Glycosylation of voltage-gated calcium channels in health and disease

Biochimica et Biophysica Acta - Biomembranes

Volumn 1859, Issue 5, 2017, Pages 662-668

  Lazniewska, Joanna ^a   Weiss, Norbert ^a  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

Author keywords

Ancillary subunit; Calcium channels; Diabetes; N glycosylation; Neuropathic pain; Plasma membrane; Stability; Trafficking; Voltage gated calcium channels

Indexed keywords

CALCIUM CHANNEL L TYPE; CALCIUM CHANNEL T TYPE; CALCIUM ION; VOLTAGE GATED CALCIUM CHANNEL; CALCIUM CHANNEL; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; COMPLEX FORMATION; DISEASES; GLYCOSYLATION; HEALTH; HUMAN; NONHUMAN; PATHOGENESIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN SUBUNIT; PROTEIN SYNTHESIS; PROTEIN TARGETING; REVIEW; ANIMAL; EXPERIMENTAL DIABETES MELLITUS; METABOLISM;

ANIMALS; CALCIUM CHANNELS; DIABETES MELLITUS, EXPERIMENTAL; GLYCOSYLATION; HUMANS; PROTEIN SUBUNITS;

EID: 85012113504     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2017.01.018     Document Type: Review

References (98)

1. [1] Berridge, M.J., Bootman, M.D., Roderick, H.L., Calcium signalling: dynamics, homeostasis and remodelling. Nat. Rev. Mol. Cell Biol., 2003, 517–529.
2. [2] Catterall, W.A., Voltage-gated calcium channels. Cold Spring Harb. Perspect. Biol., 2011, a003947.
3. [3] Simms, B.A., Zamponi, G.W., Neuronal voltage-gated calcium channels: structure, function, and dysfunction. Neuron, 2014, 24–45.
4. [4] Arikkath, J., Campbell, K.P., Auxiliary subunits: essential components of the voltage-gated calcium channel complex. Curr. Opin. Neurobiol., 2003, 298–307.
5. [5] Leuranguer, V., Bourinet, E., Lory, P., Nargeot, J., Antisense depletion of beta-subunits fails to affect T-type calcium channels properties in a neuroblastoma cell line. Neuropharmacology, 1998, 701–708.
6. [6] Dubel, S.J., Altier, C., Chaumont, S., Lory, P., Bourinet, E., Nargeot, J., Plasma membrane expression of T-type calcium channel alpha(1) subunits is modulated by high voltage-activated auxiliary subunits. J. Biol. Chem., 2004, 29263–29269.
7. [7] Bae, J., Suh, E.J., Lee, C., Interaction of T-type calcium channel Ca(V)3.3 with the β-subunit. Mol. Cell, 2010, 185–191.
8. 2 + channels by calmodulin. Sci. STKE, 2006, er1.
9. [9] Weiss, N., Zamponi, G.W., Regulation of voltage-gated calcium channels by synaptic proteins. Adv. Exp. Med. Biol., 2012, 759–775.
10. [10] Proft, J., Weiss, N., G protein regulation of neuronal calcium channels: back to the future. Mol. Pharmacol., 2015, 890–906.
11. [11] Huang, J., Zamponi, G.W., Regulation of voltage gated calcium channels by GPCRs and post-translational modification. Curr. Opin. Pharmacol., 2016, 1–8.
12. [12] Blesneac, I., Chemin, J., Bidaud, I., Huc-Brandt, S., Vandermoere, F., Lory, P., Phosphorylation of the Cav3.2 T-type calcium channel directly regulates its gating properties. Proc. Natl. Acad. Sci. U. S. A., 2015, 13705–13710.
13. 2 + channels. Am. J. Physiol. Cell Physiol., 2016, C773–C779.
14. 2 + channel from the β2 adrenergic receptor. EMBO J., 2016, 1330–1345.
15. 2 + channels. Channels (Austin), 2007, 102–112.
16. [16] Altier, C., Garcia-Caballero, A., Simms, B., You, H., Chen, L., Walcher, J., Tedford, H.W., Hermosilla, T., Zamponi, G.W., The Cavβ subunit prevents RFP2-mediated ubiquitination and proteasomal degradation of L-type channels. Nat. Neurosci., 2011, 173–180.
17. [17] García-Caballero, A., Gadotti, V.M., Stemkowski, P., Weiss, N., Souza, I.A., Hodgkinson, V., Bladen, C., Chen, L., Hamid, J., Pizzoccaro, A., Deage, M., François, A., Bourinet, E., Zamponi, G.W., The deubiquitinating enzyme USP5 modulates neuropathic and inflammatory pain by enhancing Cav3.2 channel activity. Neuron, 2014, 1144–1158.
18. [18] Waithe, D., Ferron, L., Page, K.M., Chaggar, K., Dolphin, A.C., Beta-subunits promote the expression of Ca(V)2.2 channels by reducing their proteasomal degradation. J. Biol. Chem., 2011, 9598–9611.
19. [19] Page, K.M., Rothwell, S.W., Dolphin, A.C., The CaVβ subunit protects the I-II loop of the voltage-gated calcium channel CaV2.2 from proteasomal degradation but not oligoubiquitination. J. Biol. Chem., 2016, 20402–20416.
20. 2 + channels and potential pathophysiological implications. Gen. Physiol. Biophys., 2016.
21. [21] Chien, A.J., Carr, K.M., Shirokov, R.E., Rios, E., Hosey, M.M., Identification of palmitoylation sites within the L-type calcium channel beta2a subunit and effects on channel function. J. Biol. Chem., 1996, 26465–26468.
22. 2 + channel inactivation. Proc. Natl. Acad. Sci. U. S. A., 2000, 9293–9298.
23. [23] Lazniewska, J., Weiss, N., The “sweet” side of ion channels. Rev. Physiol. Biochem. Pharmacol., 2014, 67–114.
24. [24] Schwarz, F., Aebi, M., Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol., 2011, 576–582.
25. [25] Gavel, Y., von Heijne, G., Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/ser acceptor sites: implications for protein engineering. Protein Eng., 1990, 433–442.
26. [26] Rao, R.S., Bernd, W., Do N-glycoproteins have preference for specific sequons. Bioinformation, 2010, 208–212.
27. [27] Aebi, M., N-linked protein glycosylation in the ER. Biochim. Biophys. Acta, 2013, 2430–2437.
28. [28] Caramelo, J.J., Parodi, A.J., Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem., 2008, 10221–10225.
29. [29] Wang, Q., Groenendyk, J., Michalak, M., Glycoprotein quality control and endoplasmic reticulum stress. Molecules, 2015, 13689–13704.
30. [30] Stanley, P., Golgi glycosylation. Cold Spring Harb. Perspect. Biol., 2011.
31. [31] Fisher, P., Ungar, D., Bridging the gap between glycosylation and vesicle traffic. Front. Cell Dev. Biol., 15, 2016.
32. [32] Sano, M., Korekane, H., Ohtsubo, K., Yamaguchi, Y., Kato, M., Shibukawa, Y., Tajiri, M., Adachi, H., Wada, Y., Asahi, M., Taniguchi, N., N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability. Glycobiology, 2012, 714–724.
33. [33] Vagin, O., Kraut, J.A., Sachs, G., Role of N-glycosylation in trafficking of apical membrane proteins in epithelia. Am. J. Physiol. Ren. Physiol., 2009, F459–F469.
34. [34] Ferris, S.P., Kodali, V.K., Kaufman, R.J., Glycoprotein folding and quality-control mechanisms in protein-folding diseases. Dis. Model. Mech., 2014, 331–341.
35. [35] Moremen, K.W., Tiemeyer, M., Nairn, A.V., Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol., 2012, 448–462.
36. [36] Wang, M.C., Collins, R.F., Ford, R.C., Berrow, N.S., Dolphin, A.C., Kitmitto, A., The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: comparison with the skeletal muscle form reveals a common architectural motif. J. Biol. Chem., 2004, 7159–7168.
37. 2 + channel. J. Microbiol. Biotechnol., 2015, 1371–1379.
38. [38] Yunker, A.M., Sharp, A.H., Sundarraj, S., Ranganathan, V., Copeland, T.D., McEnery, M.W., Immunological characterization of T-type voltage-dependent calcium channel CaV3.1 (alpha 1G) and CaV3.3 (alpha 1I) isoforms reveal differences in their localization, expression, and neural development. Neuroscience, 2003, 321–335.
39. [39] Chen, Y., Sharp, A.H., Hata, K., Yunker, A.M., Polo-Parada, L., Landmesser, L.T., McEnery, M.W., Site-directed antibodies to low-voltage-activated calcium channel CaV3.3 (alpha1I) subunit also target neural cell adhesion molecule-180. Neuroscience, 2007, 981–996.
40. [40] Weiss, N., Zamponi, G.W., Stephens, G., Mochida, S., (eds.) Modulation of Presynaptic Calcium Channels, 2013, Springer, 61–78.
41. [41] Orestes, P., Osuru, H.P., McIntire, W.E., Jacus, M.O., Salajegheh, R., Jagodic, M.M., Choe, W., Lee, J., Lee, S.S., Rose, K.E., Poiro, N., Digruccio, M.R., Krishnan, K., Covey, D.F., Lee, J.H., Barrett, P.Q., Jevtovic-Todorovic, V., Todorovic, S.M., Reversal of neuropathic pain in diabetes by targeting glycosylation of Ca(V)3.2 T-type calcium channels. Diabetes, 2013, 3828–3838.
42. [42] Weiss, N., Black, S.A., Bladen, C., Chen, L., Zamponi, G.W., Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation. Pflugers Arch., 2013, 1159–1170.
43. [43] Lazniewska, J., Rzhepetskyy, Y., Zhang, F.X., Zamponi, G.W., Weiss, N., Cooperative roles of glucose and asparagine-linked glycosylation in T-type calcium channel expression. Pflugers Arch., 2016, 1837–1851.
44. [44] Ondacova, K., Karmazinova, M., Lazniewska, J., Weiss, N., Lacinova, L., Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation. Channels (Austin), 2016, 175–184.
45. [45] Voisin, T., Bourinet, E., Lory, P., Genetic alteration of the metal/redox modulation of Cav3.2 T-type calcium channel reveals its role in neuronal excitability. J. Physiol., 2016, 3561–3574.
46. [46] Kang, H.W., Park, J.Y., Jeong, S.W., Kim, J.A., Moon, H.J., Perez-Reyes, E., Lee, J.H., A molecular determinant of nickel inhibition in Cav3.2 T-type calcium channels. J. Biol. Chem., 2006, 4823–4830.
47. [47] Nelson, M.T., Joksovic, P.M., Su, P., Kang, H.W., Van Deusen, A., Baumgart, J.P., David, L.S., Snutch, T.P., Barrett, P.Q., Lee, J.H., Zorumski, C.F., Perez-Reyes, E., Todorovic, S.M., Molecular mechanisms of subtype-specific inhibition of neuronal T-type calcium channels by ascorbate. J. Neurosci., 2007, 12577–12583.
48. [48] Takahashi, M., Seagar, M.J., Jones, J.F., Reber, B.F., Catterall, W.A., Subunit structure of dihydropyridine-sensitive calcium channels from skeletal muscle. Proc. Natl. Acad. Sci. U. S. A., 1987, 5478–5482.
49. [49] Dolphin, A.C., Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond. Nat. Rev. Neurosci., 2012, 542–555.
50. [50] Geisler, S., Schöpf, C.L., Obermair, G.J., Emerging evidence for specific neuronal functions of auxiliary calcium channel α₂δ subunits. Gen. Physiol. Biophys., 2015, 105–118.
51. [51] Davies, A., Kadurin, I., Alvarez-Laviada, A., Douglas, L., Nieto-Rostro, M., Bauer, C.S., Pratt, W.S., Dolphin, A.C., The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function. Proc. Natl. Acad. Sci. U. S. A., 2010, 1654–1659.
52. [52] Marais, E., Klugbauer, N., Hofmann, F., Calcium channel alpha(2)delta subunits-structure and gabapentin binding. Mol. Pharmacol., 2001, 1243–1248.
53. 2 + channel alpha 2 delta subunit in current stimulation and subunit interaction. Neuron, 1996, 431–440.
54. 2 + channels. FEBS Lett., 2004, 21–26.
55. [55] Andrade, A., Sandoval, A., González-Ramírez, R., Lipscombe, D., Campbell, K.P., Felix, R., The alpha(2)delta subunit augments functional expression and modifies the pharmacology of Ca(V)1.3 L-type channels. Cell Calcium, 2009, 282–292.
56. [56] Tétreault, M.P., Bourdin, B., Briot, J., Segura, E., Lesage, S., Fiset, C., Parent, L., Identification of glycosylation sites essential for surface expression of the CaVα2δ1 subunit and modulation of the cardiac CaV1.2 channel activity. J. Biol. Chem., 2016, 4826–4843.
57. [57] Lazniewska, J., Weiss, N., Glycosylation of α2δ1 subunit: a sweet talk with Cav1.2 channels. Gen. Physiol. Biophys., 2016, 239–242.
58. 2 + channel alpha2delta and alpha1 subunits. J. Biol. Chem., 1997, 18508–18512.
59. [59] Wu, J., Yan, Z., Li, Z., Yan, C., Lu, S., Dong, M., Yan, N., Structure of the voltage-gated calcium channel Cav1.1 complex. Science, 2015, aad2395.
60. [60] Field, M.J., Cox, P.J., Stott, E., Melrose, H., Offord, J., Su, T.Z., Bramwell, S., Corradini, L., England, S., Winks, J., Kinloch, R.A., Hendrich, J., Dolphin, A.C., Webb, T., Williams, D., Identification of the alpha2-delta-1 subunit of voltage-dependent calcium channels as a molecular target for pain mediating the analgesic actions of pregabalin. Proc. Natl. Acad. Sci. U. S. A., 2006, 17537–17542.
61. [61] Kang, M.G., Campbell, K.P., Gamma subunit of voltage-activated calcium channels. J. Biol. Chem., 2003, 21315–21318.
62. [62] Price, M.G., Davis, C.F., Deng, F., Burgess, D.L., The alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate receptor trafficking regulator “stargazin” is related to the claudin family of proteins by its ability to mediate cell-cell adhesion. J. Biol. Chem., 2005, 19711–19720.
63. [63] Sandoval, A., Andrade, A., Beedle, A.M., Campbell, K.P., Felix, R., Inhibition of recombinant N-type Ca(V) channels by the gamma 2 subunit involves unfolded protein response (UPR)-dependent and UPR-independent mechanisms. J. Neurosci., 2007, 3317–3327.
64. [64] Arikkath, J., Chen, C.C., Ahern, C., Allamand, V., Flanagan, J.D., Coronado, R., Gregg, R.G., Campbell, K.P., Gamma 1 subunit interactions within the skeletal muscle L-type voltage-gated calcium channels. J. Biol. Chem., 2003, 1212–1219.
65. [65] Angelova, A., Ulyanova, A., Shirokov, R., Gamma1 subunit renders Cav1. 2 channels dependent on cell cycle. Biophys. J., 2010, 694a.
66. [66] Baycin-Hizal, D., Gottschalk, A., Jacobson, E., Mai, S., Wolozny, D., Zhang, H., Krag, S.S., Betenbaugh, M.J., Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function. Biochem. Biophys. Res. Commun., 2014, 243–253.
67. [67] Weiss, N., Koschak, A., Pathologies of Calcium Channels. 2014.
68. [68] Zamponi, G.W., Striessnig, J., Koschak, A., Dolphin, A.C., The physiology, pathology, and pharmacology of voltage-gated calcium channels and their future therapeutic potential. Pharmacol. Rev., 2015, 821–870.
69. [69] Zamponi, G.W., Targeting voltage-gated calcium channels in neurological and psychiatric diseases. Nat. Rev. Drug Discov., 2016, 19–34.
70. [70] Dogrul, A., Gardell, L.R., Ossipov, M.H., Tulunay, F.C., Lai, J., Porreca, F., Reversal of experimental neuropathic pain by T-type calcium channel blockers. Pain, 2003, 159–168.
71. [71] Bourinet, E., Alloui, A., Monteil, A., Barrère, C., Couette, B., Poirot, O., Pages, A., McRory, J., Snutch, T.P., Eschalier, A., Nargeot, J., Silencing of the Cav3.2 T-type calcium channel gene in sensory neurons demonstrates its major role in nociception. EMBO J., 2005, 315–324.
72. [72] M'Dahoma, S., Gadotti, V.M., Zhang, F.X., Park, B., Nam, J.H., Onnis, V., Balboni, G., Lee, J.Y., Zamponi, G.W., Effect of the T-type channel blocker KYS-05090S in mouse models of acute and neuropathic pain. Pflugers Arch., 2015.
73. [73] Bourinet, E., Francois, A., Laffray, S., T-type calcium channels in neuropathic pain. Pain, 2016, S15–S22.
74. [74] Jacus, M.O., Uebele, V.N., Renger, J.J., Todorovic, S.M., Presynaptic Cav3.2 channels regulate excitatory neurotransmission in nociceptive dorsal horn neurons. J. Neurosci., 2012, 9374–9382.
75. [75] Weiss, N., Hameed, S., Fernández-Fernández, J.M., Fablet, K., Karmazinova, M., Poillot, C., Proft, J., Chen, L., Bidaud, I., Monteil, A., Huc-Brandt, S., Lacinova, L., Lory, P., Zamponi, G.W., De Waard, M., A Ca(v)3.2/syntaxin-1A signaling complex controls T-type channel activity and low-threshold exocytosis. J. Biol. Chem., 2012, 2810–2818.
76. [76] Weiss, N., Zamponi, G.W., Control of low-threshold exocytosis by T-type calcium channels. Biochim. Biophys. Acta, 2013, 1579–1586.
77. 2 + channels in primary sensory neurons in spinal nerve injury. Spine (Phila Pa 1976), 2013, 463–470.
78. [78] Watanabe, M., Ueda, T., Shibata, Y., Kumamoto, N., Shimada, S., Ugawa, S., Expression and regulation of Cav3.2 T-type calcium channels during inflammatory hyperalgesia in mouse dorsal root ganglion neurons. PLoS One, 2015, e0127572.
79. [79] Scanzi, J., Accarie, A., Muller, E., Pereira, B., Aissouni, Y., Goutte, M., Joubert-Zakeyh, J., Picard, E., Boudieu, L., Mallet, C., Gelot, A., Ardid, D., Carvalho, F.A., Dapoigny, M., Colonic overexpression of the T-type calcium channel Cav 3.2 in a mouse model of visceral hypersensitivity and in irritable bowel syndrome patients. Neurogastroenterol. Motil., 2016, 1632–1640.
80. [80] Jagodic, M.M., Pathirathna, S., Nelson, M.T., Mancuso, S., Joksovic, P.M., Rosenberg, E.R., Bayliss, D.A., Jevtovic-Todorovic, V., Todorovic, S.M., Cell-specific alterations of T-type calcium current in painful diabetic neuropathy enhance excitability of sensory neurons. J. Neurosci., 2007, 3305–3316.
81. [81] Messinger, R.B., Naik, A.K., Jagodic, M.M., Nelson, M.T., Lee, W.Y., Choe, W.J., Orestes, P., Latham, J.R., Todorovic, S.M., Jevtovic-Todorovic, V., In vivo silencing of the Ca(V)3.2 T-type calcium channels in sensory neurons alleviates hyperalgesia in rats with streptozocin-induced diabetic neuropathy. Pain, 2009, 184–195.
82. [82] Latham, J.R., Pathirathna, S., Jagodic, M.M., Choe, W.J., Levin, M.E., Nelson, M.T., Lee, W.Y., Krishnan, K., Covey, D.F., Todorovic, S.M., Jevtovic-Todorovic, V., Selective T-type calcium channel blockade alleviates hyperalgesia in Ob/Ob mice. Diabetes, 2009, 2656–2665.
83. [83] Jagodic, M.M., Pathirathna, S., Joksovic, P.M., Lee, W., Nelson, M.T., Naik, A.K., Su, P., Jevtovic-Todorovic, V., Todorovic, S.M., Upregulation of the T-type calcium current in small rat sensory neurons after chronic constrictive injury of the sciatic nerve. J. Neurophysiol., 2008, 3151–3156.
84. [84] Todorovic, S.M., Jevtovic-Todorovic, V., Neuropathic pain: role for presynaptic T-type channels in nociceptive signaling. Pflugers Arch., 2013, 921–927.
85. [85] Obradovic, A.L., Hwang, S.M., Scarpa, J., Hong, S.J., Todorovic, S.M., Jevtovic-Todorovic, V., CaV3.2 T-type calcium channels in peripheral sensory neurons are important for mibefradil-induced reversal of hyperalgesia and allodynia in rats with painful diabetic neuropathy. PLoS One, 2014, e91467.
86. 2 + channels in long-term diabetes determines increased excitability of a specific type of capsaicin-insensitive DRG neurons. Mol. Pain, 2015, 29.
87. [87] Todorovic, S.M., Jevtovic-Todorovic, V., Targeting of CaV3.2 T-type calcium channels in peripheral sensory neurons for the treatment of painful diabetic neuropathy. Pflugers Arch., 2014, 701–706.
88. [88] Aromolaran, K.A., Benzow, K.A., Cribbs, L.L., Koob, M.D., Piedras-Rentería, E.S., T-type current modulation by the actin-binding protein Kelch-like 1. Am. J. Physiol. Cell Physiol., 2010, C1353–C1362.
89. [89] Rzhepetskyy, Y., Lazniewska, J., Proft, J., Campiglio, M., Flucher, B.E., Weiss, N., A Cav3.2/Stac1 molecular complex controls T-type channel expression at the plasma membrane. Channels (Austin), 2016, 346–354.
90. [90] Liu, B., Spearman, M., Doering, J., Lattová, E., Perreault, H., Butler, M., The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody. J. Biotechnol., 2014, 17–27.
91. [91] Villacrés, C., Tayi, V.S., Lattová, E., Perreault, H., Butler, M., Low glucose depletes glycan precursors, reduces site occupancy and galactosylation of a monoclonal antibody in CHO cell culture. Biotechnol. J., 2015, 1051–1066.
92. [92] Tomlinson, D.R., Gardiner, N.J., Glucose neurotoxicity. Nat. Rev. Neurosci., 2008, 36–45.
93. [93] Rellier, N., Ruggiero-Lopez, D., Lecomte, M., Lagarde, M., Wiernsperger, N., In vitro and in vivo alterations of enzymatic glycosylation in diabetes. Life Sci., 1999, 1571–1583.
94. [94] Andrade, A., Hope, J., Allen, A., Yorgan, V., Lipscombe, D., Pan, J.Q., A rare schizophrenia risk variant of CACNA1I disrupts CaV3.3 channel activity. Sci. Rep., 2016, 34233.
95. [95] Zhu, J., Yan, J., Thornhill, W.B., N-glycosylation promotes the cell surface expression of Kv1.3 potassium channels. FEBS J., 2012, 2632–2644.
96. [96] Bar-On, H., Nesher, G., Teitelbaum, A., Ziv, E., Dolichol-mediated enhanced protein N-glycosylation in experimental diabetes—a possible additional deleterious effect of hyperglycemia. J. Diabetes Complicat., 1997, 236–242.
97. [97] Freeze, H.H., Ng, B.G., Golgi glycosylation and human inherited diseases. Cold Spring Harb. Perspect. Biol., 2011, a005371.
98. [98] Scott, K., Gadomski, T., Kozicz, T., Morava, E., Congenital disorders of glycosylation: new defects and still counting. J. Inherit. Metab. Dis., 2014, 609–617.