Literature DB >> 9815277

Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord.

S E Reznik1, C M Salafia, J M Lage, L D Fricker.   

Abstract

Carboxypeptidase E (CPE) is highly concentrated in neuroendocrine tissues and is the only carboxypeptidase detected in mature secretory vesicles. Carboxypeptidase D (CPD), a carboxypeptidase with CPE-like activity, is widely distributed in tissues and is present in the trans-Golgi network. Previous work had shown that both CPE and CPD are expressed in the human placenta and that CPD is expressed at much higher levels than CPE. The present work provides evidence for the co-localization of CPE and CPD to basal plate extravillous trophoblasts and maternal uteroplacental vascular endothelial cells, chorionic villous endothelial cells, amnionic epithelial cells, and umbilical venous and arterial smooth muscle cells. Whereas the intensity of CPD immunostaining is similar in the placenta and umbilical cord, CPE staining in the placenta is much weaker than in the umbilical cord, suggesting that CPD plays a more important role in the processing of placental peptides. Immunoelectron microscopy of umbilical venous smooth muscle cells shows subcellular localization of both enzymes to the rough endoplasmic reticulum. In addition, CPE is present just subjacent to the cell membrane. The difference in cellular and subcellular localization between the two enzymes indicates that they perform distinct functions in the processing of placental peptides and proteins.

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Year:  1998        PMID: 9815277     DOI: 10.1177/002215549804601204

Source DB:  PubMed          Journal:  J Histochem Cytochem        ISSN: 0022-1554            Impact factor:   2.479


  8 in total

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6.  Carboxypeptidase E in rat antropyloric mucosa: distribution in progenitor and mature endocrine cell types.

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Review 7.  Dissecting carboxypeptidase E: properties, functions and pathophysiological roles in disease.

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8.  Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains.

Authors:  Javier Garcia-Pardo; Sebastian Tanco; Lucía Díaz; Sayani Dasgupta; Juan Fernandez-Recio; Julia Lorenzo; Francesc X Aviles; Lloyd D Fricker
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  8 in total

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