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Volumn 17, Issue 3, 2013, Pages 429-435

Presence of N-glycosylated transthyretin in plasma of V30M carriers in familial amyloidotic polyneuropathy: An escape from ERAD

Author keywords

ERAD; N glycosylation; Transthyretin

Indexed keywords

GLYCOPEPTIDASE; MONOCLONAL ANTIBODY; PREALBUMIN;

EID: 84875784710     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/jcmm.12024     Document Type: Article
Times cited : (14)

References (19)
  • 1
    • 84860663436 scopus 로고    scopus 로고
    • Transthyretin deposition in familial amyloidotic polyneuropathy
    • Saraiva MJ, Magalhães J, Ferreira N, et al. Transthyretin deposition in familial amyloidotic polyneuropathy. Curr Med Chem. 2012; 19: 2304-11.
    • (2012) Curr Med Chem , vol.19 , pp. 2304-2311
    • Saraiva, M.J.1    Magalhães, J.2    Ferreira, N.3
  • 2
    • 0020524650 scopus 로고
    • Studies on plasma transthyretin (prealbumin) in familial amyloidotic polyneuropathy, Portuguese type
    • Saraiva MJM, Costa PP, Goodman DS. Studies on plasma transthyretin (prealbumin) in familial amyloidotic polyneuropathy, Portuguese type. J Lab Clin Med. 1983; 102: 590-603.
    • (1983) J Lab Clin Med , vol.102 , pp. 590-603
    • Saraiva, M.J.M.1    Costa, P.P.2    Goodman, D.S.3
  • 3
    • 0032544408 scopus 로고    scopus 로고
    • The crystal structure of amyloidogenic Leu55 -> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
    • Sebastião MP, Saraiva MJ, Damas AM. The crystal structure of amyloidogenic Leu55 -> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils. J Biol Chem. 1998; 273: 24715-22.
    • (1998) J Biol Chem , vol.273 , pp. 24715-24722
    • Sebastião, M.P.1    Saraiva, M.J.2    Damas, A.M.3
  • 4
    • 0034405428 scopus 로고    scopus 로고
    • Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils
    • Redondo C, Damas AM, Olofsson A, et al. Search for intermediate structures in transthyretin fibrillogenesis: soluble tetrameric Tyr78Phe TTR expresses a specific epitope present only in amyloid fibrils. J Mol Biol. 2000; 304: 461-70.
    • (2000) J Mol Biol , vol.304 , pp. 461-470
    • Redondo, C.1    Damas, A.M.2    Olofsson, A.3
  • 5
    • 0037366670 scopus 로고    scopus 로고
    • A transthyretin mutation (Tyr78Phe) associated with peripheral neuropathy, carpal tunnel syndrome and skin amyloidosis
    • Magy N, Liepnieks JJ, Gil H, et al. A transthyretin mutation (Tyr78Phe) associated with peripheral neuropathy, carpal tunnel syndrome and skin amyloidosis. Amyloid. 2003; 10: 29-33.
    • (2003) Amyloid , vol.10 , pp. 29-33
    • Magy, N.1    Liepnieks, J.J.2    Gil, H.3
  • 6
    • 0033053678 scopus 로고    scopus 로고
    • Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants, Proc
    • Goldsteins G, Persson H, Andersson K, et al. Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants, Proc. Natl. Acad. Sci. USA. 1999; 96: 3108-13.
    • (1999) Natl. Acad. Sci. USA , vol.96 , pp. 3108-3113
    • Goldsteins, G.1    Persson, H.2    Andersson, K.3
  • 7
    • 0034465430 scopus 로고    scopus 로고
    • Antibody recognition of amyloidogenic transthyretin variants in serum of patients with familial amyloidotic polyneuropathy
    • Palha JA, Moreira P, Olofsson A, et al. Antibody recognition of amyloidogenic transthyretin variants in serum of patients with familial amyloidotic polyneuropathy. J Mol Med. 2001; 78: 703-7.
    • (2001) J Mol Med , vol.78 , pp. 703-707
    • Palha, J.A.1    Moreira, P.2    Olofsson, A.3
  • 8
    • 0030971508 scopus 로고    scopus 로고
    • Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy
    • Kohno K, Palha JA, Miyakawa K, et al. Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy. Am J Pathol. 1997; 150: 1497-508.
    • (1997) Am J Pathol , vol.150 , pp. 1497-1508
    • Kohno, K.1    Palha, J.A.2    Miyakawa, K.3
  • 9
    • 0027512354 scopus 로고
    • Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone
    • Episkopou V, Maeda S, Nishiguchi S, et al. Disruption of the transthyretin gene results in mice with depressed levels of plasma retinol and thyroid hormone. Proc Natl Acad Sci USA. 1993; 90: 2375-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2375-2379
    • Episkopou, V.1    Maeda, S.2    Nishiguchi, S.3
  • 10
    • 0030885583 scopus 로고    scopus 로고
    • Thyroxine binding to transthyretin Met 119 - comparative studies of different heterozygotic carriers and structural analysis
    • Almeida MR, Damas AM, Lans MC, et al. Thyroxine binding to transthyretin Met 119 - comparative studies of different heterozygotic carriers and structural analysis. Endocrine. 1997; 6: 309-15.
    • (1997) Endocrine , vol.6 , pp. 309-315
    • Almeida, M.R.1    Damas, A.M.2    Lans, M.C.3
  • 11
    • 0028041578 scopus 로고
    • Determination of amyloid type by ELISA using milligram amounts of tissue
    • Kaplan B, German G, Ravid M, et al. Determination of amyloid type by ELISA using milligram amounts of tissue. Clin Chim Acta. 1994; 229: 171-9.
    • (1994) Clin Chim Acta , vol.229 , pp. 171-179
    • Kaplan, B.1    German, G.2    Ravid, M.3
  • 12
    • 0035958040 scopus 로고    scopus 로고
    • Internalization of transthyretin: evidence for a novel yet unidentified receptor-associated protein (RAP) - sensitive receptor
    • Sousa MM, Saraiva MJ. Internalization of transthyretin: evidence for a novel yet unidentified receptor-associated protein (RAP) - sensitive receptor. J Biol Chem. 2001; 276: 14420-5.
    • (2001) J Biol Chem , vol.276 , pp. 14420-14425
    • Sousa, M.M.1    Saraiva, M.J.2
  • 13
    • 0034651822 scopus 로고    scopus 로고
    • A new diagnostic procedure to detect unknown transthyretin (TTR) mutations in familial amyloidotic polyneuropathy (FAP)
    • Yamashita T, Ando Y, Suhr O, et al. A new diagnostic procedure to detect unknown transthyretin (TTR) mutations in familial amyloidotic polyneuropathy (FAP). J Neurol Sci. 2000; 173: 154-9.
    • (2000) J Neurol Sci , vol.173 , pp. 154-159
    • Yamashita, T.1    Ando, Y.2    Suhr, O.3
  • 14
    • 0030724162 scopus 로고    scopus 로고
    • Comparative stability and clearance of Met30 transthyretin and Met119 transthyretin
    • Alves IL, Hays MT, Saraiva MJM. Comparative stability and clearance of Met30 transthyretin and Met119 transthyretin. Eur J Biochem. 1997; 249: 662-8.
    • (1997) Eur J Biochem , vol.249 , pp. 662-668
    • Alves, I.L.1    Hays, M.T.2    Saraiva, M.J.M.3
  • 15
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima Y, Wiseman RL, Matteson J, et al. The biological and chemical basis for tissue-selective amyloid disease. Cell. 2005; 121: 73-85.
    • (2005) Cell , vol.121 , pp. 73-85
    • Sekijima, Y.1    Wiseman, R.L.2    Matteson, J.3
  • 16
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci USA. 1994; 91: 913-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 17
    • 24044487195 scopus 로고    scopus 로고
    • Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII
    • Bolt G, Kristensen C, Steenstrup TD. Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII. Glycobiology. 2005; 15: 541-7.
    • (2005) Glycobiology , vol.15 , pp. 541-547
    • Bolt, G.1    Kristensen, C.2    Steenstrup, T.D.3
  • 18
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada C, Kelleher DJ, Gilmore R. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell. 2009; 136: 272-83.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 19
    • 84863846134 scopus 로고    scopus 로고
    • STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein
    • Sato T, Sako Y, Sho M, et al. STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. Mol Cell. 2012; 47: 99-110.
    • (2012) Mol Cell , vol.47 , pp. 99-110
    • Sato, T.1    Sako, Y.2    Sho, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.