Effects of different raising systems on colour and quality characteristics of Turkish Pekin duck meats

The current trial was conducted to determine the influence of different raising systems on the meat quality properties of male Turkish Pekin ducks. Ninety male ducklings were randomly allocated to three experimental groups: an animal-fish integrated farming group (IG), a non-animal-fish integrated farming group (NIG) and a poultry house group (PHG). All ducklings were fed a starter diet from weeks 2 to 6 and a finisher diet from weeks 6 to 10. Feed and water were offered ad libitum. At the end of the trial all ducks were slaughtered and the carcasses were stored at 3 °C for 24 hours, after which L*, a* and b* values of the carcass skins were measured. After standard dissection of carcasses, pectoralis muscles were obtained on which pH, colour (L*, a*, b*, C and H), total aerobic mesophilic, total aerobic psychrotrophic, lactic acid bacteria, Micrococcus/Staphylococcus, yeast-mould and Enterobacteriaceae counts were determined. The different raising systems of the ducks had significant effects on the pH, total aerobic mesophilic, Enterobacteriaceae, and L* and b* values of the pectoralis muscle. The lowest pH, total aerobic mesophilic and Enterobacteriaceae counts were found in the PHG group. The lowest L* values for the pectoralis muscle were found in the IG group while the highest a* value was recorded in the IG group. Significant differences in skin colour were observed between the experimental groups. For all production groups, all microbial counts were found to be within acceptable ranges. However, pH, total aerobic mesophilic and Enterobacteriaceae results were found to be lower in the PHG group than in the other groups. Different raising systems were thus found to affect the meat and skin colour of ducks, which may influence the preference of consumers. Keywords: Pekin duck, integrated farming, carcass and meat colour, microbial propertiesSouth African Journal of Animal Science Vol. 38 (3) 2008: pp. 217-22

Coe Genes Are Expressed in Differentiating Neurons in the Central Nervous System of Protostomes

Genes of the coe (collier/olfactory/early B-cell factor) family encode Helix-Loop-Helix transcription factors that are widely conserved in metazoans and involved in many developmental processes, neurogenesis in particular. Whereas their functions during vertebrate neural tube formation have been well documented, very little is known about their expression and role during central nervous system (CNS) development in protostomes. Here we characterized the CNS expression of coe genes in the insect Drosophila melanogaster and the polychaete annelid Platynereis dumerilii, which belong to different subgroups of protostomes and show strikingly different modes of development. In the Drosophila ventral nerve cord, we found that the Collier-expressing cells form a subpopulation of interneurons with diverse molecular identities and neurotransmitter phenotypes. We also demonstrate that collier is required for the proper differentiation of some interneurons belonging to the Eve-Lateral cluster. In Platynereis dumerilii, we cloned a single coe gene, Pdu-coe, and found that it is exclusively expressed in post mitotic neural cells. Using an original technique of in silico 3D registration, we show that Pdu-coe is co-expressed with many different neuronal markers and therefore that, like in Drosophila, its expression defines a heterogeneous population of neurons with diverse molecular identities. Our detailed characterization and comparison of coe gene expression in the CNS of two distantly-related protostomes suggest conserved roles of coe genes in neuronal differentiation in this clade. As similar roles have also been observed in vertebrates, this function was probably already established in the last common ancestor of all bilaterians

Ovarian pregnancy; Relationship to an intrauterine device

Ovarian pregnancy is a rare form of ectopic pregnancy in which the gestational sac is implanted within the ovary. The incidence is 0.5 to 3% of all ectopic gestations (1). In contrast to patients with tubal pregnancies, traditional risk factors, such as pelvic inflammatory disease and prior surgical procedure upon the pelvis, may not play a role in the aetiology. In the 2 cases reported hen, it seems that using an intrauterine contraceptive device was an important factor

A case of acanthosis nigricans as a paraneoplastic syndrome with squamous cell lung cancer

Yusuf Karakas,1 Ece Esin,1 Sahin Lacin,1 Koray Ceyhan,2 Aylin Okcu Heper,2 Suayib Yalcin1 1Medical Oncology Department, Hacettepe University Cancer Institute, 2Department of Medical Pathology, Ankara University School of Medicine, Ankara, Turkey Abstract: A 55-year-old man presented with oral mucosal ulcers, blackening of both hands, and hyperpigmentation on axillary, anal, and inguinal regions for the last 3 months, which were all progressive. The patient was referred to the oncology department with the diagnosis of acanthosis nigricans for investigation of an underlying malignancy. He was a smoker. A computed tomography scan of thorax revealed enlarged mediastinal lymphadenopathies and a lesion on the left upper lobe. Fine-needle aspiration biopsy of the mediastinal lesion was consistent with squamous cell carcinoma, and biopsies of the skin and oral mucosal lesion also further confirmed the diagnosis of acanthosis nigricans. After docetaxel and cisplatin chemotherapy, a significant improvement in his skin and mucosal lesions was observed with almost complete resolution of the pulmonary lesion and the mediastinal lymph nodes. Keywords: acanthosis nigricans, squamous cell lung cancer, paraneoplastic syndrom

Dynamic role of the tether helix in PIP2-dependent gating of a G protein-gated potassium channel

G protein-gated inwardly rectifying potassium (GIRK) channels control neuronal excitability in the brain and are implicated in several different neurological diseases. The anionic phospholipid phosphatidylinositol 4,5 bisphosphate (PIP2) is an essential cofactor for GIRK channel gating, but the precise mechanism by which PIP2 opens GIRK channels remains poorly understood. Previous structural studies have revealed several highly conserved, positively charged residues in the "tether helix" (C-linker) that interact with the negatively charged PIP2 However, these crystal structures of neuronal GIRK channels in complex with PIP2 provide only snapshots of PIP2's interaction with the channel and thus lack details about the gating transitions triggered by PIP2 binding. Here, our functional studies reveal that one of these conserved basic residues in GIRK2, Lys200 (6'K), supports a complex and dynamic interaction with PIP2 When Lys200 is mutated to an uncharged amino acid, it activates the channel by enhancing the interaction with PIP2 Atomistic molecular dynamic simulations of neuronal GIRK2 with the same 6' substitution reveal an open GIRK2 channel with PIP2 molecules adopting novel positions. This dynamic interaction with PIP2 may explain the intrinsic low open probability of GIRK channels and the mechanism underlying activation by G protein Gβγ subunits and ethanol

Dynamic role of the tether helix in PIP2-dependent gating of a G protein-gated potassium channel

G protein-gated inwardly rectifying potassium (GIRK) channels control neuronal excitability in the brain and are implicated in several different neurological diseases. The anionic phospholipid phosphatidylinositol 4,5 bisphosphate (PIP2) is an essential cofactor for GIRK channel gating, but the precise mechanism by which PIP2 opens GIRK channels remains poorly understood. Previous structural studies have revealed several highly conserved, positively charged residues in the "tether helix" (C-linker) that interact with the negatively charged PIP2 However, these crystal structures of neuronal GIRK channels in complex with PIP2 provide only snapshots of PIP2's interaction with the channel and thus lack details about the gating transitions triggered by PIP2 binding. Here, our functional studies reveal that one of these conserved basic residues in GIRK2, Lys200 (6'K), supports a complex and dynamic interaction with PIP2 When Lys200 is mutated to an uncharged amino acid, it activates the channel by enhancing the interaction with PIP2 Atomistic molecular dynamic simulations of neuronal GIRK2 with the same 6' substitution reveal an open GIRK2 channel with PIP2 molecules adopting novel positions. This dynamic interaction with PIP2 may explain the intrinsic low open probability of GIRK channels and the mechanism underlying activation by G protein Gβγ subunits and ethanol