Increased Blood Concentration of IgG Degradation Products in Prostate Cancer


如何引用文章

全文:

开放存取 开放存取
受限制的访问 ##reader.subscriptionAccessGranted##
受限制的访问 订阅存取

详细

For elucidation of the mechanisms of IgG binding with human plasminogen in prostate cancer patients, we propose an original ELISA on polystyrene plates with immobilized heavy and light plasminogen chains. The level of IgG bound to plasminogen heavy chain in the serum of prostate cancer patients significantly exceeded that in healthy volunteers. IgG treated with plasmin more actively (by more than 2 times) bound plasminogen heavy chain than intact IgG. These findings indicate the involvement of lysine-binding sites of plasminogen heavy chain in the interaction with the C-terminal lysine of IgG and their fragments. ROC analysis of ELISA data showed significant differences between serum samples from patients with prostate cancer and benign prostatic hyperplasia. It is hypothesized that IgG in the tumor region undergo proteolysis and their products appear in the circulation.

作者简介

I. Goufman

Research Institute of Human Morphology

编辑信件的主要联系方式.
Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

V. Yakovlev

Angiogen Company

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

N. Tikhonova

Research Institute of Human Morphology

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

K. Matevosyan

Research Institute of Human Morphology

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

M. Boltovskaya

Research Institute of Human Morphology

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

R. Aisina

M. V. Lomonosov Moscow State University

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

L. Mukhametova

M. V. Lomonosov Moscow State University

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow

K. Gershkovich

N. M. Emanuel Institute for Biochemical Physics, Russian Academy of Sciences

Email: eugene_goufman@mail.ru
俄罗斯联邦, Moscow


版权所有 © Springer Science+Business Media, LLC, part of Springer Nature, 2019
##common.cookie##