메뉴 건너뛰기




Volumn 116, Issue 1, 2001, Pages 135-142

Chemical typing of amyloid protein contained in formalin-fixed paraffin-embedded biopsy specimens

Author keywords

Amyloid; Amyloid typing; Amyloidosis; Chemical characterization; Formalin fixation

Indexed keywords

AMYLOID PROTEIN; FORMALDEHYDE; PARAFFIN;

EID: 17844409327     PISSN: 00029173     EISSN: None     Source Type: Journal    
DOI: 10.1309/TWBM-8L4E-VK22-FRH5     Document Type: Article
Times cited : (125)

References (41)
  • 1
    • 0030682237 scopus 로고    scopus 로고
    • Amyloidosis: A review of recent diagnostic and therapeutic developments
    • Gillmore JD, Hawkins PN, Pepys MB. Amyloidosis: a review of recent diagnostic and therapeutic developments. Br J Haematol. 1997;99:245-256.
    • (1997) Br J Haematol , vol.99 , pp. 245-256
    • Gillmore, J.D.1    Hawkins, P.N.2    Pepys, M.B.3
  • 2
    • 0033088258 scopus 로고    scopus 로고
    • Nomenclature of amyloid fibril proteins: Report from the meeting of the International Nomenclature Committee on Amyloidosis, August 8-9, 1998, part 1
    • Westermark P, Araki S, Benson MD, et al. Nomenclature of amyloid fibril proteins: report from the meeting of the International Nomenclature Committee on Amyloidosis, August 8-9, 1998, part 1. Amyloid. 1999;6:63-66.
    • (1999) Amyloid , vol.6 , pp. 63-66
    • Westermark, P.1    Araki, S.2    Benson, M.D.3
  • 3
    • 0028970456 scopus 로고
    • Primary systemic amyloidosis: Clinical and laboratory features in 474 cases
    • Kyle RA, Gertz MA. Primary systemic amyloidosis: clinical and laboratory features in 474 cases. Semin Hematol. 1995; 32:45-59.
    • (1995) Semin Hematol , vol.32 , pp. 45-59
    • Kyle, R.A.1    Gertz, M.A.2
  • 5
    • 0017343553 scopus 로고
    • Potassium permanganate reaction in amyloidosis: A histologic method to assist in differentiating forms of this disease
    • Wright JR, Calkins E, Humphrey RL. Potassium permanganate reaction in amyloidosis: a histologic method to assist in differentiating forms of this disease. Lab Invest. 1977;36:274-281.
    • (1977) Lab Invest , vol.36 , pp. 274-281
    • Wright, J.R.1    Calkins, E.2    Humphrey, R.L.3
  • 7
    • 0022283219 scopus 로고
    • Immunochemical typing of amyloid deposits after microextraction from biopsies
    • Linke RP. Immunochemical typing of amyloid deposits after microextraction from biopsies. Appl Pathol. 1985;3:18-28.
    • (1985) Appl Pathol , vol.3 , pp. 18-28
    • Linke, R.P.1
  • 8
    • 0022655168 scopus 로고
    • Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins
    • van de Kaa CA, Hol PR, Huber J, et al. Diagnosis of the type of amyloid in paraffin wax embedded tissue sections using antisera against human and animal amyloid proteins. Virchows Arch A Pathol Anat Histopathol. 1986;408:649-664.
    • (1986) Virchows Arch A Pathol Anat Histopathol , vol.408 , pp. 649-664
    • Van De Kaa, C.A.1    Hol, P.R.2    Huber, J.3
  • 9
    • 0023554781 scopus 로고
    • Primary amyloidosis A: Immunohistochemical and biochemical characterization
    • Picken MM, Pelton K, Frangione B, et al. Primary amyloidosis A: immunohistochemical and biochemical characterization. Am J Pathol. 1987;129:536-542.
    • (1987) Am J Pathol , vol.129 , pp. 536-542
    • Picken, M.M.1    Pelton, K.2    Frangione, B.3
  • 10
    • 0029816662 scopus 로고    scopus 로고
    • The classification of amyloid deposits in clinicopathological practice
    • Röcken C, Schwotzer EB, Linke RP, et al. The classification of amyloid deposits in clinicopathological practice. Histopathology. 1996;29:325-335.
    • (1996) Histopathology , vol.29 , pp. 325-335
    • Röcken, C.1    Schwotzer, E.B.2    Linke, R.P.3
  • 11
    • 1542739091 scopus 로고    scopus 로고
    • Immunochemical characterization of amyloid in diagnostic biopsy tissue
    • Kaplan B, Yakar S, Kumar A, et al. Immunochemical characterization of amyloid in diagnostic biopsy tissue. Amyloid. 1997;4:80-86.
    • (1997) Amyloid , vol.4 , pp. 80-86
    • Kaplan, B.1    Yakar, S.2    Kumar, A.3
  • 12
    • 0033491253 scopus 로고    scopus 로고
    • Immunochemical microanalysis of amyloid proteins in fine-needle aspirates of abdominal fat
    • Kaplan B, Vidal R, Kumar A, et al. Immunochemical microanalysis of amyloid proteins in fine-needle aspirates of abdominal fat. Am J Clin Pathol. 1999;112:403-407.
    • (1999) Am J Clin Pathol , vol.112 , pp. 403-407
    • Kaplan, B.1    Vidal, R.2    Kumar, A.3
  • 13
    • 0033035051 scopus 로고    scopus 로고
    • The use of subcutaneous fat tissue for amyloid typing by enzyme linked immunosorbent assay
    • Olsen KE, Sletten K, Westermark P. The use of subcutaneous fat tissue for amyloid typing by enzyme linked immunosorbent assay. Am J Clin Pathol. 1999;111:355-362.
    • (1999) Am J Clin Pathol , vol.111 , pp. 355-362
    • Olsen, K.E.1    Sletten, K.2    Westermark, P.3
  • 14
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)
    • Solomon A, Weiss DT. Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis). Amyloid. 1995;2:269-279.
    • (1995) Amyloid , vol.2 , pp. 269-279
    • Solomon, A.1    Weiss, D.T.2
  • 15
    • 0024353778 scopus 로고
    • Use of subcutaneous abdominal fat biopsy specimen for detailed typing of amyloid fibril protein-AL by amino acid sequence analysis
    • Westermark P, Benson L, Juul J, et al. Use of subcutaneous abdominal fat biopsy specimen for detailed typing of amyloid fibril protein-AL by amino acid sequence analysis. J Clin Pathol. 1989;42:817-819.
    • (1989) J Clin Pathol , vol.42 , pp. 817-819
    • Westermark, P.1    Benson, L.2    Juul, J.3
  • 16
    • 0001620355 scopus 로고    scopus 로고
    • Immunoglobulin lambda light chains are the precursors of ureteral localized amyloidosis: A micromethod for extraction of amyloid
    • Castaño EM, Prelli F, Morelli L, et al. Immunoglobulin lambda light chains are the precursors of ureteral localized amyloidosis: a micromethod for extraction of amyloid. Amyloid. 1997;4:253-258.
    • (1997) Amyloid , vol.4 , pp. 253-258
    • Castaño, E.M.1    Prelli, F.2    Morelli, L.3
  • 17
    • 0032576990 scopus 로고    scopus 로고
    • Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: Kappa IV immunoglobulin light chain
    • Olsen KE, Sletten K, Westermark P. Extended analysis of AL-amyloid protein from abdominal wall subcutaneous fat biopsy: kappa IV immunoglobulin light chain. Biochem Biophys Res Commun. 1998;245:713-716.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 713-716
    • Olsen, K.E.1    Sletten, K.2    Westermark, P.3
  • 18
    • 0032877133 scopus 로고    scopus 로고
    • Microextraction and purification techniques applicable to chemical characterization of amyloid proteins in minute amounts of tissue
    • Kaplan B, Hrncic R, Murphy CL, et al. Microextraction and purification techniques applicable to chemical characterization of amyloid proteins in minute amounts of tissue. Methods Enzymol. 1999;309:67-81.
    • (1999) Methods Enzymol , vol.309 , pp. 67-81
    • Kaplan, B.1    Hrncic, R.2    Murphy, C.L.3
  • 19
    • 0035098425 scopus 로고    scopus 로고
    • Micro-method to isolate and purify amyloid proteins for chemical characterization
    • Kaplan B, Murphy CL, Ratner V, et al. Micro-method to isolate and purify amyloid proteins for chemical characterization. Amyloid. 2001;8:22-29.
    • (2001) Amyloid , vol.8 , pp. 22-29
    • Kaplan, B.1    Murphy, C.L.2    Ratner, V.3
  • 20
    • 0020052864 scopus 로고
    • Demonstration of AA-protein in formalin-fixed, paraffin-embedded tissues
    • Shtrasburg S, Pras M, Langevitch P, et al. Demonstration of AA-protein in formalin-fixed, paraffin-embedded tissues. Am J Pathol. 1982;106:141-144.
    • (1982) Am J Pathol , vol.106 , pp. 141-144
    • Shtrasburg, S.1    Pras, M.2    Langevitch, P.3
  • 21
    • 0020636457 scopus 로고
    • Identification of amyloid A protein in a sporadic Muckle-Wells syndrome: N-terminal amino acid sequence after isolation from formalin-fixed tissue
    • Linke RP, Heilmann KL, Nathrath WBJ, et al. Identification of amyloid A protein in a sporadic Muckle-Wells syndrome: N-terminal amino acid sequence after isolation from formalin-fixed tissue. Lab Invest. 1983;48:698-704.
    • (1983) Lab Invest , vol.48 , pp. 698-704
    • Linke, R.P.1    Heilmann, K.L.2    Nathrath, W.B.J.3
  • 22
    • 0030443649 scopus 로고    scopus 로고
    • Extraction and protein sequencing of immunoglobulin light chain from formalin-fixed cerebrovascular amyloid deposits
    • Layfield R, Bailey K, Lowe J, et al. Extraction and protein sequencing of immunoglobulin light chain from formalin-fixed cerebrovascular amyloid deposits. J Pathol. 1996;180:455-459.
    • (1996) J Pathol , vol.180 , pp. 455-459
    • Layfield, R.1    Bailey, K.2    Lowe, J.3
  • 23
    • 0031282263 scopus 로고    scopus 로고
    • Application of formalin fixation to the purification of amyloid proteins
    • Layfield R, Bailey K, Dineen R, et al. Application of formalin fixation to the purification of amyloid proteins. Anal Biochem. 1997;253:142-144.
    • (1997) Anal Biochem , vol.253 , pp. 142-144
    • Layfield, R.1    Bailey, K.2    Dineen, R.3
  • 24
    • 14444276493 scopus 로고    scopus 로고
    • Extraction and analysis of diagnostically useful proteins from formalin-fixed, paraffin-embedded tissue sections
    • Ikeda K, Monden T, Kanoh T, et al. Extraction and analysis of diagnostically useful proteins from formalin-fixed, paraffin-embedded tissue sections. J Histochem Cytochem. 1998;46:397-403.
    • (1998) J Histochem Cytochem , vol.46 , pp. 397-403
    • Ikeda, K.1    Monden, T.2    Kanoh, T.3
  • 25
    • 0025049732 scopus 로고
    • Immunocytochemical detection of kappa and lambda light chain V region subgroups in human B-cell malignancies
    • Solomon A, Weiss DT, Macy SD, et al. Immunocytochemical detection of kappa and lambda light chain V region subgroups in human B-cell malignancies. Am J Pathol. 1990;137:855-862.
    • (1990) Am J Pathol , vol.137 , pp. 855-862
    • Solomon, A.1    Weiss, D.T.2    Macy, S.D.3
  • 27
    • 0022472793 scopus 로고
    • Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis
    • Wallace MR, Dwulet FE, Conneally PM, et al. Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest. 1986;78:6-12.
    • (1986) J Clin Invest , vol.78 , pp. 6-12
    • Wallace, M.R.1    Dwulet, F.E.2    Conneally, P.M.3
  • 28
    • 0031834740 scopus 로고    scopus 로고
    • Amyloid tumors in the soft tissues of the legs: Case report and review of the literature
    • Sidoni A, Alberti PF, Bravi S, et al. Amyloid tumors in the soft tissues of the legs: case report and review of the literature. Virchows Arch. 1998;432:563-566.
    • (1998) Virchows Arch , vol.432 , pp. 563-566
    • Sidoni, A.1    Alberti, P.F.2    Bravi, S.3
  • 29
    • 0006112299 scopus 로고
    • Reactions of formaldehyde with amines, amides and nitrites
    • New York, NY: Reinhold Publishing
    • Walker JF. Reactions of formaldehyde with amines, amides and nitrites. In: Formaldehyde. 3rd ed. New York, NY: Reinhold Publishing; 1964:359-414.
    • (1964) Formaldehyde. 3rd Ed. , pp. 359-414
    • Walker, J.F.1
  • 30
    • 0021331659 scopus 로고
    • Demonstration of amyloid protein AA in old museum specimens
    • Westermark P, Nilsson GT. Demonstration of amyloid protein AA in old museum specimens. Arch Pathol Lab Med. 1984;108:217-219.
    • (1984) Arch Pathol Lab Med , vol.108 , pp. 217-219
    • Westermark, P.1    Nilsson, G.T.2
  • 31
    • 0019863278 scopus 로고
    • Amyloidosis, part 3: Secondary amyloidosis
    • Kyle, RA. Amyloidosis, part 3: secondary amyloidosis. Int J Dermatol. 1981;20:75-80.
    • (1981) Int J Dermatol , vol.20 , pp. 75-80
    • Kyle, R.A.1
  • 32
    • 0032525180 scopus 로고    scopus 로고
    • Dose-intensive melphalan with blood stem-cell support for the treatment of AL (amyloid light-chain) amyloidosis: Survival and responses in 25 patients
    • Comenzo RL, Vosburgh E, Falk RH, et al. Dose-intensive melphalan with blood stem-cell support for the treatment of AL (amyloid light-chain) amyloidosis: survival and responses in 25 patients. Blood. 1998;91:3662-3670.
    • (1998) Blood , vol.91 , pp. 3662-3670
    • Comenzo, R.L.1    Vosburgh, E.2    Falk, R.H.3
  • 33
    • 1842527698 scopus 로고    scopus 로고
    • Transthyretin amyloidosis
    • Benson MD, Clemicki T. Transthyretin amyloidosis. Amyloid. 1996;3:44-56.
    • (1996) Amyloid , vol.3 , pp. 44-56
    • Benson, M.D.1    Clemicki, T.2
  • 34
    • 0030600371 scopus 로고    scopus 로고
    • Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation
    • Soto C, Kindy MS, Baumann M, et al. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem Biophys Res Commun. 1996;226:672-680.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 672-680
    • Soto, C.1    Kindy, M.S.2    Baumann, M.3
  • 35
    • 0029094670 scopus 로고
    • New drug therapy of amyloidoses: Resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin
    • Gianni L, Bellotti V, Gianni AM, et al. New drug therapy of amyloidoses: resorption of AL-type deposits with 4′-iodo-4′-deoxydoxorubicin. Blood. 1995;86:855-861.
    • (1995) Blood , vol.86 , pp. 855-861
    • Gianni, L.1    Bellotti, V.2    Gianni, A.M.3
  • 36
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis
    • Tennent GA, Lovat LB, Pepys MB. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc Natl Acad Sci U S A. 1995;92:4299-4303.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 37
    • 0028913416 scopus 로고
    • Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implication for Alzheimer's disease
    • Kisilevsky R, Lemieux LJ, Fraser PE, et al. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implication for Alzheimer's disease. Nat Med. 1995;1:143-148.
    • (1995) Nat Med , vol.1 , pp. 143-148
    • Kisilevsky, R.1    Lemieux, L.J.2    Fraser, P.E.3
  • 38
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on apo-serum amyloid A: Implications for the therapeutic intervention of amyloidosis
    • Ancsin JB, Kisilevsky R. The heparin/heparan sulfate-binding site on apo-serum amyloid A: implications for the therapeutic intervention of amyloidosis. J Biol Chem. 1999;274:7172-7181.
    • (1999) J Biol Chem , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 39
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer disease-like pathology in the PDAPP mouse
    • Schenk D, Barbour R, Dunn W, et al. Immunization with amyloid-beta attenuates Alzheimer disease-like pathology in the PDAPP mouse. Nature. 1999;400:173-177.
    • (1999) Nature , vol.400 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3
  • 40
    • 0033810109 scopus 로고    scopus 로고
    • Antibody-mediated resolution of light chain-associated amyloid deposits
    • Hrncic R, Wall J, Wolfenbarger DA, et al. Antibody-mediated resolution of light chain-associated amyloid deposits. Am J Pathol. 2000;157:1239-1246.
    • (2000) Am J Pathol , vol.157 , pp. 1239-1246
    • Hrncic, R.1    Wall, J.2    Wolfenbarger, D.A.3
  • 41
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease
    • Bard F, Cannon C, Barbour R, et al. Peripherally administered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease. Nat Med. 2000;6:916-919.
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.