(Pro)renin receptor and prorenin: their plausible sites of interaction.

نویسندگان

  • A H M Nurun Nabi
  • Kazal Boron Biswas
  • Yoshie Arai
  • Tsutomu Nakagawa
  • Akio Ebihara
  • Laila N Islam
  • Fumiaki Suzuki
چکیده

Before discovery of (pro)renin receptor, prorenin was regarded as a source of renin and probable diagnostic marker for diabetic nephropathy/Wilms' tumor. It is now considered that prorenin can perform renin activity by binding to (P)RR and binding mechanism of (pro)renin to (P)RR was indicated in many in vitro studies. Considering the physiological importance and pathological involvement of (P)RR, it is indeed a demand of time to determine the three dimensional structure of (P)RR to design (P)RR blocker(s) effective for (pro)renin. It may also facilitate to explain the incompatible data about the effective application of decoy peptide as (P)RR blocker. So far, studies have discussed the bindings of (pro)renin to (P)RR using peptides mimicking the structures of ligands (e.g., the decoy including "handle" region peptide, the "hinge" peptide etc). In this review, the binding mechanism of ligands has been highlighted from the structural aspect of (P)RR using several anti-(P)RR antibodies designed from the primary structure of (pro)renin receptor. Therefore, this review would give us a clue regarding the plausible binding region(s) for prorenin in the (P)RR.

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

Renin and Prorenin Renin- and Prorenin-Induced Effects in Rat Vascular Smooth Muscle Cells Overexpressing the Human (Pro)Renin Receptor Does (Pro)Renin-(Pro)Renin Receptor Interaction Actually Occur?

Renin/prorenin binding to the (pro)renin receptor ([P]RR) results in direct (angiotensin-independent) secondmessenger activation in vitro, whereas in vivo studies in rodents overexpressing prorenin ( 400-fold) or the (P)RR do not support such activation. To solve this discrepancy, DNA synthesis, extracellular signal–regulated kinase 1/2 phosphorylation, and plasminogen-activator inhibitor 1 rel...

متن کامل

Editorial Commentary ( Pro ) renin Receptor and Vacuolar H - ATPase

The discovery of a “(pro)renin receptor”1 has renewed the interest in prorenin, the inactive precursor of renin. Prorenin binding to this receptor allows prorenin to display enzymatic activity without the accompanying cleavage of the prosegment that normally occurs in the kidney when prorenin is converted to renin. The underlying concept is that binding to the (pro)renin receptor induces a conf...

متن کامل

( Pro ) renin Receptor and Vacuolar H - ATPase

The discovery of a “(pro)renin receptor”1 has renewed the interest in prorenin, the inactive precursor of renin. Prorenin binding to this receptor allows prorenin to display enzymatic activity without the accompanying cleavage of the prosegment that normally occurs in the kidney when prorenin is converted to renin. The underlying concept is that binding to the (pro)renin receptor induces a conf...

متن کامل

(Pro)renin and its receptors: pathophysiological implications.

Tissue angiotensin generation depends on the uptake of circulating (kidney-derived) renin and/or its precursor prorenin [together denoted as (pro)renin]. Since tissue renin levels are usually somewhat higher than expected based upon the amount of (renin-containing) blood in tissue, an active uptake mechanism has been proposed. Several candidates have been evaluated in the past three decades, in...

متن کامل

Critical review of prorenin and (pro)renin receptor research.

The renin-angiotensin system (RAS) plays an important role in cardiovascular and renal physiology and disease, and the benefits of angiotensin-converting enzyme inhibitor, angiotensin type 1 receptor blocker, and renin inhibitor therapies are mediated in part by their modification of the levels and actions of angiotensin peptides. Despite its long history, the RAS remains an active area of rese...

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:
  • Frontiers in bioscience

دوره 17  شماره 

صفحات  -

تاریخ انتشار 2012