Добавил:
Sekretar
kiopkiopkiop18@yandex.ru
t.me/Prokururor I Вовсе не секретарь, но почту проверяю
Опубликованный материал нарушает ваши авторские права? Сообщите нам.
Вуз:
Предмет:
Файл:Ординатура / Хирургия / Библиотека им академика М.И. Перельмана / Книга_3099_Библиотеки_им_академика_М_И_Перельмана.pdf
Clinical Management of Amyloidosis
67
the treatment of transthyretin-associated polyneuropathy. Amyloid: The
International Journal of Experimental and Clinical Investigation: The
Official Journal of the International Society of Amyloidosis, 19 Suppl. 1,
43–4.
Adams, D. (2000). The course and prognostic factors of familial amyloid
polyneuropathy after liver transplantation. Brain, 123(7), 1495–1504.
Adams, D., Lozeron, P., Theaudin, M., Mincheva, Z., Cauquil, C., Adam, C.,
… Lacroix, C. (2012). Regional difference and similarity of familial
amyloidosis with polyneuropathy in France. Amyloid : The International
Journal of Experimental and Clinical Investigation: The Official Journal
of the International Society of Amyloidosis, 19 Suppl. 1, 61–4.
Almeida, V. M., Costa, P. M., Moreira, P., Gonçalves, J., and Braga, J. (2005).
Birth of two healthy females after preimplantation genetic diagnosis for
familial amyloid polyneuropathy. Reproductive Biomedicine Online, 10
(5), 641–4.
Artl, A., Marsche, G., Lestavel, S., Sattler, W., and Malle, E. (2000). Role of
Serum Amyloid A During Metabolism of Acute-Phase HDL by
Macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology, 20(3),
763–772.
Benson, M. D. (2003). The hereditary amyloidoses. Best Practice and
Research. Clinical Rheumatology, 17(6), 909–27.
Benson, M. D. (2005). Ostertag revisited: the inherited systemic amyloidoses
without neuropathy. Amyloid: The International Journal of Experimental
and Clinical Investigation: The Official Journal of the International
Society of Amyloidosis, 12(2), 75–87.
Benson, M. D., Kluve-Beckerman, B., Zeldenrust, S. R., Siesky, A. M.,
Bodenmiller, D. M., Showalter, A. D., and Sloop, K. W. (2006). Targeted
suppression of an amyloidogenic transthyretin with antisense
oligonucleotides. Muscle and Nerve, 33(5), 609–618.
Bispo, M., Marcelino, P., Freire, A., Martins, A., Mourão, L., and Barroso, E.
(2009). High incidence of thrombotic complications early after liver
transplantation for familial amyloidotic polyneuropathy. Transplant
International: Official Journal of the European Society for Organ
Transplantation, 22(2), 165–71.
Blancas-Mejía, L. M., and Ramirez-Alvarado, M. (2013). Systemic
amyloidoses. Annual Review of Biochemistry, 82, 745–74.
Jennifer Davey, Jen Bevilacqua, Andrew Hesse et al.
68
Bodin, K., Ellmerich, S., Kahan, M. C., Tennent, G. A., Loesch, A.,
Gilbertson, J. A., … Pepys, M. B. (2010). Antibodies to human serum
amyloid P component eliminate visceral amyloid deposits. Nature, 468
(7320), 93–7.
Butler, J. S., Chan, A., Charisse, K., Costelha, S., Fishman, S., Concalves, P.,
… Zimmermann, T. (2010). Preclinical Evaluation of RNAi Therapeutics
for the Treatment of ATTR: An Update. Retrieved from http://www.
alnylam.com/web/assets/Preclinical-Evaluation-of-RNAiTx-for-TTR-
Poster-ISA2014.pdf.
Coelho, T., Adams, D., Silva, A., Lozeron, P., Hawkins, P. N., Mant, T., …
Suhr, O. B. (2013). Safety and efficacy of RNAi therapy for transthyretin
amyloidosis. The New England Journal of Medicine, 369(9), 819–29.
Desport, E., Bridoux, F., Sirac, C., Delbes, S., Bender, S., Fernandez, B., …
Jaccard, A. (2012). Al amyloidosis. Orphanet Journal of Rare Diseases, 7,
54.
Eklund, K. K., Niemi, K., and Kovanen, P. T. (2012). Immune functions of
serum amyloid A. Critical Reviews in Immunology, 32(4), 335–48.
Falk, R. H., Comenzo, R. L., and Skinner, M. (1997). The systemic
amyloidoses. The New England Journal of Medicine, 337(13), 898–909.
FDA. (2012). Vyndaqel (tafamidis meglumine) capsules: Proposed indication:
Treatment of transthyretin (TTR) familial amyloid polyneuropathy.
Retrieved from http://www.fda.gov/downloads/Advisorycommittees
MeetingMaterials/Drugs/PeripheralandCentralNervousSystemDrugsAdvis
oryCommittee/UCM304830.pdf.
Floege, J., and Ketteler, M. (2001). beta2-microglobulin-derived amyloidosis:
an update. Kidney International. Supplement, 78(78), S164–71.
Graceffa, A., Russo, M., Vita, G. L., Toscano, A., Dattola, R., Messina, C., …
Mazzeo, A. (2009). Psychosocial impact of presymptomatic genetic
testing for transthyretin amyloidotic polyneuropathy. Neuromuscular
Disorders: NMD, 19(1), 44–8.
Hawkins, P. N., Ando, Y., Dispenzeri, A., Gonzalez-Duarte, A., Adams, D.,
and Suhr, O. B. (2015). Evolving landscape in the management of
transthyretin amyloidosis. Annals of Medicine, 47(8), 625–38.
Jaccard, A., Moreau, P., Leblond, V., Leleu, X., Benboubker, L., Hermine, O.,
… Fermand, J.-P. (2007). High-dose melphalan versus melphalan plus
dexamethasone for AL amyloidosis. The New England Journal of
Medicine, 357(11), 1083–93.
Clinical Management of Amyloidosis
69
Kallianidis, A. F., Ray, A., Goudkade, D., and de Fijter, J. W. (2016).
Amyloid A amyloidosis secondary to hyper IgD syndrome and response to
IL-1 blockage therapy. The Netherlands Journal of Medicine, 74(1), 43–6.
Kapoor, P., Thenappan, T., Singh, E., Kumar, S., and Greipp, P. R. (2011).
Cardiac amyloidosis: a practical approach to diagnosis and management.
The American Journal of Medicine, 124(11), 1006–15.
Kyle, R. A., and Gertz, M. A. (1995). Primary systemic amyloidosis: clinical
and laboratory features in 474 cases. Seminars in Hematology, 32(1), 45–
59.
Kyle, R. A., Linos, A., Beard, C. M., Linke, R. P., Gertz, M. A., O’Fallon, W.
M., and Kurland, L. T. (1992). Incidence and natural history of primary
systemic amyloidosis in Olmsted County, Minnesota, 1950 through 1989.
Blood, 79(7), 1817–22.
Lachmann, H. J., Booth, D. R., Booth, S. E., Bybee, A., Gilbertson, J. A.,
Gillmore, J. D., … Hawkins, P. N. (2002). Misdiagnosis of hereditary
amyloidosis as AL (primary) amyloidosis. The New England Journal of
Medicine, 346(23), 1786–91.
Lachmann, H. J., Goodman, H. J. B., Gilbertson, J. A., Gallimore, J. R., Sabin,
C. A., Gillmore, J. D., and Hawkins, P. N. (2007). Natural history and
outcome in systemic AA amyloidosis. The New England Journal of
Medicine, 356(23), 2361–71.
Leung, N., Nasr, S. H., and Sethi, S. (2012). How I treat amyloidosis: the
importance of accurate diagnosis and amyloid typing. Blood, 120(16),
3206–13.
Mereuta, O. M., Theis, J. D., Vrana, J. A., Law, M. E., Grogg, K. L., Dasari,
S., … Dogan, A. (2014). Leukocyte cell-derived chemotaxin 2 (LECT2)-
associated amyloidosis is a frequent cause of hepatic amyloidosis in the
United States. Blood, 123(10), 1479–1482.
Muchtar, E., Buadi, F. K., Dispenzieri, A., and Gertz, M. A. (2016).
Immunoglobulin Light-Chain Amyloidosis: From Basics to New
Developments in Diagnosis, Prognosis and Therapy. Acta Haematologica,
135(3), 172–90.
Nelson LM, Penninga L, Sander K, Hansen PB, Villadsen GE, Rasmussen A
et al. Long-term outcome in patients treated with combined heart and liver
transplantation for familial amyloidotic cardiomyopathy. Clin Transplant.
2013;27:203–9.
NSGC. (2012). Genetic Testing of Minors for Adult-Onset Conditions.
Retrieved March 27, 2016, from http://nsgc.org/p/bl/et/blogid=47&
blogaid=28.
Jennifer Davey, Jen Bevilacqua, Andrew Hesse et al.
70
Obici, L., Cortese, A., Lozza, A., Lucchetti, J., Gobbi, M., Palladini, G., …
Merlini, G. (2012). Doxycycline plus tauroursodeoxycholic acid for
transthyretin amyloidosis: a phase II study. Amyloid, 19(S1), 34–36.
Obici, L., Kuks, J. B., Buades, J., Adams, D., Suhr, O. B., Coelho, T., and
Kyriakides, T. (2016). Recommendations for presymptomatic genetic
testing and management of individuals at risk for hereditary transthyretin
amyloidosis. Current Opinion in Neurology, 29 Suppl. 1, S27–35.
Obici, L., Perfetti, V., Palladini, G., Moratti, R., and Merlini, G. (2005).
Clinical aspects of systemic amyloid diseases. In: Biochimica et
Biophysica Acta - Proteins and Proteomics (Vol. 1753, pp. 11–22).
Palladini, G., Perfetti, V., Obici, L., Caccialanza, R., Semino, A., Adami, F.,
… Merlini, G. (2004). Association of melphalan and high-dose
dexamethasone is effective and well tolerated in patients with AL
(primary) amyloidosis who are ineligible for stem cell transplantation.
Blood, 103(8), 2936–8.
Paneque, M., Lemos, C., Sousa, A., Velázquez, L., Fleming, M., and
Sequeiros, J. (2009). Role of the disease in the psychological impact of
pre-symptomatic testing for SCA2 and FAP ATTRV30M: Experience
with the disease, kinship and gender of the transmitting parent. Journal of
Genetic Counseling, 18(5), 483–93.
Pepys, M. B. (2006). Amyloidosis. Annual Review of Medicine, 57, 223–41.
Pinney, J. H., Smith, C. J., Taube, J. B., Lachmann, H. J., Venner, C. P.,
Gibbs, S. D. J., … Gillmore, J. D. (2013). Systemic amyloidosis in
England: an epidemiological study. British Journal of Haematology, 161
(4), 525–32.
Real de Asúa, D., Costa, R., Galván, J. M., Filigheddu, M. T., Trujillo, D., and
Cadiñanos, J. (2014). Systemic AA amyloidosis: epidemiology, diagnosis,
and management. Clinical Epidemiology, 6, 369–77.
Reddi, H. V, Jenkins, S., Theis, J., Thomas, B. C., Connors, L. H., Van Rhee,
F., and Highsmith, W. E. (2014). Homozygosity for the V122I mutation in
transthyretin is associated with earlier onset of cardiac amyloidosis in the
African American population in the seventh decade of life. The Journal of
Molecular Diagnostics: JMD, 16(1), 68–74.
Reddi, H. V, Thomas, B. C., Willkomm, K. S., Ferber, M. J., Rumilla, K. M.,
Raymond, K. M., … Highsmith, W. E. (2013). Discordant results between
biochemical and molecular transthyretin assays: lessons learned from a
unique testing algorithm at the Mayo Clinic. Journal of Genetics, 92(3),
599–604.
Clinical Management of Amyloidosis
71
Richards, D. B., Cookson, L. M., Berges, A. C., Barton, S. V, Lane, T., Ritter,
J. M., … Pepys, M. B. (2015). Therapeutic Clearance of Amyloid by
Antibodies to Serum Amyloid P Component. The New England Journal of
Medicine, 373(12), 1106–14.
Ross et al. Ross, L. F. L. F., Saal, H. M., David, K. L., and Anderson, R. R.
(2013). Ethical and Policy Issues in Genetic Testing and Screening of
Children. Pediatrics, 15, 234–45.
Sanchorawala, V. (2006). Light-chain (AL) amyloidosis: diagnosis and
treatment. Clinical Journal of the American Society of Nephrology:
CJASN, 1(6), 1331–41.
Scarpioni, R., Ricardi, M., and Albertazzi, V. (2016). Secondary amyloidosis
in autoinflammatory diseases and the role of inflammation in renal
damage. World Journal of Nephrology, 5(1), 66–75.
Sekijima, Y., Wiseman, R. L., Matteson, J., Hammarström, P., Miller, S. R.,
Sawkar, A. R., … Kelly, J. W. (2005). The biological and chemical basis
for tissue-selective amyloid disease. Cell, 121(1), 73–85.
Sekijima, Y., Yoshida, K., Tokuda, T., and Ikeda, S. (2012, January 26).
Familial Transthyretin Amyloidosis. University of Washington, Seattle.
Retrieved from http://www.ncbi.nlm.nih.gov/books/NBK1194/.
Skirton, H., Goldsmith, L., Jackson, L., and Tibben, A. (2013). Quality in
genetic counselling for presymptomatic testing--clinical guidelines for
practice across the range of genetic conditions. European Journal of
Human Genetics: EJHG, 21(3), 256–60.
Solomon, J. P., Page, L. J., Balch, W. E., and Kelly, J. W. (2012). Gelsolin
amyloidosis: genetics, biochemistry, pathology and possible strategies for
therapeutic intervention. Critical Reviews in Biochemistry and Molecular
Biology, 47(3), 282–296.
Swan, N., Skinner, M., and O’Hara, C. J. (2003). Bone marrow core biopsy
specimens in AL (primary) amyloidosis. A morphologic and
immunohistochemical study of 100 cases. American Journal of Clinical
Pathology, 120(4), 610–6.
Vrana, J. A., Gamez, J. D., Madden, B. J., Theis, J. D., Bergen, H. R., and
Dogan, A. (2009). Classification of amyloidosis by laser microdissection
and mass spectrometry-based proteomic analysis in clinical biopsy
specimens. Blood, 114(24), 4957–4959.
Wechalekar, A. D., Hawkins, P. N., and Gillmore, J. D. (2008). Perspectives in
treatment of AL amyloidosis. British Journal of Haematology, 140(4),
365–77.
Jennifer Davey, Jen Bevilacqua, Andrew Hesse et al.
72
Yamamoto, S., Wilczek, H. E., Nowak, G., Larsson, M., Oksanen, A., Iwata,
T., … Ericzon, B.-G. (2007). Liver transplantation for familial
amyloidotic polyneuropathy (FAP): a single-center experience over 16
years. American Journal of Transplantation: Official Journal of the
American Society of Transplantation and the American Society of
Transplant Surgeons, 7(11), 2597–604.
Zimmermann, T., Karsten, V., Harrop, J., Chan, A., Chiesa, J., Peters, G., …
Gollob, J. (2013). Phase I First-in-Human Trial of ALN-TTRsc, A Novel
RNA Interference Therapeutic for the Treatment of Familial Amyloidotic
Cardiomyopathy (FAC). Heart Failure Society of America Annual
Scientific Meeting, 10.
In: Amyloidosis ISBN: 978-1-63485-884-7
Editor: Raquel Watts © 2017 Nova Science Publishers, Inc.
Chapter 4
TISSUE EXAMINATION IN A
DIAGNOSTIC PROCEDURE
Pavla Flodrova
1,*
, Tomas Pika
2
and Patrik Flodr
1
1
Department of Clinical and Molecular Pathology,
Faculty of Medicine and Dentistry,
Palacky University Olomouc, Czech Republic
2
Department of Hemato-oncology,
University Hospital Olomouc, Czech Republic
ABSTRACT
Apart from a general clinical examination, a tissue biopsy with the
morphological proof of amyloid deposits plays an unsubstitutable role in
making a diagnosis. In cases of systemic diseases, a biopsy could be
untargeted at first (subcutaneous fat, small labial glands, rectal mucosa,
and tongue) and followed by a targeted biopsy of the involved organ
(heart or kidney) when the first untargeted specimen was not diagnostic.
In methods of special histological staining, amyloid reacts positively
with histochemical dyes Congo red or Sirius red, a metachromatic
staining (methyl violet) can also be used. Characteristic properties of
amyloid using Congo red stained slides seen under polarized light are
required for the diagnosis.
*
Corresponding author: latalova.pavla@seznam.cz.
Pavla Flodrova, Tomas Pika and Patrik Flodr
74
An ultrastructure of amyloid deposits is demonstrated by using an
electron microscope, where non-branching fibrils composed of
protofibrils can be seen.
Nowadays a determination of a specific amyloid type is dominantly
based on immunological methods with an antigen-antibody
reaction (immunohistochemistry, immunofluorescence, or less used
immunoelectron microscopy), that is the indirect evidence of the
protein. Several difficulties have been described in immunohisto-
chemistochemical examination of formalin-fixed paraffin embedded
tissue samples. For example, the heterogeneity of variable domains of
light chains, antigen masking due to protein folding, or contamination of
amyloid deposits by serum proteins could reduce reliability of the testing
using an immunohistochemical method.
To avoid problems with nonspecific protein detection, the new
methodology based on mass spectrometry seems to be highly specific and
sensitive with the direct protein recognition in a small piece of tissue
sample. Liquid chromatography-mass spectrometry is an analytic
chemistry technique and a well established powerful proteomic tool
which allows an identification of the amyloidogenic protein and other
amyloid-associated molecules as well (serum amyloid P component,
apolipoproteins). These form usual constituent parts of the amyloid and
may serve as an ancillary diagnostic approach. Laser microdissection of
amyloid deposit from histological sections significantly increases the
accuracy and reliability of the LC-MS analysis and is preferred.
INTRODUCTION
Amyloidosis as a disease includes an incoherent group of amyloid
subtypes. Although the aetiology and pathogenesis of amyloidosis are diverse
according to individual subtypes of the disease, regardless of the subtype it can
be defined as an extracellular accumulation of insoluble or poorly soluble
complex deposits in various tissues and organs in the body. Amyloid deposits
could be local or more often systemic involving various types of tissues. The
beginning of the amyloid history is associated with Rudolph Virchow, who
described macroscopically a substance in brain tissue, which was recognized
by characteristic tinctorial properties when treated with iodine and sulphuric
acid treatment [1]. Conditions that underlie the origin of amyloidosis, are
connected either with inherent instability of a native wild-type protein, or
overproduction of a normal protein with reduced stability and increased
propensity to misfold or with production of an abnormal unstable protein [2].
Tissue Examination in a Diagnostic Procedure
75
For a long time, it was not of physicians and investigators’ primary
interest. The reasons were primarily the absence of adequate therapy,
knowledge of aetiology, and pathogenesis of the disease and last but not least
late diagnoses of patients in advanced and incurable stages. With significant
improvement of precise diagnostic methods and new drug and therapy
possibilities in last decades, this diagnosis gains an adequate attention through
the whole spectrum of research and medical teams.
Protein misfolding has been described as a feature in many pathological
conditions ranging from neurodegenerative disorders to amyloidosis. From
clinical point of view, in genuine amyloidosis the deposits are unequivocally
harmful and cause the disease; there is no clinical or pathological evidence of
disease in the absence of such deposits (deposits of amyloid can also be found
in the Islet of Langerhans of pancreatic tissue in some patients with diabetes
mellitus II, but there is no evidence of amyloidosis in these patients since
deposits do not cause the disease) [3]. On the other hand, modern biophysical
definition of the term amyloid reads unbranching protein fibre the repeating
substructure of which consists of β strands that run perpendicular to the fibre
axis, forming a cross-β sheet of indefinite length [30], with the designation of
“amyloid fibril” when they accumulate extracellularly and propose
“intracellular inclusions” in case of fibrils morphologically and structurally
related to extracellular amyloid form inside the cell [4]. Since the deposits are
not a necessary condition for diseases such Alzheimer’s disease, Parkinson’s
disease and prion diseases, finding of abnormal protein aggregates in these
conditions should not be called amyloidosis [3]. The term “functional
amyloid” was established to define the amyloid structure found to have
beneficial function for a living organism and this was supported by increasing
findings of fibrillar aggregates with no link to protein deposition disease.
Some organisms (bacteria as well as higher organisms) are able to transform a
normal endogenous protein into amyloid fibrils during their physiological life
and this process is thought to be useful for specific and specialized biological
functions and takes place under highly controlled conditions [4].
HISTOPATHOLOGY IN BASIC AND SPECIAL STAINS
A histological examination with a proof of amyloid deposits is necessary
to make a diagnosis. In cases of systemic diseases, a biopsy could be
untargeted at first (subcutaneous fat, small labial glands, rectal mucosa, and
Pavla Flodrova, Tomas Pika and Patrik Flodr
76
tongue) and followed by a targeted biopsy of the involved organ (heart or
kidney) when the first untargeted specimen was not diagnostic.
Basic staining in histology, the hematoxylin-eosin, gives an eosinophilic
colour in amyloid deposits as well as other proteinaceous substances in tissues.
In methods of special histologic staining, amyloid reacts with Congo red and
Sirius red label and metachromatic staining (methyl violet) can also be used.
Figure 1. Kidney, Congo red, original magnification 100x. Massive amyloid deposition
in glomeruli, which is characteristic for amyloid based on fibrinogen.
Figure 2. Rectal biopsy, Congo red (A) and Sirius red (B) in original magnification
200x. Very few blood vessels with intramural deposition of amyloid can cause serious
diagnostic problem due to the oversight.