Lysosomal enzymes in human urine: evidence for polymorphonuclear leucocyte proteinase involvement in the pathogenesis of human glomerulonephritis.

نویسندگان

  • E Sanders
  • G A Coles
  • M Davies
چکیده

1. Lysosomal proteinase activity was assayed in human cadaver kidney, urine, granules from poly­ morphonuclear leucocytes of normal persons, and urine samples from 154 patients with renal disease. 2. Granules from polymorphonuclear leuco­ cytes showed proteinase activity at acid and neutral pH, whereas cadaver kidney showed proteinase activity at acid pH only. 3. The urine from 13 patients with glomerulo­ nephritis showed proteinase activity at both acid and neutral pH as well as increased amounts of antigenic glomerular basement membrane frag­ ments. The properties of the urinary proteinases suggested that they had originated in polymorpho­ nuclear leucocytes. 4. Only the urine samples containing these proteinases were capable of degrading isolated human glomerular basement membrane in vitro. 5. Clinical recovery, where it occurred, was ac­ companied by the disappearance of urinary proteinase activity, and reduction in glomerular basement membrane antigen excretion.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The degradation of human glomerular basement membrane with purified lysosomal proteinases: evidence for the pathogenic role of the polymorphonuclear leucocyte in glomerulonephritis.

1. Human polymorphonuclear leucocyte elastase and cathepsin G were incubated with preparations of isolated human glomerular basement membrane at neutral pH and 37 degrees C. 2. The ability of these enzymes to degrade glomerular basement membrane was followed by the release of hydroxyproline. Both proteinases released considerable amounts of hydroxyproline. 3. By using Sephadex G-100 it was show...

متن کامل

EXPRESSION OF HUMAN PROTEINASE 3 IN CHINESE HAMSTER OVARY CELLS (CHO-CELLS)

Proteinase 3(PR3) is a human polymorphonuclear leukocyte serine proteinase and is the main target antigen for antineutrophil cytoplasmic antibodies (ANCA) found in Wegener's granulomatosis (WG). We developed a stable expression system for conformationally intact recombinant PR3 (rPR3) in Chinese hamster ovary cells (CHO-cells). The part of PR3 cDNA that encoded the active form of PR3 was s...

متن کامل

Perfluorooctanesulfonate (PFOS) Induces Apoptosis Signaling and Proteolysis in Human Lymphocytes through ROS Mediated Mitochondrial Dysfunction and Lysosomal Membrane Labialization

Perfluorinated compounds (PFCs) such as perfluorooctanesulfonate (PFOS) are stable chemicals that accumulate in biological matrix. Toxicity of these compounds including immunotoxicity has been demonstrated in experimental models and wildlife. Although limited number of studies examined the effects of PFOS on human lymphocytes but so far no research has investigated the complete mechanisms of PF...

متن کامل

Molecular Epidemiology of Human Papillomavirus in Pterygium

Abstract Background and Objective: Ophthalmic pterygium is a potentially vision-threatening lesion of unknown etiology that often extends on the corneal surface and has a worldwide distribution. Despite various studies, the pathogenesis of pterygium remains unclear and the involvement of human papillomavirus is controversial. We aimed to investigate the involvement of papillomavirus in pte...

متن کامل

Perfluorooctanesulfonate (PFOS) Induces Apoptosis Signaling and Proteolysis in Human Lymphocytes through ROS Mediated Mitochondrial Dysfunction and Lysosomal Membrane Labialization

Perfluorinated compounds (PFCs) such as perfluorooctanesulfonate (PFOS) are stable chemicals that accumulate in biological matrix. Toxicity of these compounds including immunotoxicity has been demonstrated in experimental models and wildlife. Although limited number of studies examined the effects of PFOS on human lymphocytes but so far no research has investigated the complete mechanisms of PF...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Clinical science and molecular medicine

دوره 54 6  شماره 

صفحات  -

تاریخ انتشار 1978