Journal reading

Summary
Amyloid deposits in tissue from 8 patients with generalized primary amyloidosis, 1 1 patients with
generalized secondary amyloidosis, 1 1 nasopharyngeal carcinomas, 1 1 basal cell carcinomas, 4 islet
cell tumours, 4 medullary carcinomas of the thyroid and 9 cases of lichen amyloidosis were studied
using the indirect immunoperoxidase and peroxidase-antiperoxidase methods with specific antisera
against Amyloid A (AA) protein and human immunoglobulin lambda and kappa light chains. The
perrnanganate method of Wright was also applied to tissue sections. Positive staining for AA protein
was observed only in secondary amyloidosis. There was excellent correlation between
AA positivity and permanganate sensitivity. Positivity for immunoglobulin light chains was not
observed in secondary amyloidosis but was noted in 5 (63%) cases of primary
amyloidosis and 18-27% of intratumour amyloidosis. Lichen amyloidosis did not stain for AA protein
or light chains. It is shown that assessment of the permanganate reaction and AA positivity of amyloid
deposits can reliably differentiate secondary from primary amyloidosis and may contribute
significantly to selection of patients for appropriate therapy
Key words: Amyloid, amyloidosis, amyloid proteins, AA protein, immunoperoxidase, permanganate
reaction, immunoglobulin, light chains Accepted June 11, 1985
INTRODUCTION
It is known that the major protein components of the amyloid fibril differ in the various types of
amyloidosis. f 2 The fibril protein of primary amyloid and amyloid associated with plasma cell
dyscrasias, termed Amyloid Light Chain (AL) Protein, has been dernonstrated to contain peptide units
identical to the amino-terminal variable regions of immunoglobulin light chain^.^ The amyloid fibril
in secondary amyloid and familial mediterranean fever, however, is composed largely of Amyloid A
(AA) Protein which does not resemble any immun~globul in.L~o calized amyloid deposits found in
endocrine tumours are believed to be related to the respective peptide hormone produced whereas
amyloid deposits in localized cutaneous amyloidosis6 and epithelial tumours such as nasopharyngeal
carcinoma and basal cell carcinoma may be related to keratin. The fibril protein of senile cardiac
amyloidosis, termed ASC Protein, differs from that of senile amyloid deposits in the brain and the
pancreatic islet^.^ In addition, different types of localized amyloidosis, each with a different fibril
protein, may affect the aging or diseased heart.- Amyloid deposits present in the brain in Alzheimers
disease have recently been demonstrated to contain prealbumin. In contrast to the fibril proteins, the
globular protein Amyloid P component has been shown to be present in most types of amyloids, with
the possible exception of intracerebral amyloid in Alzheimers di~ease.R~e cent studies have also
revealed the presence of immunoglobulins and C3 in some a r n y l o i d ~ , p~a rticularly localized
cutaneous
amyloid, but these are thought not to be integral parts of the amyloid fibril.16
It is clear that categorization of amyloidosis by its fibril protein will have important implications on
the pathogenesis, diagnosis and subsequent therapy of the disease.
However, isolation and purification of the fibril protein from amyloid deposits to determine its
biochemical nature is clearly not within the ability of most laboratories. This paper presents the results
of an investigation for the presence of AA protein and immunoglobulin light chains in different types
of amyloid using immunoperoxidase
methods on conventional formaiin-fixed, paraffinembedded tissue sections. The correlation between
immunoperoxidase findings and permanganate reaction of amyloid deposits was studied and a simple
practical laboratory approach to the investigation and classification of amyloidosis is suggested.

MATERIALS AND METHODS

The types of amyloid studied were:
1. Primary arnyloid, using biopsy tissues from 8 patients with generalized
amyloidosis for which no cause could be found. The biopsies were of
rectum (3), kidney ( I ) , liver (I), spleen (I), heart ( I ) and lung ( I ) .
2. Secondary amyloid, using autopsy tissues from 10 Orang Ash
(Malayan aborigine) subjects with generalized arnyloidosis associated
with tuberculosis and 6 patients with generalized amyloidosis associated
with leprosy. The tissues studied were from kidney (9). liver (4), heart
(2) and pancreas (1).
3. Localized intratumour amyloid, using biopsy material from 1 I
nasopharyngeal carcinomas, 11 basal cell carcinomas, 4 islet cell turnours
and 4 medullary carcinomas of the thyroid, in which intratumour
stromal deposits of arnyloid were present.
4. Lichen amyloid, using skin biopsies from 9 consecutive cases of lichen
amyloidosis.
All tissues studied were fixed in 10% buffered formalin and embedded in paraffin. 4 pn thick sections
were stained with hematoxylin and eosin, alkaline Congo red and thioflavine-T. In addition, sections
were also stained with alkaline Congo red after prior treatment with potassium permanganate as
described by Wright et aI.l7
The indirect immunoperoxidase method for AA protein
Formalin-fixed, paraffin-embedded sections from amyloid positive tissues were deparaffinized and
overlaid with 0.5% hydrogen peroxide in methanol for 30 min. The sections were washed and overlaid
with 3% normal rabbit serum (NRS). After tipping off, sections were overlaid with commercially
obtained goat anti-AA protein antiserum (Atlantic Laboratories), diluted 1:160 in 3% NRS, and
incubated in a moist chamber at room temperature for 30 min. The sections were then well washed
with phosphate buffered saline (PBS) and incubated for another 30 min with rabbit anti-goat
peroxidase, diluted 1:20 in 3% NRS. After further washing with PBS, 0.05% 3 , 3 diaminobenzidine
tetrahydrochloride (substrate) was added. The sections were washed, counterstained with hematoxylin
and mounted in Protexx. Controls: The method was repeated using normal goat serum instead of
primary antiserum (goat anti-AA protein antiserum).
The peroxidase antiperoxidase method for human immunoglobulin
lambda and kappa lighr chains
Sections were deparaffinized to alcohol and overlaid with 0.5% hydrogen peroxide in methanol for 30
min. After washing with PBS, they were treated with 3% normal swine serum (NSS) for 20 min. After
tipping off, the sections were overlaid with commercially obtained rabbit antihuman immunoglobulin
kappa or lambda chains (Dako) diluted 1:400 and incubated for 30 min in a moist chamber at room
temperature.
The sections were then rinsed in PBS and incubated for 30 min with swine antirabbit IgG (Dako)
diluted 1:20. After washing in PBS, rabbit antihorseradish peroxidase complex (Dako) diluted 1 :50
was applied and the sections were incubated for 30 min. The sections were then washed with PBS and
an enzyme reaction was developed with 0.05% 3,3 -diaminobenridine tetrahydrochloride. Sections
were washed, counterstained with hematoxylin and mounted in Protexx.
Controls: The method was repeated using normal rabbit serum instead

of primary antisera.
RESULTS
Tinctorial characteristics All the amyloid deposits appeared amorphous and eosinophilic on the
routine H & E stain. They stained rose-pink to orange with alkaline Congo red and exhibited an applegreen birefringence under cross-polarized light. When treated with thioflavine-T and viewed under
ultraviolet light, they showed a whitish-yellow fluorescence. These were the conventional tinctorial
characteristics of amyloid.
Potassium perrnanganate reaction
The various types of amyloid differed in their sensitivity to potassium permanganate. Secondary
amyloid deposits were uniformly sensitive to potassium permanganate in
that they lost affinity for Congo red and birefringence after prior treatment with potassium
permanganate. In contrast, primary amyloid, lichen amyloid and the various
types of intratumour amyloid were resistant to permanganate action and retained both Congo red
affinity and birefringence. AA Protein Using the indirect immunoperoxidase method, anti-AA
antiserum stained positively with amyloid deposits from patients with secondary amyloidosis (Figs 1
& 2), butfailed to stain any amyloid deposits of primary,
intratumour or lichen amyloidosis. AA positivity occurred in the same locations as Congo red
positivity. Normal goat serum controls showed no staining. When AA positivity was compared with
permanganate sensitivity, a good correlation was noted (Table 1).
Amyloid deposits which were AA negative were permanganate resistant while those which stained
positively with anti-AA antiserum were permanganate
sensitive.
Immunoglobulin light chains
The reactions of the various types of amyloid with antilambda and anti-kappa antisera are shown in
Table 2. Five out of 8 (63%) cases of primary amyloid gave a positive reaction for lambda chains.
None of the cases of secondary amyloidosis stained positively for light chains. Positive staining with
either or both light chain antisera was observed in deposits in 27% of nasopharyngeal carcinomas,
more than 18% of basal cell carcinomas, 25% of medullary carcinomas of the thyroid and 25% of islet
cell tumours. These reactions, however, were only weakly positive. Light chains failed to be
detected in lichen amyloidosis. Normal rabbit serum controls showed no staining. DISCUSSION
The classification of amyloidosis has undergone several revisions since its recognition as a disease
entity in 1851 by Virchow. The earlier classifications have been largely
clinical. However, in recent times, rapid advancements in amyloidosis research have evolved the
concept of amyloidosis as a beta-fibrillosis, the chemistry of the betapleated
amyloid fibril differing in the different types of amyloidosis. In view of the many fibril proteins and
precursor proteins characterized, the nomenclature of amyloid fibril proteins was standardized in the
Second International Symposium on Amyloidosis in Helsinki in
1975. In the Third International Symposium held inPortugal in 1979, additions and modifications to
the nomenclature were agreed upon and a new clinicochemical
classification scheme was adopted." This classification has led to better understanding of the disease
and provided a basis for selection of patients for appropriate chemotherapy. However, since
characterization of the amyloid fibril protein by protein extraction is a difficult task, workers are now
turning to immunohistochemical techniques for the classification of amyloidosis. This study has
shown that it is possible to differentiate AA type (secondary) amyloid reliably from several other
major types of amyloid by the use of immunoperoxidase and permanganate methods on conventional

formalinfixed, paraffin-embedded tissue sections. There was excellent correlation between AA

positivity and permanganate sensitivity of amyloid deposits. Both of
these reactions were only observed in deposits from patients who were proven to have either
tuberculosi~'~ or leprosy and were thus accepted as suffering from secondary amyloidosis. However,
the reaction for light chains was not consistent in that many deposits expected to be of AL (primary)
type failed to stain for light chains. This could be because the light chains involved in individual cases
of amyloidosis are idiotypic. Thus, staining for light chains does not appear to be useful in
differentiating the various types of amyloid. It is suggested that a useful histopathological investigative
procedure for classifying amyloidosis would be to assess the AA positivity and permanganate reaction
of the deposits. These histochemical reactions, together with consideration of the other pathological
features of the case under study (e.g. whether the amyloidosis is
localized, generalized or intratumour) should be sufficient in most instances to differentiate the various
types of amyloid. The immunoperoxidase and permanganate methods were reasonably convenient and
easy to carry out and140 Loo[ have several advantages over the immunofluorescence technique used
in earlier studies.20*2T1 he use of paraffinembedded instead of frozen sections allows better
visualization of tisue structures and permanence of the sections which can then be kept for future
review. Some of the sections were made from blocks which had been stored at tropical room
temperature for as long as 15 yrs, an indication that these methods can be used for
retrospective as well as prospective studies. By differentiating the various types of amyloidosis, the
laboratory can now contribute significantly to the selection of patients for appropriate therapy. Recent
reports have suggested that AA type amyloidosis may
respond favourably to colchicine22 and dimethyls ~ l p h o x i d e ,p~a~rt icularly if given before the
rapid deposition phase,24 whereas primary amyloidosis of the immunoglobulin type may respond to
mel~halan.~ Familial mediterranean fever and senile amyloidosis are uncommon in Malaysia and
have not been included in this study. Macular amyloidosis has also not been studied but its
immunohistochemical properties have been shown to be identical to that of lichen amyloidosis by
other workers. There are also suggestions that both macular amyloidosis and lichen amyloidosis are
variants of one disease. ACKNOWLEDGEMENT1S a m grateful to Mr Janson Emmanual and Mr M.
Y. Lim for technical assistance. This investigation was supported by research grant F66/83, University
of Malaysia

Transkate

Ringkasan

Deposito Amiloid dalam jaringan dari 8 pasien dengan amiloidosis primer umum, 11 pasien dengan
amiloidosis sekunder umum, 11 pasien karsinoma nasofaring, 11 karsinoma sel basal, 4 sel islet tumor,
4 karsinoma medulla tiroid dan 9 kasus lichen amiloidosis dipelajari menggunakan metode
Immunoperoxidase dan Peroksidase-antiperoxidase sebagai metode spesifik terhadap protein amiloid
A (AA) dan immunoglobulin kappa rantai ringan. Metode perrnanganate dari Wright juga diterapkan
pada bagian jaringan. Positif untuk protein AA hanya diamati dalam amiloidosis sekunder. Ada
korelasi yang sangat baik antara AA positif dan sensitivitas permanganat. Positif untuk
immunoglobulin rantai ringan tidak diamati dalam amiloidosis sekunder namun tercatat dalam 5
(63%) kasus primer amiloidosis dan 18-27% dari amiloidosis intratumour. Lichen amiloidosis tidak
menodai untuk protein AA atau rantai ringan. Hal ini menunjukkan bahwa penilaian terhadap reaksi
permanganat dan AA positif dari deposito amiloid dipercaya bisa membedakan sekunder dari
amiloidosis primer dan dapat memberikan kontribusi yang signifikan untuk terapi pada pasien yang
tepat.
Kata kunci: amiloid, amiloidosis, protein amiloid, protein AA, immunoperoxidase, reaksi
permanganat, immunoglobulin, rantai ringan Diterima 11 Juni 1985
PENDAHULUAN
Hal ini diketahui bahwa komponen protein utama dari amiloid fibril berbeda dalam berbagai jenis
amiloidosis. 'F 2 protein amiloid fibril primer dan amyloid yang terkait dengan dyscrasia sel plasma,
disebut Protein Amyloid Cahaya (Amyloid Light Chain), telah dernonstrated mengandung unit peptida
identik dengan daerah variabel amino-terminal dari rantai ringan. Amyloid fibril di amyloid sekunder
dan demam familial Fever Mediterania, bagaimanapun, sebagian besar terdiri dari protein amiloid A
(AA) yang tidak menyerupai immunglobulin. Deposito amiloid lokal ditemukan pada tumor endokrin
diyakini terkait dengan hormone peptida yang diproduksi, selain itu juga deposito amiloid lokal
berada di lapisan kutaneus kulit dan epitel tumor seperti karsinoma nasofaring dan karsinoma sel
basal mungkin berkaitan dengan keratin. Protein fibril dari penyakit Cardiac Amyloidosis senilis, ,
berbeda dengan deposito amiloid pikun di otak dan islet pankreas .Selain itu, berbagai jenis
amiloidosis lokal, masing-masing dengan protein fibril yang berbeda, dapat mempengaruhi penuaan
atau penyakit hati . Deposito amiloid hadir dalam otak pada penyakit Alzheimer baru-baru ini
menunjukkan mengandung prealbumin. Berbeda dengan protein fibril, protein globular komponen
amiloid P telah terbukti hadir dalam sebagian besar jenis amyloid, dengan kemungkinan pengecualian
dari amyloid intracerebral di penyakit Alzheimer . Studi terbaru telah mengungkapkan adanya
imunoglobulin dan C3 di beberapa arnyloid ~, 'p ~ a kulit rticularly lokal
amyloid, tetapi ini dianggap tidak menjadi bagian integral dari fibril.
Hal ini jelas bahwa kategorisasi amiloidosis oleh protein fibril yang akan memiliki peran penting pada
patogenesis, diagnosis dan terapi untuk penyakit. Namun, isolasi dan purifikasi protein fibril dari
deposito amiloid untuk menentukan sifat biokimia yang jelas tidak dalam kemampuan pada semua
laboratorium. Makalah ini menyajikan hasil investigasi untuk kehadiran protein AA dan
immunoglobulin rantai ringan di berbagai jenis amiloid menggunakan metode immunoperoxidase
pada formaiin-tetap, potongan jaringan paraffin. Korelasi antara temuan immunoperoxidase dan reaksi
permanganat deposito amiloid dipelajari dan praktis secara simple mendekati laboratorium untuk
penyelidikan dan klasifikasi amiloidosis yang disarankan.

BAHAN DAN METODE

Jenis amiloid yang diteliti adalah:
1. Arniloid primer menggunakan jaringan biopsi dari 8 pasien dengan umum
amiloidosis tidak dapat penyebabnya. Biopsi yang dari
rektum (3), ginjal (I), hati (I), limpa (I), jantung (I) dan paru-paru (I).
2. Amiloid sekunder menggunakan jaringan otopsi dari 10 Orang asli
(Malayan) dengan arnyloidosis umum terkait dengan pasien TBC dan 6 dengan amiloidosis umum
terkait kusta. Jaringan yang diteliti adalah dari ginjal (9). hati (4), jantung
(2) dan pankreas (1).
3. Localized intratumour amyloid, menggunakan bahan biopsi dari 1 I
karsinoma nasofaring, 11 karsinoma sel basal, 4 sel islet turnor dan 4 karsinoma medulla tiroid, di
mana terdapat intratumur stroma dari deposita arnyloid.
4. Amiloid likenifikasi menggunakan biopsi kulit dari 9 kasus lichen amiloidosis.
Semua jaringan yang diteliti ditetapkan dalam 10% buffered formalin dan ditanamkan dalam parafin. 4
m bagian tebal diwarnai dengan hematoxylin dan eosin, alkali Congo merah dan thioflavine-T. Selain
itu, juga diwarnai alkaline Congo merah setelah pengobatan sebelumnya dengan kalium permanganat
seperti yang dijelaskan oleh Wright et al.
Metode immunoperoxidase secara indirek untuk protein AA
Formalin-tetap, parafin-embedded bagian dari jaringan positif amyloid yang telah di deparaffini dan
dilapis dengan 0,5% hidrogen peroksida dalam metanol selama 30 menit. Kemudian dicuci dan
dilapis dengan 3% serum kelinci yang normal Setelah tip off, bagian yang dilapis diperoleh secara
komersial anti protein AA antiserum (Atlantic Laboratories), diencerkan 1: 160 di 3% NRS, dan
diinkubasi dalam ruang lembab pada suhu kamar selama 30 menit. Kemudian juga dicuci dengan
buffer fosfat saline (PBS) dan diinkubasi selama 30 menit dengan rabbit anti goat peroksidase,
diencerkan 1:20 dalam 3% NRS. Setelah mencuci ldilanjutkan dengan PBS, 0,05% 3, 3'diaminobenzidine tetrahydrochloride (substrat) ditambahkan. Bagian dicuci dengan hematoxylin .
Kontrol: Metode diulangi menggunakan serum kambing biasa bukan antiserum primer ( Protein
kambing anti AA antiserum).
Metode peroksidase antiperoxidase untuk imunoglobulin manusia lambda dan kappa rantai ringan.
Bagian yang deparaffini alkohol dan dilapis dengan 0,5% hidrogen peroksida dalam metanol selama
30 menit. Setelah mencuci dengan PBS, diperlakukan dengan 3% yang serum babi normal selama 20
menit. Setelah tip off, bagian yang dilapis diperoleh secara komersial antihuman kappa
immunoglobulin atau rantai lambda (Dako) diencerkan 1: 400 dan diinkubasi selama 30 menit dalam
ruang lembab pada suhu kamar. Bagian itu kemudian dibilas dengan PBS dan diinkubasi selama 30
menit dengan serum babi antirabbit IgG (Dako) diencerkan 1:20. Setelah cuci di PBS, kelinci
antihorseradish peroksidase complex (Dako) diencerkan 1: 50 diaplikasikan dan bagian diinkubasi
selama 30 menit. Bagian kemudian dicuci dengan PBS dan reaksi enzim dikembangkan dengan 0,05%

3,3 'tetrahydrochloride -diaminobenridine. Bagian dicuci, dengan hematoxylin dan dipasang di

Protexx.
Kontrol: Metode diulangi menggunakan serum kelinci normal bukan
dari antisera primer.
HASIL
Semua deposito amiloid muncul amorf dan eosinophilic pada rutinitas H & E noda. Mereka bernoda
pink sampai orange dengan basa Kongo merah dan dipamerkan birefringence apel hijau di bawah sinar
lintas-terpolarisasi. Ketika diobati dengan thioflavine-T dan dilihat di bawah sinar ultraviolet, mereka
menunjukkan fluoresensi keputihan-kuning. Ini adalah karakteristik yg mencat konvensional amiloid.
Reaksi perrnanganate kalium
Berbagai jenis amiloid berbeda dalam sensitivitas untuk kalium permanganat. Deposito amiloid
sekunder yang seragam sensitif terhadap kalium permanganat bahwa mereka kehilangan ketertarikan
untuk Kongo merah dan birefringence setelah pengobatan sebelumnya dengan kalium permanganat.
Sebaliknya, amiloid primer, lichen amiloid dan berbagai jenis amiloid intratumour resisten terhadap
permanganat tindakan dan dipertahankan baik Kongo afinitas merah dan birefringence. AA Protein
menggunakan metode immunoperoxidase tidak langsung, anti-AA antiserum bernoda positif dengan
deposito amiloid dari pasien dengan amiloidosis sekunder (Gambar 1 & 2), butfailed noda setiap
deposit amyloid primer, intratumour atau lumut amiloidosis. AA positif terjadi di lokasi yang sama
seperti Kongo positif merah. kontrol serum kambing normal tidak menunjukkan pewarnaan. Ketika
AA positif dibandingkan dengan sensitivitas permanganat, korelasi yang baik tercatat (Tabel 1).
deposito amiloid yang AA negatif resisten permanganat sementara mereka yang diwarnai positif
dengan anti-AA antiserum yang permanganate peka. rantai ringan Immunoglobulin Reaksi dari
berbagai jenis amiloid dengan antilambda dan anti-kappa antisera ditunjukkan pada Tabel 2. Lima dari
8 (63%) kasus amiloid primer memberikan reaksi positif bagi rantai lambda. Tak satu pun dari kasus
amiloidosis sekunder bernoda positif untuk rantai ringan. pewarnaan positif dengan salah satu atau
kedua rantai antisera cahaya diamati pada deposito di 27% dari karsinoma nasofaring, lebih dari 18%
dari karsinoma sel basal, 25% dari karsinoma meduler tiroid dan 25% dari tumor sel islet. Reaksireaksi ini, bagaimanapun, hanya lemah positif. rantai ringan gagal menjadi
terdeteksi di lichen amiloidosis. kontrol serum kelinci normal tidak menunjukkan pewarnaan.
DISKUSI
Klasifikasi amiloidosis telah mengalami beberapa revisi sejak pengakuan sebagai entitas penyakit pada
tahun 1851 oleh Virchow. Klasifikasi sebelumnya telah banyak
klinis. Namun, dalam beberapa kali, kemajuan pesat dalam penelitian amiloidosis telah berevolusi
konsep amiloidosis sebagai beta-fibrillosis, kimia dari betapleated
amyloid fibril berbeda dalam berbagai jenis amiloidosis. Mengingat banyak protein fibril dan protein
prekursor ditandai, nomenklatur protein fibril amiloid dibakukan dalam Simposium Internasional
Kedua Amiloidosis di Helsinki di
1975. Dalam Simposium Internasional Ketiga diadakan inPortugal pada tahun 1979, penambahan dan
modifikasi nomenklatur yang disepakati dan clinicochemical baru
skema klasifikasi diadopsi. "Klasifikasi ini telah menyebabkan pemahaman yang lebih baik dari
penyakit dan memberikan dasar untuk pemilihan pasien kemoterapi yang tepat. Namun, karena
karakterisasi protein amiloid fibril dengan ekstraksi protein adalah tugas yang sulit, pekerja kini

beralih ke teknik imunohistokimia untuk klasifikasi amiloidosis. penelitian ini telah menunjukkan
bahwa adalah mungkin untuk membedakan jenis AA (sekunder) amiloid andal dari beberapa jenis
utama lainnya dari amiloid dengan menggunakan immunoperoxidase dan permanganate metode pada
formalinfixed konvensional, parafin-embedded bagian jaringan. ada korelasi yang sangat baik antara
AA positif dan sensitivitas permanganat deposito amiloid. Kedua
reaksi ini hanya teramati pada deposito dari pasien yang terbukti memiliki baik tuberculosi ~ '~ atau
kusta dan dengan demikian diterima sebagai menderita amiloidosis sekunder. Namun, reaksi untuk
rantai ringan tidak konsisten dalam banyak deposito diharapkan dari AL (primer) ketik gagal noda
untuk rantai ringan. Ini bisa jadi karena rantai cahaya yang terlibat dalam kasus-kasus individu
amiloidosis yang idiotypic. Dengan demikian, pewarnaan untuk rantai ringan tampaknya tidak berguna
dalam membedakan berbagai jenis amiloid. Disarankan bahwa prosedur investigasi histopatologi
berguna untuk mengklasifikasikan amiloidosis akan menilai positif AA dan reaksi permanganat dari
deposito. Reaksi-reaksi ini histokimia, bersama-sama dengan pertimbangan fitur patologis lain dari
kasus yang diteliti (misalnya apakah amiloidosis adalah
lokal, umum atau intratumour) harus cukup dalam kebanyakan kasus untuk membedakan berbagai
jenis amiloid. The immunoperoxidase dan permanganat metode yang cukup nyaman dan mudah untuk
melaksanakan and140 Loo [memiliki beberapa keunggulan dibandingkan teknik immunofluorescence
digunakan di awal studies.20 * 2T1 ia menggunakan dari paraffinembedded bukan bagian beku
memungkinkan visualisasi yang lebih baik dari struktur tisue dan permanen dari bagian yang
kemudian dapat disimpan untuk meninjau masa depan. Beberapa bagian dibuat dari blok yang telah
disimpan pada suhu kamar tropis selama 15 thn, sebuah indikasi bahwa metode ini dapat digunakan
untuk
retrospektif serta studi prospektif. Dengan membedakan berbagai jenis amiloidosis, laboratorium
sekarang dapat memberikan kontribusi signifikan terhadap pemilihan pasien untuk terapi yang tepat.
Laporan terbaru menunjukkan bahwa jenis AA amiloidosis mungkin
merespon positif untuk colchicine22 dan dimethyls ~ lphoxide, p ~ a ~ rt icularly jika diberikan
sebelum tahap deposisi cepat, 24 sedangkan amiloidosis utama dari jenis imunoglobulin dapat
menanggapi mel ~ halan. ~ 'demam Mediterania familial dan amiloidosis pikun jarang terjadi di
Malaysia dan belum dimasukkan dalam penelitian ini. amiloidosis makula juga belum diteliti tetapi
sifat imunohistokimia yang telah terbukti identik dengan lichen amiloidosis oleh pekerja lainnya. "Ada
juga saran yang baik amiloidosis makula dan lichen amiloidosis adalah varian dari satu penyakit.
ACKNOWLEDGEMENT1S m berterima kasih kepada Mr Janson Emmanual dan Mr M. Y. Lim
untuk bantuan teknis. Penelitian ini didukung oleh penelitian hibah F66 / 83, University of Malaysia