Catecholamine-synthesizing enzymes in the adult and prenatal human testis.
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Catecholamine-synthesizing enzymes in the adult and prenatal human testis. / Davidoff, Michail S; Ungefroren, Hendrik; Middendorff, Ralf; Koeva, Yvetta; Bakalska, Mariana; Atanassova, Nina; Holstein, Adolf-Friedrich; Jezek, Davor; Pusch, Wolfgang; Müller, Dieter.
in: HISTOCHEM CELL BIOL, Jahrgang 124, Nr. 3-4, 3-4, 2005, S. 313-323.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - Catecholamine-synthesizing enzymes in the adult and prenatal human testis.
AU - Davidoff, Michail S
AU - Ungefroren, Hendrik
AU - Middendorff, Ralf
AU - Koeva, Yvetta
AU - Bakalska, Mariana
AU - Atanassova, Nina
AU - Holstein, Adolf-Friedrich
AU - Jezek, Davor
AU - Pusch, Wolfgang
AU - Müller, Dieter
PY - 2005
Y1 - 2005
N2 - Catecholamines play functional roles in the mature and developing mammalian testis but the cell types responsible for their local synthesis are still controversially discussed. Here, we demonstrate that four enzymes involved in the biosynthesis of catecholamines, namely, tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), dopamine beta-hydroxylase (DBH) and phenylethanolamine- N-methyltransferase (PNMT), are expressed in Leydig cells of the human testis. Tyrosine hydroxylase, the key enzyme of the biosynthesis of catecholamines, was localized to Leydig cells both at the transcript level (by RT-PCR analyses and by in situ hybridization assays) and at the protein level (by immunoblotting and by immunohistochemistry). The other enzymes were also demonstrated in Leydig cells by RT-PCR and immunohistochemical analyses. The presence of TH, AADC, DBH, and PNMT in human Leydig cells was found, in addition, by immunohistochemical approaches carried out on sections from prenatal human testes. Thus, the present study identifies the Leydig cells as the presumed sites of catecholamine production in both the mature and fetal human testes and further supports the previously recognized neuroendocrine characteristics of this cell type.
AB - Catecholamines play functional roles in the mature and developing mammalian testis but the cell types responsible for their local synthesis are still controversially discussed. Here, we demonstrate that four enzymes involved in the biosynthesis of catecholamines, namely, tyrosine hydroxylase (TH), aromatic amino acid decarboxylase (AADC), dopamine beta-hydroxylase (DBH) and phenylethanolamine- N-methyltransferase (PNMT), are expressed in Leydig cells of the human testis. Tyrosine hydroxylase, the key enzyme of the biosynthesis of catecholamines, was localized to Leydig cells both at the transcript level (by RT-PCR analyses and by in situ hybridization assays) and at the protein level (by immunoblotting and by immunohistochemistry). The other enzymes were also demonstrated in Leydig cells by RT-PCR and immunohistochemical analyses. The presence of TH, AADC, DBH, and PNMT in human Leydig cells was found, in addition, by immunohistochemical approaches carried out on sections from prenatal human testes. Thus, the present study identifies the Leydig cells as the presumed sites of catecholamine production in both the mature and fetal human testes and further supports the previously recognized neuroendocrine characteristics of this cell type.
M3 - SCORING: Zeitschriftenaufsatz
VL - 124
SP - 313
EP - 323
JO - HISTOCHEM CELL BIOL
JF - HISTOCHEM CELL BIOL
SN - 0948-6143
IS - 3-4
M1 - 3-4
ER -
