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Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid.

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Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid. / Rylett, Caroline M.; Walker, Michael J.; Howell, Gareth J. et al.
In: Journal of Experimental Biology, Vol. 210, No. 20, 15.10.2007, p. 3601-3606.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

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Rylett CM, Walker MJ, Howell GJ, Shirras AD, Isaac RE. Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid. Journal of Experimental Biology. 2007 Oct 15;210(20):3601-3606. doi: 10.1242/jeb.009035 This Article

Author

Rylett, Caroline M. ; Walker, Michael J. ; Howell, Gareth J. et al. / Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid. In: Journal of Experimental Biology. 2007 ; Vol. 210, No. 20. pp. 3601-3606.

Bibtex

@article{205a9efbd3f0408c874e4612d8f25925,
title = "Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid.",
abstract = "Angiotensin I-converting enzyme (ACE) expressed on the surface of endothelial cells is responsible for the last step in the synthesis of circulating angiotensin II and the inactivation of bradykinin. Mammalian ACE is also expressed in the prostate with other components of the renin–angiotensin system, and in developing spermatids, where the peptidase activity is known to be critical for normal sperm function. The importance of an ACE gene to male fertility has also been demonstrated in Drosophila melanogaster, where Ance is expressed in spermatids, and hypomorphic alleles of Ance cause a defect in spermiogenesis. Here we show that ANCE, which shares many enzymatic properties with mammalian ACE, is also a product of the male accessory gland of D. melanogaster. It is expressed in the secondary cells and is associated with the electron dense granule within the large vesicles of these cells. ACE proteolytic activity is lost from the accessory glands during mating, consistent with transfer to the mated female in the seminal fluid. The accessory gland ACE-like activity might have an evolutionarily conserved function processing biologically active peptides with a role in male fertility.",
keywords = "Drosophila, male accessory gland, angiotensin I-converting enzyme, dicarboxypeptidase, ANCE",
author = "Rylett, {Caroline M.} and Walker, {Michael J.} and Howell, {Gareth J.} and Shirras, {Alan D.} and Isaac, {R. Elwyn}",
year = "2007",
month = oct,
day = "15",
doi = "10.1242/jeb.009035 This Article",
language = "English",
volume = "210",
pages = "3601--3606",
journal = "Journal of Experimental Biology",
issn = "0022-0949",
publisher = "Company of Biologists Ltd",
number = "20",

}

RIS

TY - JOUR

T1 - Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid.

AU - Rylett, Caroline M.

AU - Walker, Michael J.

AU - Howell, Gareth J.

AU - Shirras, Alan D.

AU - Isaac, R. Elwyn

PY - 2007/10/15

Y1 - 2007/10/15

N2 - Angiotensin I-converting enzyme (ACE) expressed on the surface of endothelial cells is responsible for the last step in the synthesis of circulating angiotensin II and the inactivation of bradykinin. Mammalian ACE is also expressed in the prostate with other components of the renin–angiotensin system, and in developing spermatids, where the peptidase activity is known to be critical for normal sperm function. The importance of an ACE gene to male fertility has also been demonstrated in Drosophila melanogaster, where Ance is expressed in spermatids, and hypomorphic alleles of Ance cause a defect in spermiogenesis. Here we show that ANCE, which shares many enzymatic properties with mammalian ACE, is also a product of the male accessory gland of D. melanogaster. It is expressed in the secondary cells and is associated with the electron dense granule within the large vesicles of these cells. ACE proteolytic activity is lost from the accessory glands during mating, consistent with transfer to the mated female in the seminal fluid. The accessory gland ACE-like activity might have an evolutionarily conserved function processing biologically active peptides with a role in male fertility.

AB - Angiotensin I-converting enzyme (ACE) expressed on the surface of endothelial cells is responsible for the last step in the synthesis of circulating angiotensin II and the inactivation of bradykinin. Mammalian ACE is also expressed in the prostate with other components of the renin–angiotensin system, and in developing spermatids, where the peptidase activity is known to be critical for normal sperm function. The importance of an ACE gene to male fertility has also been demonstrated in Drosophila melanogaster, where Ance is expressed in spermatids, and hypomorphic alleles of Ance cause a defect in spermiogenesis. Here we show that ANCE, which shares many enzymatic properties with mammalian ACE, is also a product of the male accessory gland of D. melanogaster. It is expressed in the secondary cells and is associated with the electron dense granule within the large vesicles of these cells. ACE proteolytic activity is lost from the accessory glands during mating, consistent with transfer to the mated female in the seminal fluid. The accessory gland ACE-like activity might have an evolutionarily conserved function processing biologically active peptides with a role in male fertility.

KW - Drosophila

KW - male accessory gland

KW - angiotensin I-converting enzyme

KW - dicarboxypeptidase

KW - ANCE

U2 - 10.1242/jeb.009035 This Article

DO - 10.1242/jeb.009035 This Article

M3 - Journal article

VL - 210

SP - 3601

EP - 3606

JO - Journal of Experimental Biology

JF - Journal of Experimental Biology

SN - 0022-0949

IS - 20

ER -