-hydroxylase, a monomer, do not contain detectable protein disulphide-isomerase activity. Since the hydroxylase reaction mechanisms are similar, the data suggest that the protein disulphide-isomerase activity of the vertebrate prolyl

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20

Arsenault, Patrick R., Katherine J. Heaton-Johnson, Lin-sheng Li, et al. "Identification of prolyl hydroxylation modifications in mammalian cell proteins." PROTEOMICS 15, no. 7 (2015): 1259–67. http://dx.doi.org/10.1002/pmic.201400398.

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21

Núñez-O’Mara, Analía, and Edurne Berra. "Deciphering the emerging role of SUMO conjugation in the hypoxia-signaling cascade." Biological Chemistry 394, no. 4 (2013): 459–69. http://dx.doi.org/10.1515/hsz-2012-0319.

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Abstract By driving the primary transcriptional response, the hypoxia inducible factor (HIF) is a master player of the hypoxia-signaling cascade, activation of which is essential to maintain oxygen homeostasis. HIF is formed by the interaction of a constitutive HIF-1β subunit with a HIF-α subunit tightly regulated through the concerted action of the prolyl hydroxylase domain containing proteins (PHDs) and factor inhibiting HIF. In well-oxygenated cells, HIF-α prolyl-hydroxylation by PHDs is the recognition signal for the binding of the ubiquitin E3 ligase pVHL, allowing protein poly-ubiquitina

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22

Loenarz, Christoph, Rasheduzzaman Chowdhury, Christopher J. Schofield, and Emily Flashman. "Oxygenases for oxygen sensing." Pure and Applied Chemistry 80, no. 8 (2008): 1837–47. http://dx.doi.org/10.1351/pac200880081837.

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In animals, cellular and physiological responses to oxygen level variations are regulated via the post-translational modification of the heterodimeric hypoxia-inducible transcription factor (HIF). Hydroxylation of the HIF-α subunit at either of two conserved prolyl residues enables binding to the von Hippel-Lindau protein (pVHL) elongin C/B complex (VCB) which targets HIF-α for degradation via the ubiquitin proteasome pathway. Hydroxylation of an asparaginyl residue in the C-terminal transcriptional activation domain of HIF-α reduces its interaction with the transcriptional coactivator p300. T

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23

Homan, Erica P., Caressa Lietman, Ingo Grafe, et al. "Differential Effects of Collagen Prolyl 3-Hydroxylation on Skeletal Tissues." PLoS Genetics 10, no. 1 (2014): e1004121. http://dx.doi.org/10.1371/journal.pgen.1004121.

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Pokidysheva, E., S. Boudko, J. Vranka, et al. "Biological role of prolyl 3-hydroxylation in type IV collagen." Proceedings of the National Academy of Sciences 111, no. 1 (2013): 161–66. http://dx.doi.org/10.1073/pnas.1307597111.

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Martin, Falk, Tobias Linden, Dörthe M. Katschinski, et al. "Copper-dependent activation of hypoxia-inducible factor (HIF)-1: implications for ceruloplasmin regulation." Blood 105, no. 12 (2005): 4613–19. http://dx.doi.org/10.1182/blood-2004-10-3980.

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Abstract Cellular oxygen partial pressure is sensed by a family of prolyl-4-hydroxylase domain (PHD) enzymes that modify hypoxia-inducible factor (HIF)α subunits. Upon hydroxylation under normoxic conditions, HIFα is bound by the von Hippel-Lindau tumor suppressor protein and targeted for proteasomal destruction. Since PHD activity is dependent on oxygen and ferrous iron, HIF-1 mediates not only oxygen- but also iron-regulated transcriptional gene expression. Here we show that copper (CuCl2) stabilizes nuclear HIF-1α under normoxic conditions, resulting in hypoxia-response element (HRE)-depend

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Yan, Qin, Steven Bartz, Mao Mao, Lianjie Li та William G. Kaelin. "The Hypoxia-Inducible Factor 2α N-Terminal and C-Terminal Transactivation Domains Cooperate To Promote Renal Tumorigenesis In Vivo". Molecular and Cellular Biology 27, № 6 (2007): 2092–102. http://dx.doi.org/10.1128/mcb.01514-06.

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ABSTRACT Hypoxia-inducible factor (HIF) is a heterodimeric transcription factor, consisting of an alpha subunit and a beta subunit, that controls cellular responses to hypoxia. HIFα contains two transcriptional activation domains called the N-terminal transactivation domain (NTAD) and the C-terminal transactivation domain (CTAD). HIFα is destabilized by prolyl hydroxylation catalyzed by EglN family members. In addition, CTAD function is inhibited by asparagine hydroxylation catalyzed by FIH1. Both hydroxylation reactions are linked to oxygen availability. The von Hippel-Lindau tumor suppressor

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Jiang, Wei, Xiaoyan Zhou, Zengxia Li, et al. "Prolyl 4-hydroxylase 2 promotes B-cell lymphoma progression via hydroxylation of Carabin." Blood 131, no. 12 (2018): 1325–36. http://dx.doi.org/10.1182/blood-2017-07-794875.

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Key Points P4HA2, associated with progression and poor overall survival in DLBCL patients, could serve as a novel biomarker and therapeutic target. P4HA2 counteracts the negative effect of Carabin on lymphoma by hydroxylation of Carabin at Pro306.

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Strowitzki, Moritz, Eoin Cummins, and Cormac Taylor. "Protein Hydroxylation by Hypoxia-Inducible Factor (HIF) Hydroxylases: Unique or Ubiquitous?" Cells 8, no. 5 (2019): 384. http://dx.doi.org/10.3390/cells8050384.

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All metazoans that utilize molecular oxygen (O2) for metabolic purposes have the capacity to adapt to hypoxia, the condition that arises when O2 demand exceeds supply. This is mediated through activation of the hypoxia-inducible factor (HIF) pathway. At physiological oxygen levels (normoxia), HIF-prolyl hydroxylases (PHDs) hydroxylate proline residues on HIF-α subunits leading to their destabilization by promoting ubiquitination by the von-Hippel Lindau (VHL) ubiquitin ligase and subsequent proteasomal degradation. HIF-α transactivation is also repressed in an O2-dependent way due to asparagin

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Asada, Shinichi, Takaki Koide, Hiroyuki Yasui, and Kazuhiro Nagata. "Effect of HSP47 on Prolyl 4-Hydroxylation of Collagen Model Peptides." Cell Structure and Function 24, no. 4 (1999): 187–96. http://dx.doi.org/10.1247/csf.24.187.

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ELEFTHERIADES, E., A. FERGUSON, M. SPRAGIA, and A. SAMAREL. "Prolyl hydroxylation regulates intracellular procollagen degradation in cultured rat cardiac fibroblasts." Journal of Molecular and Cellular Cardiology 27, no. 8 (1995): 1459–73. http://dx.doi.org/10.1016/s0022-2828(95)90095-0.

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31

Chan, Denise A., Patrick D. Sutphin, Nicholas C. Denko та Amato J. Giaccia. "Role of Prolyl Hydroxylation in Oncogenically Stabilized Hypoxia-inducible Factor-1α". Journal of Biological Chemistry 277, № 42 (2002): 40112–17. http://dx.doi.org/10.1074/jbc.m206922200.

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Serra-Pérez, Anna, Anna M. Planas, Analía Núñez-O'Mara та ін. "Extended Ischemia Prevents HIF1α Degradation at Reoxygenation by Impairing Prolyl-hydroxylation". Journal of Biological Chemistry 285, № 24 (2010): 18217–24. http://dx.doi.org/10.1074/jbc.m110.101048.

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MARXSEN, Jan H., Petra STENGEL, Kathrin DOEGE та ін. "Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-α-prolyl-4-hydroxylases". Biochemical Journal 381, № 3 (2004): 761–67. http://dx.doi.org/10.1042/bj20040620.

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An important regulator involved in oxygen-dependent gene expression is the transcription factor HIF (hypoxia-inducible factor), which is composed of an oxygen-sensitive α-subunit (HIF-1α or HIF-2α) and a constitutively expressed β-subunit. In normoxia, HIF-1α is destabilized by post-translational hydroxylation of Pro-564 and Pro-402 by a family of oxygen-sensitive dioxygenases. The three HIF-modifying human enzymes have been termed prolyl hydroxylase domain containing proteins (PHD1, PHD2 and PHD3). Prolyl hydroxylation leads to pVHL (von-Hippel-Lindau protein)-dependent ubiquitination and rap

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Baader, E., G. Tschank, K. H. Baringhaus, H. Burghard, and V. Günzler. "Inhibition of prolyl 4-hydroxylase by oxalyl amino acid derivatives in vitro, in isolated microsomes and in embryonic chicken tissues." Biochemical Journal 300, no. 2 (1994): 525–30. http://dx.doi.org/10.1042/bj3000525.

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The potency of oxalyl amino acid derivatives as inhibitors of prolyl 4-hydroxylase was studied in vitro, in isolated microsomes and in chicken embryonic-tissue culture. These compounds represent structural analogues of 2-oxoglutarate in which the -CH2- moiety at C-3 is replaced by -NH-, with or without further structural modifications. The most efficient inhibitor of purified prolyl 4-hydroxylase was oxalylglycine. Its mode of inhibition was competitive with respect to 2-oxoglutarate. The Ki value varied between 1.9 and 7.8 microM, depending on the variable substrate used. Oxalylalanine inhibi

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Chang, Weizhong, Aileen M. Barnes, Wayne A. Cabral, Joann N. Bodurtha, and Joan C. Marini. "Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex." Human Molecular Genetics 19, no. 2 (2009): 223–34. http://dx.doi.org/10.1093/hmg/ddp481.

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Shi, Run, Shanshan Gao, Jie Zhang, et al. "Collagen prolyl 4-hydroxylases modify tumor progression." Acta Biochimica et Biophysica Sinica 53, no. 7 (2021): 805–14. http://dx.doi.org/10.1093/abbs/gmab065.

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Abstract Collagen is the main component of the extracellular matrix. Hydroxylation of proline residues on collagen, catalyzed by collagen prolyl 4-hydroxylase (C-P4H), is essential for the stability of the collagen triple helix. Vertebrate C-P4H is an α2β2 tetramer with three isoenzymes differing in the catalytic α-subunits, which are encoded by P4HA1, P4HA2, and P4HA3 genes. In contrast, β-subunit is encoded by a single gene P4HB. The expressions of P4HAs and P4HB are regulated by multiple cellular factors, including cytokines, transcription factors, and microRNAs. P4HAs and P4HB are highly e

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Joyce, Paul B. M., and Warwick Kimmins. "Prolyl-4-hydroxylase activity in excised elongating and nonelongating regions of bean hypocotyl." Canadian Journal of Botany 64, no. 8 (1986): 1594–98. http://dx.doi.org/10.1139/b86-214.

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Apical (elongating) and basal (nonelongating) segments of bean hypocotyls were labelled with [4-3H] proline and in vivo prolyl-4-hydroxylase activity, and peptidyl proline synthesis and hydroxylation were determined. Prolyl-4-hydroxylase activity was negligible in newly excised segments. However, if segments were aerated before labelling, hydroxylase activity, uptake, and incorporation of [4-3H]proline were all significantly increased. 3H loss was negligible in the presence of α, α′-dipyridyl or when sections were labelled with [2,3-3H]proline. In basal sections aerated for 24 h, prolyl-4-hydr

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Minamishima, Yoji Andrew, Javid Moslehi, Robert F. Padera, Roderick T. Bronson, Ronglih Liao, and William G. Kaelin. "A Feedback Loop Involving the Phd3 Prolyl Hydroxylase Tunes the Mammalian Hypoxic Response In Vivo." Molecular and Cellular Biology 29, no. 21 (2009): 5729–41. http://dx.doi.org/10.1128/mcb.00331-09.

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ABSTRACT Hypoxia-inducible factor (HIF), consisting of a labile α subunit and a stable β subunit, is a master regulator of hypoxia-responsive mRNAs. HIFα undergoes oxygen-dependent prolyl hydroxylation, which marks it for polyubiquitination by a complex containing the von Hippel-Lindau protein (pVHL). Among the three Phd family members, Phd2 appears to be the primary HIF prolyl hydroxylase. Phd3 is induced by HIF and, based on findings from in vitro studies, may participate in a HIF-regulatory feedback loop. Here, we report that Phd3 loss exacerbates the HIF activation, hepatic steatosis, dila

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Nytko, Katarzyna J., Nobuyo Maeda, Philipp Schläfli, Patrick Spielmann, Roland H. Wenger, and Daniel P. Stiehl. "Vitamin C is dispensable for oxygen sensing in vivo." Blood 117, no. 20 (2011): 5485–93. http://dx.doi.org/10.1182/blood-2010-09-307637.

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Abstract Prolyl-4-hydroxylation is necessary for proper structural assembly of collagens and oxygen-dependent protein stability of hypoxia-inducible transcription factors (HIFs). In vitro function of HIF prolyl-4-hydroxylase domain (PHD) enzymes requires oxygen and 2-oxoglutarate as cosubstrates with iron(II) and vitamin C serving as cofactors. Although vitamin C deficiency is known to cause the collagen-disassembly disease scurvy, it is unclear whether cellular oxygen sensing is similarly affected. Here, we report that vitamin C–deprived Gulo−/− knockout mice show normal HIF-dependent gene ex

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Pagé, Elisabeth L., Denise A. Chan, Amato J. Giaccia, Mark Levine та Darren E. Richard. "Hypoxia-inducible Factor-1α Stabilization in Nonhypoxic Conditions: Role of Oxidation and Intracellular Ascorbate Depletion". Molecular Biology of the Cell 19, № 1 (2008): 86–94. http://dx.doi.org/10.1091/mbc.e07-06-0612.

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Hypoxia-inducible factor-1 (HIF-1) is a decisive element for the transcriptional regulation of many genes induced under low oxygen conditions. Under normal oxygen conditions, HIF-1α, the active subunit of HIF-1, is hydroxylated on proline residues by specific HIF prolyl-hydroxylases, leading to ubiquitination and degradation by the proteasome. In hypoxia, hydroxylation and ubiquitination are blocked and HIF-1α accumulates in cells. Recent studies have shown that in normal oxygen conditions G-protein–coupled receptor agonists, including angiotensin (Ang) II and thrombin, potently induce and act

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Lando, David, Jeffrey J. Gorman, Murray L. Whitelaw, and Daniel J. Peet. "Oxygen-dependent regulation of hypoxia-inducible factors by prolyl and asparaginyl hydroxylation." European Journal of Biochemistry 270, no. 5 (2003): 781–90. http://dx.doi.org/10.1046/j.1432-1033.2003.03445.x.

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Torpe, Nanna, and Roger Pocock. "Regulation of Axonal Midline Guidance by Prolyl 4-Hydroxylation in Caenorhabditis elegans." Journal of Neuroscience 34, no. 49 (2014): 16348–57. http://dx.doi.org/10.1523/jneurosci.1322-14.2014.

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Mikhaylova, Olga, Monika L. Ignacak, Teresa J. Barankiewicz, et al. "The von Hippel-Lindau Tumor Suppressor Protein and Egl-9-Type Proline Hydroxylases Regulate the Large Subunit of RNA Polymerase II in Response to Oxidative Stress." Molecular and Cellular Biology 28, no. 8 (2008): 2701–17. http://dx.doi.org/10.1128/mcb.01231-07.

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ABSTRACT Human renal clear cell carcinoma (RCC) is frequently associated with loss of the von Hippel-Lindau (VHL) tumor suppressor (pVHL), which inhibits ubiquitylation and degradation of the alpha subunits of hypoxia-inducible transcription factor. pVHL also ubiquitylates the large subunit of RNA polymerase II, Rpb1, phosphorylated on serine 5 (Ser5) within the C-terminal domain (CTD). A hydroxylated proline 1465 within an LXXLAP motif located N-terminal to the CTD allows the interaction of Rpb1 with pVHL. Here we report that in RCC cells, pVHL regulates expression of Rpb1 and is necessary fo

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VEIJOLA, Johanna, Pia ANNUNEN, Peppi KOIVUNEN, Antony P. PAGE, Taina PIHLAJANIEMI та Kari I. KIVIRIKKO. "Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their β subunit". Biochemical Journal 317, № 3 (1996): 721–29. http://dx.doi.org/10.1042/bj3170721.

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Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the β subunit of prolyl 4-hydroxylases. We report here on the cloning and expression of the Caenorhabditis elegans PDI/β polypeptide and its isoform. The overall amino acid sequence identity and similarity between the processed human and C. elegans PDI/β polypeptides are 61% and 85% respectively, and those between the C. elegans PDI/β polypeptide and the PDI isoform 46% and 73%. The isoform differs from the PDI/β and ERp60 polypeptides in that its N-terminal thioredoxin-like domain has an unusu

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Boulahbel, Houda, Raúl V. Durán, and Eyal Gottlieb. "Prolyl hydroxylases as regulators of cell metabolism." Biochemical Society Transactions 37, no. 1 (2009): 291–94. http://dx.doi.org/10.1042/bst0370291.

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Cellular response to oxygen depletion is mediated by HIF (hypoxia-inducible factor). HIF is a heterodimer consisting of a constitutively expressed subunit (HIFβ) and an oxygen-regulated subunit (HIFα). HIFα stability is regulated by prolyl hydroxylation by PHD (prolyl hydroxylase domain-containing protein) family members. PHD activity depends on the availability of molecular oxygen, making PHDs the oxygen-sensing system in animal cells. However, PHDs have recently been shown to respond to stimuli other than oxygen, such as 2-oxoglutarate (α-ketoglutarate), succinate or fumarate, as illustrated

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Hudson, David M., and David R. Eyre. "Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification?" Connective Tissue Research 54, no. 4-5 (2013): 245–51. http://dx.doi.org/10.3109/03008207.2013.800867.

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Hiwatashi, Yusuke, Kohei Kanno, Chikahisa Takasaki, et al. "PHD1 interacts with ATF4 and negatively regulates its transcriptional activity without prolyl hydroxylation." Experimental Cell Research 317, no. 20 (2011): 2789–99. http://dx.doi.org/10.1016/j.yexcr.2011.09.005.

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Scotti, John S., Ivanhoe K. H. Leung, Wei Ge, et al. "Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation." Proceedings of the National Academy of Sciences 111, no. 37 (2014): 13331–36. http://dx.doi.org/10.1073/pnas.1409916111.

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Kageyama, Yukio, Minori Koshiji, Kenneth K. W. To, Ya‐Min Tian, Peter J. Ratcliffe та L. Eric Huang. "Leu‐574 of human HIF‐1α is a molecular determinant of prolyl hydroxylation". FASEB Journal 18, № 9 (2004): 1028–30. http://dx.doi.org/10.1096/fj.03-1233fje.

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Taga, Yuki, Masashi Kusubata, Kiyoko Ogawa-Goto, and Shunji Hattori. "Developmental Stage-dependent Regulation of Prolyl 3-Hydroxylation in Tendon Type I Collagen." Journal of Biological Chemistry 291, no. 2 (2015): 837–47. http://dx.doi.org/10.1074/jbc.m115.686105.

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