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Inactive renin--a renin proenzyme?

B J Leckie, A McConnell, J Jordan

Advances in Experimental Medicine and Biology

|January 1, 1977

Summary

This summary is machine-generated.

Inactive renin in human plasma, with a higher molecular weight, can be activated by acid or trypsin, similar to findings in rabbit kidneys. This suggests a potential proenzyme form of renin.

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Area of Science:

Biochemistry
Renal Physiology

Background:

Human plasma contains an inactive renin form (55,000 m.w.) distinct from active renin (40,000 m.w.).
Inactive renin activation mechanisms are not fully understood.

Purpose of the Study:

To investigate the properties and potential activation pathways of inactive human renin.
To compare inactive human renin with findings in other species, such as rabbit kidneys.

Main Methods:

Analysis of human plasma and kidney extracts.
Acidification to pH 3.0 and incubation with trypsin to assess renin activity and molecular weight changes.

Main Results:

Acidification (pH 3.0) or trypsin treatment activated inactive plasma renin, reducing its molecular weight to that of active renin.

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Acidification also increased renin concentration in human kidney extracts.

Inactive renin in human kidneys may be activated by removal of an acid-labile inhibitor, similar to rabbit kidney renin.

Conclusions:

Human plasma contains an inactive renin form that can be converted to an active form.
The findings suggest that inactive renin may be a proenzyme or associated with an inhibitor.
Further research is needed to confirm the proenzyme nature of inactive renin.