Journal
REGULATORY PEPTIDES
Volume 122, Issue 2, Pages 119-129Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.regpep.2004.06.008
Keywords
EGF; growth factor precursor; kallikrein; kidney; protease; secretion
Categories
Ask authors/readers for more resources
Epidermal growth factor (EGF) is present in kidney membranes as an integral type I precursor protein, enzymatically processed to release immunoreactive materials in urine or incubation medium. The aim of this work was the elucidation of both the anchor of the serine protease activity that processes pro-EGF, and the determination of the steps of the enzymatic processing. Quantification of EGF containing molecules by RIA following gel filtration analysis demonstrated that the membrane precursor is first shed from the kidney membrane principally into a 170-kDa soluble precursor. This entire ectodomain is further processed into a 70-kDa precursor and finally into the mature 5.9 kDa urinary EGF. These species correspond to the ones found in urines. Both shedding and maturation events are clearly realized by membrane anchored serine protease activity, which remains active in detergent. By use of wild-type and knockout mice urines, we found that tissue kallikrein (TK) was not involved in the regulation of this processing. (C) 2004 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available