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Volumn 74, Issue 2, 2008, Pages 218-222

Leukocyte chemotactic factor 2: A novel renal amyloid protein

Author keywords

Amyloid; Kidney; Nephrotic syndrome

Indexed keywords

AMYLOID; AMYLOID PROTEIN; LEUKOCYTE CHEMOTACTIC FACTOR 2; MONOCLONAL ANTIBODY; PROTEIN SUBUNIT;

EID: 46249120706     PISSN: 00852538     EISSN: 15231755     Source Type: Journal    
DOI: 10.1038/ki.2008.152     Document Type: Article
Times cited : (131)

References (18)
  • 1
    • 46249113009 scopus 로고    scopus 로고
    • Benson MD. Amyloidosis. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B (eds). The Metabolic and Molecular Bases of Inherited Disease, 8th edn, (IV) Chapter 209, Part 22 Connective Tissue McGraw Hill Book Co.: New York, NY, 2001, pp 5345-5378.
    • Benson MD. Amyloidosis. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B (eds). The Metabolic and Molecular Bases of Inherited Disease, 8th edn, (Volume IV) Chapter 209, Part 22 Connective Tissue McGraw Hill Book Co.: New York, NY, 2001, pp 5345-5378.
  • 2
    • 0027465319 scopus 로고
    • Hereditary renal amyloidosis associated with a mutant fibrinogen α-chain
    • Benson MD, Liepnieks J, Uemichi T et al. Hereditary renal amyloidosis associated with a mutant fibrinogen α-chain. Nature Genet 1993; 3: 252-255.
    • (1993) Nature Genet , vol.3 , pp. 252-255
    • Benson, M.D.1    Liepnieks, J.2    Uemichi, T.3
  • 3
    • 0025006134 scopus 로고
    • A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy
    • Nichols WC, Gregg RE, Brewer HB et al. A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy. Genomics 1990; 8: 318-323.
    • (1990) Genomics , vol.8 , pp. 318-323
    • Nichols, W.C.1    Gregg, R.E.2    Brewer, H.B.3
  • 4
    • 0035868431 scopus 로고    scopus 로고
    • A new human hereditary amyloidosis: The result of a stop-codon mutation in the apolipoprotein AII gene
    • Benson MD, Liepnieks JJ, Yazaki M et al. A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene. Genomics 2001; 72: 272-277.
    • (2001) Genomics , vol.72 , pp. 272-277
    • Benson, M.D.1    Liepnieks, J.J.2    Yazaki, M.3
  • 5
    • 0027506498 scopus 로고
    • Human lysozyme gene mutations cause hereditary systemic amyloidosis
    • Pepys MB, Hawkins PN, Booth DR et al. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 1993; 362: 553-557.
    • (1993) Nature , vol.362 , pp. 553-557
    • Pepys, M.B.1    Hawkins, P.N.2    Booth, D.R.3
  • 6
    • 77957180065 scopus 로고
    • A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves
    • Andrade C. A peculiar form of peripheral neuropathy. Familial atypical generalized amyloidosis with special involvement of the peripheral nerves. Brain 1952; 75: 408-427.
    • (1952) Brain , vol.75 , pp. 408-427
    • Andrade, C.1
  • 7
    • 0030217827 scopus 로고    scopus 로고
    • Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2
    • Yamagoe S, Yamakawa Y, Matsuo Y et al. Purification and primary amino acid sequence of a novel neutrophil chemotactic factor LECT2. Immunol Lett 1996; 52: 9-13.
    • (1996) Immunol Lett , vol.52 , pp. 9-13
    • Yamagoe, S.1    Yamakawa, Y.2    Matsuo, Y.3
  • 8
    • 0032481611 scopus 로고    scopus 로고
    • Molecular cloning of human and bovine LECT2 having a neutrophil chemotactic activity and its specific expression in the liver
    • Yamagoe S, Mizuno S, Suzuki K. Molecular cloning of human and bovine LECT2 having a neutrophil chemotactic activity and its specific expression in the liver. Biochem Biophys Acta 1998; 1396: 105-113.
    • (1998) Biochem Biophys Acta , vol.1396 , pp. 105-113
    • Yamagoe, S.1    Mizuno, S.2    Suzuki, K.3
  • 9
    • 0029787833 scopus 로고    scopus 로고
    • A novel growth-promoting factor derived from fetal bovine cartilage, chondromodulin II. Purification and amino acid sequence
    • Hiraki Y, Inoue H, Kondo J et al. A novel growth-promoting factor derived from fetal bovine cartilage, chondromodulin II. Purification and amino acid sequence. J Biol Chem 1996; 271: 22657-22662.
    • (1996) J Biol Chem , vol.271 , pp. 22657-22662
    • Hiraki, Y.1    Inoue, H.2    Kondo, J.3
  • 10
    • 0032520903 scopus 로고    scopus 로고
    • Molecular cloning, structural characterization, and chromosomal mapping of the human LECT2 gene
    • Yamagoe S, Kameoka Y, Hashimoto K et al. Molecular cloning, structural characterization, and chromosomal mapping of the human LECT2 gene. Genomics 1998; 48: 324-329.
    • (1998) Genomics , vol.48 , pp. 324-329
    • Yamagoe, S.1    Kameoka, Y.2    Hashimoto, K.3
  • 11
    • 0031559576 scopus 로고    scopus 로고
    • Expression of a neutrophil chemotactic protein LECT2 in human hepatocytes revealed by immunochemical studies using polyclonal and monoclonal antibodies to a recombinant LECT2
    • Yamagoe S, Akasaka T, Uchida T et al. Expression of a neutrophil chemotactic protein LECT2 in human hepatocytes revealed by immunochemical studies using polyclonal and monoclonal antibodies to a recombinant LECT2. Biochem Biophys Res Commun 1997; 237: 116-120.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 116-120
    • Yamagoe, S.1    Akasaka, T.2    Uchida, T.3
  • 12
    • 0031760412 scopus 로고    scopus 로고
    • Systemic expression of a newly recognized protein, LECT2, in the human body
    • Nagai H, Hamada T, Uchida T et al. Systemic expression of a newly recognized protein, LECT2, in the human body. Pathol Int 1998; 48: 882-886.
    • (1998) Pathol Int , vol.48 , pp. 882-886
    • Nagai, H.1    Hamada, T.2    Uchida, T.3
  • 13
    • 0000375747 scopus 로고
    • The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences
    • Benditt EP, Eriksen N, Hermodson MA et al. The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences. FEBS Lett 1971; 19: 169-173.
    • (1971) FEBS Lett , vol.19 , pp. 169-173
    • Benditt, E.P.1    Eriksen, N.2    Hermodson, M.A.3
  • 14
    • 0015419122 scopus 로고
    • The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils
    • Levin M, Franklin EC, Frangione B et al. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest 1972; 51: 2773-2776.
    • (1972) J Clin Invest , vol.51 , pp. 2773-2776
    • Levin, M.1    Franklin, E.C.2    Frangione, B.3
  • 15
    • 0014278442 scopus 로고
    • The characterization of soluble amyloid prepared in water
    • Pras M, Schubert M, Zucker-Franklin D et al. The characterization of soluble amyloid prepared in water. J Clin Invest 1968; 47: 924-933.
    • (1968) J Clin Invest , vol.47 , pp. 924-933
    • Pras, M.1    Schubert, M.2    Zucker-Franklin, D.3
  • 16
    • 0034787401 scopus 로고    scopus 로고
    • Shoulder-pad sign of amyloidosis: Structure of an immunoglobulin kappa III protein
    • Liepnieks JJ, Burt C, Benson MD. Shoulder-pad sign of amyloidosis: structure of an immunoglobulin kappa III protein. Scand J Immunol 2001; 54: 404-408.
    • (2001) Scand J Immunol , vol.54 , pp. 404-408
    • Liepnieks, J.J.1    Burt, C.2    Benson, M.D.3
  • 17
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate- polyacrylamide gel electro-phoresis for the separation of proteins in the range from 1-100 kDa
    • Schägger H, Von Jagow G. Tricine-sodium dodecyl sulfate- polyacrylamide gel electro-phoresis for the separation of proteins in the range from 1-100 kDa. Anal Biochem 1987; 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 18
    • 0001948629 scopus 로고
    • Sambrook J, Fritsch EF, Maniatis J eds, 2nd edn. Cold Spring Harbor Laboratory: Cold Spring Harbor, NY
    • Sambrook J, Fritsch EF, Maniatis J (eds). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory: Cold Spring Harbor, NY, 1989, pp 280.
    • (1989) Molecular Cloning: A Laboratory Manual , pp. 280


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.