New capacities of the diagnosis and monitoring of the course of AL-amyloidosis
- 作者: Rameyev V1, Kozlovskaya L2, Kogarko I3, Kogarko B3
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隶属关系:
- I. M. Sechenov Moscow Medical
- I. M. Sechenov Moscow MedicalResearch Center, I. M. Sechenov Moscow Medical Academy
- N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow
- 期: 卷 82, 编号 6 (2010)
- 页面: 29-32
- 栏目: Editorial
- URL: https://journals.rcsi.science/0040-3660/article/view/30597
- ID: 30597
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Subjects and methods. The content of free ILCs was studied by a nephelometric technique after their fixation in the blood of 31 patients with AL amyloidosis; monoclonal gammapathy was associated with the hyperproduction of monoclonal ILCs of λ- and κ-type in 14 and 17 patients, respectively. The obtained value was compared with the data of physical examination and laboratory and instrumental studies indicating lesions to target organs and with the course of the disease.
Results. In patients with the good course of AL amyloidosis, the average level of free ILCs was 1.8 (range 0.77-3) times greater than the normal values (the range of ILCs of λ and k-type was 20.24 to 67.4 and 20.14 to 81.38 mg/l, respectively); in those with the poor course, the excess of ILCs was 5.8 (range 3.7-13) times higher than the normal values (the range of ILCs of λ and κ-type was 54.32 to 286.7 and 117.06 to 2606.0 mg/l, respectively). The optimal range of diagnostic sensitivity (75%) and specificity (75%) in the estimation of prognosis was determined at the ILC levels that were three times greater (64.5 mg/l for κ-ILCs and 80 mg/l for λ-ILCs). Among the patients with a blood free ILC level of m 3 times more than the normal values, the good and poor courses of AL amyloidosis were noted in 13 and 4 cases, respectively.
Conclusion. The determination of serum ILC concentration by the Freelite method may be used to diagnose AL amyloidosis and to specify the presence of appropriate organ dysfunction; this study over time makes it possible to monitor the course of the disease and to estimate its response to therapy.
作者简介
V Rameyev
I. M. Sechenov Moscow Medical
Email: vvrameev@mtu-net.ru
Кафедра терапии профболезнейотдел нефрологииканд. мед. наук, ассистентвед. науч. сотр; ММА им. И. М. СеченоваНаучно-исследовательский центр ММА им. И. М. Сеченова; I. M. Sechenov Moscow Medical
L Kozlovskaya
I. M. Sechenov Moscow MedicalResearch Center, I. M. Sechenov Moscow Medical AcademyКафедра терапии профболезнейд-р мед. наук, проф; ММА им. И. М. Сеченова; I. M. Sechenov Moscow MedicalResearch Center, I. M. Sechenov Moscow Medical Academy
I Kogarko
N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, MoscowN. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow
B Kogarko
N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, MoscowN. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow
参考
- Glenner G. G., Terry W., Harada M. et al. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analysis. Science 1971; 172: 1150-1151.
- Sipe J. D., ed. Amyloid proteins. The beta sheet conformation and disease. Chichester: WILEY-VCH; 2005.
- Bradwell A. R. Serum free light chain analysis. 4-th ed. Birmingham: The Binding Site Ltd; 2006.