Premenstrual Disappearance of Aminopeptidase A in Endometrial Stromal Cells around Endometrial Spiral Arteries/Arterioles during the Decidual Change
Aminopeptidase A (APA, BP-1) is a membrane-bound zinc metallopeptidase that converts angiotensin II (AngII) into AngIII by selectively hydrolyzing the N-terminal aspartyl residue. AngII has been proposed as a candidate for the initial vasoconstrictor of endometrial spiral arteries/arterioles in the...
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Published in | The journal of clinical endocrinology and metabolism Vol. 87; no. 5; pp. 2303 - 2309 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
Endocrine Society
01.05.2002
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Abstract | Aminopeptidase A (APA, BP-1) is a membrane-bound zinc metallopeptidase that converts angiotensin II (AngII) into AngIII by selectively hydrolyzing the N-terminal aspartyl residue. AngII has been proposed as a candidate for the initial vasoconstrictor of endometrial spiral arteries/arterioles in the preliminary step of menstruation. In the late secretory phase, endometrial stromal cells (ESC) around the blood vessels begin to differentiate into decidual cells, and AngII has been reported to accumulate around such vessels. However, whether there is a concurrent increase in renin or angiotensin-converting enzyme in this area has not been determined. We hypothesized that APA may be involved in the metabolism of AngII in the cycling endometrium.
Western blot analysis in the present study demonstrated that a considerable amount of APA was present in the secretory phase endometrium. ESC in the secretory phase showed strong expression of APA by immunohistochemical analysis and of APA mRNA by in situ hybridization. In contrast, both APA mRNA and protein were absent in decidual cells. The enzyme activity and the biosynthesis of [35S]methionine-labeled APA significantly decreased during the in vitro decidualization of cultured ESC.
These results suggest that the perivascular disappearance of APA is a differentiation-specific change that occurs along with the decidualization, and that the disappearance of APA might accelerate the accumulation of AngII around the vessels. |
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AbstractList | Aminopeptidase A (APA, BP-1) is a membrane-bound zinc metallopeptidase that converts angiotensin II (AngII) into AngIII by selectively hydrolyzing the N-terminal aspartyl residue. AngII has been proposed as a candidate for the initial vasoconstrictor of endometrial spiral arteries/arterioles in the preliminary step of menstruation. In the late secretory phase, endometrial stromal cells (ESC) around the blood vessels begin to differentiate into decidual cells, and AngII has been reported to accumulate around such vessels. However, whether there is a concurrent increase in renin or angiotensin-converting enzyme in this area has not been determined. We hypothesized that APA may be involved in the metabolism of AngII in the cycling endometrium. Western blot analysis in the present study demonstrated that a considerable amount of APA was present in the secretory phase endometrium. ESC in the secretory phase showed strong expression of APA by immunohistochemical analysis and of APA mRNA by in situ hybridization. In contrast, both APA mRNA and protein were absent in decidual cells. The enzyme activity and the biosynthesis of [(35)S]methionine-labeled APA significantly decreased during the in vitro decidualization of cultured ESC. These results suggest that the perivascular disappearance of APA is a differentiation-specific change that occurs along with the decidualization, and that the disappearance of APA might accelerate the accumulation of AngII around the vessels. Aminopeptidase A (APA, BP-1) is a membrane-bound zinc metallopeptidase that converts angiotensin II (AngII) into AngIII by selectively hydrolyzing the N-terminal aspartyl residue. AngII has been proposed as a candidate for the initial vasoconstrictor of endometrial spiral arteries/arterioles in the preliminary step of menstruation. In the late secretory phase, endometrial stromal cells (ESC) around the blood vessels begin to differentiate into decidual cells, and AngII has been reported to accumulate around such vessels. However, whether there is a concurrent increase in renin or angiotensin-converting enzyme in this area has not been determined. We hypothesized that APA may be involved in the metabolism of AngII in the cycling endometrium. Western blot analysis in the present study demonstrated that a considerable amount of APA was present in the secretory phase endometrium. ESC in the secretory phase showed strong expression of APA by immunohistochemical analysis and of APA mRNA by in situ hybridization. In contrast, both APA mRNA and protein were absent in decidual cells. The enzyme activity and the biosynthesis of [35S]methionine-labeled APA significantly decreased during the in vitro decidualization of cultured ESC. These results suggest that the perivascular disappearance of APA is a differentiation-specific change that occurs along with the decidualization, and that the disappearance of APA might accelerate the accumulation of AngII around the vessels. |
Author | Itakura, Atsuo Toda, Shigeru Nomura, Masao Kotani, Yoshiaki Ando, Hisao Murata, Yasutaka Nagasaka, Tetsuro Tsukahara, Shin-Ichiro Mizutani, Shigehiko |
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SubjectTerms | Adult Aminopeptidases - genetics Aminopeptidases - metabolism Arteries Arterioles Biological and medical sciences Cells, Cultured Decidua - physiology Endometrium - blood supply Endometrium - cytology Endometrium - enzymology Female Fundamental and applied biological sciences. Psychology Glutamyl Aminopeptidase Hormone metabolism and regulation Humans Immunohistochemistry In Situ Hybridization Mammalian male genital system Medical sciences Menstruation - metabolism Nephrology. Urinary tract diseases Nephropathies. Renovascular diseases. Renal failure Renovascular diseases RNA, Messenger - metabolism Stromal Cells - enzymology Vertebrates: reproduction |
Title | Premenstrual Disappearance of Aminopeptidase A in Endometrial Stromal Cells around Endometrial Spiral Arteries/Arterioles during the Decidual Change |
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