Tissue Specificity of Human Angiotensin I-Converting Enzyme

人类血管紧张素转换酶的组织特异性

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作者:Olga V Kryukova, Victoria E Tikhomirova, Elena Z Golukhova, Valery V Evdokimov, Gavreel F Kalantarov, Ilya N Trakht, David E Schwartz, Randal O Dull, Alexander V Gusakov, Igor V Uporov, Olga A Kost, Sergei M Danilov

Background

Angiotensin-converting enzyme (ACE), which metabolizes many peptides and plays a key role in blood pressure regulation and vascular remodeling, as well as in reproductive functions, is expressed as a type-1 membrane glycoprotein on the surface of endothelial and epithelial cells. ACE also presents as a soluble form in biological fluids, among which seminal fluid being the richest in ACE content - 50-fold more than that in blood.

Conclusions

Dramatic differences in the local conformations of seminal fluid and lung ACEs, as well as the effects of ACE-binding partners on mAbs binding to these ACEs, suggest different regulation of ACE functions and shedding from epithelial cells in epididymis and prostate and endothelial cells of lung capillaries. The differences in local conformation of ACE could be the base for the generation of mAbs distingushing tissue-specific ACEs.

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