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F Leenders

Publications and source records attributed to F Leenders.

30 records · Page 2Linked to original sources
PubMed1995

The organelles containing porcine 17 beta-estradiol dehydrogenase are peroxisomes.

Porcine 17 beta-estradiol dehydrogenase was recently purified and cloned. It catalyzes the NAD(+)-dependent oxidation of estradiol to estrone 360-fold more efficiently than the reverse reaction with NADPH. Immunogold electron microscopy localizes 17 beta-estradiol dehydrogenase in organelles of 120 to 500 nm with moderate electron-dense matrices bounded by single membranes. Antibodies against the peroxisomal markers catalase and acyl-CoA oxidase recognize the same organelles in double-labeling studies. This is the first report on the participation of peroxisomes in the metabolism of estradiol.

Acyl-CoA Oxidase↗
PubMed1994

Molecular cloning and amino acid sequence of the porcine 17 beta-estradiol dehydrogenase.

We describe the cloning and sequencing of porcine 17 beta-estradiol dehydrogenase. The enzyme performs oxidation 360-fold more efficiently than reduction, both measured under optimal conditions. It is localized in specialized vesicles of epithelial cells. The cDNA clones were isolated from a lambda UNI ZAP XR library of porcine kidney and polymerase-chain-reaction-amplified from templates of uterus epithelium. In both tissues, the same enzyme is coded by a transcript of 2.9 kb. It contains a 69-b 5'-noncoding region, an open reading frame of 2211 b and a 3'-noncoding region of 624 b. The open reading frame of 737 amino acids with a predicted molecular mass 79,973 Da was confirmed by amino acid sequencing of peptides. The 80-kDa translation product is processed to the N-terminal 32-kDa enzyme, part of which is then covalently linked to actin. The estradiol dehydrogenase/actin complex and the 80-kDa translation product comigrate in SDS/PAGE.

Amino Acid Sequence↗
PubMed1994

The sequence of porcine 80 kDa 17 beta-estradiol dehydrogenase reveals similarities to the short chain alcohol dehydrogenase family, to actin binding motifs and to sterol carrier protein 2.

The cDNA of porcine 17 beta-estradiol dehydrogenase codes for a polypeptide of 737 amino acids. The dehydrogenase activity of the 80 kDa translation product is located in its N-terminal 32 kDa fragment, which is the major form isolated from endometrial epithelium. beta-Actin co-purifies with some of the 32 kDa enzyme, which contains actin-binding motifs and is homologous to hydratase-dehydrogenase-epimerase of Candida tropicalis. The microbody-targeting signal AKI and sequences resembling sterol carrier protein 2 are present in the C-terminal part of the 80 kDa protein. The N- and C-terminal parts are connected by a sequence containing the putative protease recognition signal AAP.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1988

[Infants with a very low birth weight: their development and interaction with their mothers].

Twenty-eight very low birthweight children (less than or equal to 1500 grams; the VLBW-group) and 24 term born children were studied from birth to 2 years of age. Over this period the interaction of these children with their mothers was observed in 6 naturalistic situations, and other aspects of their development were measured. The VLBW-group consisted of a relatively homogeneous group of healthy preterms, who had no sign of handicap at birth. It emerged that these VLBW-children were more liable to develop various types of problem, although such problems were on the whole not very serious in nature. Interesting differences were observed in mother-infant interaction, particularly in relation to the expression of negative emotions between mother and child. These differences were mainly interpreted in terms of their function in the mutual adaptation of mother and child.

Child Development↗
PubMedDate not supplied

Characterization of the HSD17B4 gene: D-specific multifunctional protein 2/17beta-hydroxysteroid dehydrogenase IV.

The HSD17B4 gene codes for a 80 kDa multifunctional enzyme containing three distinct functional domains and is localized in peroxisomes. The N-terminal part exhibits 3-hydroxyacyl-CoA dehydrogenase and 17beta-hydroxysteroid dehydrogenase activity whereas the central part shows enoyl-CoA hydratase activity. The carboxy-terminal part of the protein has sterol-carrier-protein activity. The protein is widely expressed, however in several tissues like brain, uterus and lung its expression is limited to specific cells like Purkinje cells or luminal epithelium. The HSD17B4 gene consist of 24 exons and 23 introns with classical intron-exon junctions spanning more than 100 kbp. The importance of the HSD17B4 protein is stressed by the identification of patients with severe clinical abnormalities due to mutations in the HSD17B4 gene. We have now checked the consequences of one frequent mutation, G16 S, which results in inactivation of the enzyme due to loss of interaction with NAD+.

17-Hydroxysteroid Dehydrogenases↗