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Biomedical subjects

M Hiden

Publications and source records attributed to M Hiden.

7 recordsLinked to original sources
PubMed2000

The role of lipoprotein lipase in adipose tissue development and metabolism.

Lipoprotein lipase (LPL) is essential for the hydrolysis and distribution of triglyceride-rich lipoprotein-associated fatty acids among extrahepatic tissues. Additionally, the enzyme facilitates several non-lipolysis associated functions including the cellular uptake of whole lipoprotein particles and lipophilic vitamins. The tissue-specific variations of LPL expression have been implicated in the pathogenesis of various lipid disorders, obesity and atherosclerosis. Transgenic technology provided the means to study the physiological response to the overexpression or absence of the enzyme in adipose tissue, muscle and macrophages. The effects of varying LPL expression in adipose tissue and muscle are summarized in this article.

Adipose Tissue↗
PubMed2000

cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase.

Straight-chain acyl-CoA oxidase is the first and rate limiting enzyme in the peroxisomal beta-oxidation pathway catalysing the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs, thereby producing H2O2. To study peroxisomal beta-oxidation we cloned and characterized the cDNA of mouse peroxisomal acyl-CoA oxidase. It consists of 3778 bp, including a 1983-bp ORF encoding a polypeptide of 661 amino-acid residues. Like the rat and human homologue the C-terminus contains an SKL motif, an import signal present in several peroxisomal matrix proteins. Sequence analysis revealed high amino-acid homology with rat (96%) and human (87%) acyl-CoA oxidase in addition to minor homology ( approximately 40%) with other related proteins, such as rabbit trihydroxy-cholestanoyl-CoA oxidase, human branched chain acyl-CoA oxidase and rat trihydroxycoprostanoyl-CoA oxidase. Acyl-CoA oxidase mRNA and protein expression were most abundant in liver followed by kidney, brain and adipose tissue. During mouse brain development acyl-CoA oxidase mRNA expression was highest during the suckling period indicating that peroxisomal beta-oxidation is most critical during this developmental stage. Comparing tissue mRNA levels of peroxisome proliferator-activated receptor alpha and acyl-CoA oxidase, we noticed a constant relationship in all tissues investigated, except heart and adipose tissue in which much more, and respectively, much less, peroxisome proliferator-activated receptor alpha mRNA in proportion to acyl-CoA oxidase mRNA was found. Our data show that acyl-CoA oxidase is an evolutionary highly conserved enzyme with a distinct pattern of expression and indicate an important role in lipid metabolism.

Acyl-CoA Oxidase↗
PubMed1994

cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region.

Enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme is one of the four enzymes of the peroxisomal beta-oxidation pathway. Here, we report the full-length human cDNA sequence and the localization of the corresponding gene on chromosome 3q26.3-3q28. The cDNA sequence spans 3779 nucleotides with an open reading frame of 2169 nucleotides. The tripeptide SKL at the carboxy terminus, known to serve as a peroxisomal targeting signal, is present. DNA sequence comparison of the coding region showed an 80% homology between human and rat bifunctional enzyme cDNA. The 3' noncoding sequence contains 117 nucleotides homologous to an Alu repeat. Based on sequence comparison, we propose that these nucleotides are a free left Alu arm with 86% homology to the Alu-J family. RNA analysis shows one band with highest intensity in liver and kidney. This cDNA will allow in-depth studies of molecular defects in patients with defective peroxisomal bifunctional enzyme. Moreover, it will also provide a means for studying the regulation of peroxisomal beta-oxidation in humans.

3-Hydroxyacyl CoA Dehydrogenases↗
PubMed1990

Pathologic features of placentas from singleton pregnancies obtained by in vitro fertilization and embryo transfer.

Fifty placentas were collected at term from singleton pregnancies resulting from in vitro fertilization (IVF) and intrauterine embryo transfer. Their pathologic features were compared with those of a control group composed of 50 placentas obtained from spontaneous singleton pregnancies. The mean maternal age, mean gestational age, mean fetal weight, sex ratio, and rate of pregnancy complications did not differ. There was also no significant difference between the groups in the mean placental weight and in the incidence of placental pathologic lesions, including extended infarcts, massive perivillous fibrin depositions, chorioangiomas, and placental inflammatory lesions. The incidence of abnormal placental shapes was significantly (P less than .05) greater in the IVF group (22%) compared with the control group (6%). A significant (P less than .025) difference was observed between the groups in the distribution of umbilical cord insertions. The mean distance between the cord insertion and the closest placental margin was significantly (P less than .005) shorter in the group conceived by IVF (3.23 +/- 1.91 cm) than in the control group (4.54 +/- 2.42 cm). A relationship between these placental morphologic features and the superficial implantation and/or inadequate orientation of the blastocyst after IVF and intrauterine embryo transfer is proposed.

Adult↗
PubMed1988

Hepatic telangiectasia and cirrhosis.

In a woman with hereditary hemorrhagic telangiectasia (HHT) (Osler-Weber-Rendu disease) who died of fulminant hepatitis B, autopsy revealed cirrhosis of the liver and diffuse hepatic telangiectasia. Her daughter and grandson also suffered from the hepatic involvement of HHT. Sufficient laboratory investigations were available to exclude known causes of cirrhosis. We review the relationship between Osler-Weber-Rendu disease and liver cirrhosis or fibrosis.

Aged↗
PubMed1985

Amyloidosis of the joints: evidence that human hip capsules have a unique predisposition for amyloid of the senile systemic type.

Amyloid-containing tissues were sampled from 19 capsules and 10 cartilages from hip, knee and sternoclavicular joints of 16 elderly patients. Heart ventricles from 3 of these patients were also studied. Histochemistry and immunofluorescence were performed and amyloid fibrils extracted from one hip capsule. The results indicate that 9 of 13 hip capsules contained prealbumin-like amyloid fibril protein ASc1, a finding characteristic of senile systemic amyloidosis. The amyloid of 16 out of 17 other joint structures showed no reaction with anti-ASc1 or antisera to 3 other systemic forms of amyloid, indicating that they represent localized forms of amyloid.

Aged↗