scholarly journals High Transcript Level of Fatty Acid-Binding Protein 11 but Not of Very Low-Density Lipoprotein Receptor Is Correlated to Ovarian Follicle Atresia in a Teleost Fish (Solea senegalensis)1

2007 ◽  
Vol 77 (3) ◽  
pp. 504-516 ◽  
Author(s):  
Maria J. Agulleiro ◽  
Michèle André ◽  
Sofia Morais ◽  
Joan Cerdà ◽  
Patrick J. Babin
2012 ◽  
Vol 23 (9) ◽  
pp. 1742-1764 ◽  
Author(s):  
Anupma Jha ◽  
Simon C. Watkins ◽  
Linton M. Traub

Clathrin-mediated endocytosis and phagocytosis are both selective surface internalization processes but have little known mechanistic similarity or interdependence. Here we show that the phosphotyrosine-binding (PTB) domain protein Ced-6, a well-established phagocytosis component that operates as a transducer of so-called “eat-me” signals during engulfment of apoptotic cells and microorganisms, is expressed in the female Drosophila germline and that Ced-6 expression correlates with ovarian follicle development. Ced-6 exhibits all the known biochemical properties of a clathrin-associated sorting protein, yet ced-6–null flies are semifertile despite massive accumulation of soluble yolk precursors in the hemolymph. This is because redundant sorting signals within the cytosolic domain of the Drosophila vitellogenin receptor Yolkless, a low density lipoprotein receptor superfamily member, occur; a functional atypical dileucine signal binds to the endocytic AP-2 clathrin adaptor directly. Nonetheless, the Ced-6 PTB domain specifically recognizes the noncanonical Yolkless FXNPXA sorting sequence and in HeLa cells promotes the rapid, clathrin-dependent uptake of a Yolkless chimera lacking the distal dileucine signal. Ced-6 thus operates in vivo as a clathrin adaptor. Because the human Ced-6 orthologue GULP similarly binds to clathrin machinery, localizes to cell surface clathrin-coated structures, and is enriched in placental clathrin-coated vesicles, new possibilities for Ced-6/Gulp operation during phagocytosis must be considered.


2021 ◽  
Vol 9 (10) ◽  
pp. 339-349
Author(s):  
Bhumika Upadhyay ◽  
◽  
Hina Yaseen ◽  
Hina Kauser ◽  
Chandra Mohan Kumar ◽  
...  

Introduction: Diabetes mellitus is acomplex metabolic disorder associated with increased risk of microvascular and macrovascular disease characterized by chronic hyperglycaemia resulting from defect in insulin secretion, insulin action, or both. Diabetic retinopathy (DR) causes visual impairment as a result of long term accumulated damaged to the small blood vessels in the retina.Adipocyte fatty acid binding protein(AFABP), been suggested as a third adipokine, in addition to leptin and adiponectin. AFABP might have a role in the proliferation of endothelial cells, as well as in angiogenesis. A-FABP levels were determined in subjects witout diabetes mellitus, with type 2 diabetes mellitus without DR and with DR at admission in order to investigate a possible association of A-FABP to the increased risk of incidence of DR. Material and methods: This study was done on non-diabetic (n=25) and Type 2 diabetes subjectswith(n=25) and without retinopathy (n=25) who visited HAHC hospital. Blood glucose (fasting and post prandial), glycated hemoglobin(HbA1c), urea, creatinine, uric acid, total protein, serum albumin,serum electrolytes (sodium, potassiumand chloride), totalcholesterol,triglyceride, high density lipoprotein(HDL), low density lipoprotein (LDL), very low density lipoprotein (VLDL) and and AFABP were measured . Result: The mean values of blood glucose (fasting and post prandial),HbA1C,urea, creatinine , TG, LDL VLDL and AFABP were higher in diabetic subjectswith diabetic retinopathy in comparison to diabetic subjects without retinopathy and subjects without diabetes mellitus and were highly significant statistically.(p<0.01). The mean value of HDL was lower in diabetic subjects with diabetic retinopathy in comparison to diabetic subjects without retinopathy and subjects without diabetes mellitus and was highly significant statistically. Conclusion:The study helps in associating AFABP as an early biochemical marker for identifying onset of diabetic retinopathy in subjects with diabetes mellitus at an early stage.


1997 ◽  
Vol 77 (04) ◽  
pp. 710-717 ◽  
Author(s):  
Marieke E van der Kaaden ◽  
Dingeman C Rijken ◽  
J Kar Kruijt ◽  
Theo J C van Berkel ◽  
Johan Kuiper

SummaryUrokinase-type plasminogen activator (u-PA) is used as a thrombolytic agent in the treatment of acute myocardial infarction. In vitro, recombinant single-chain u-PA (rscu-PA) expressed in E.coli is recognized by the Low-Density Lipoprotein Receptor-related Protein (LRP) on rat parenchymal liver cells. In this study we investigated the role of LRP in the liver uptake and plasma clearance of rscu-PA in rats. A preinjection of the LRP inhibitor GST-RAP reduced the maximal liver uptake of 125I-rscu-PA at 5 min after injection from 50 to 30% of the injected dose and decreased the clearance of rscu-PA from 2.37 ml/min to 1.58 ml/min. Parenchymal, Kupffer and endothelial cells were responsible for 40, 50 and 10% of the liver uptake, respectively. The reduction in liver uptake of rscu-PA by the preinjection of GST-RAP was caused by a 91 % and 62% reduction in the uptake by parenchymal and Kupffer cells, respectively. In order to investigate the part of rscu-PA that accounted for the interaction with LRP, experiments were performed with a mutant of rscu-PA lacking residues 11-135 (= deltal25- rscu-PA). Deletion of residues 11-135 resulted in a 80% reduction in liver uptake and a 2.4 times slower clearance (0.97 ml/min). The parenchymal, Kupffer and endothelial cells were responsible for respectively 60, 33 and 7% of the liver uptake of 125I-deltal25-rscu-PA. Preinjection of GST-RAP completely reduced the liver uptake of delta 125-rscu-PA and reduced its clearance to 0.79 ml/min. Treatment of isolated Kupffer cells with PI-PLC reduced the binding of rscu-PA by 40%, suggesting the involvement of the urokinase-type Plasminogen Activator Receptor (u-PAR) in the recognition of rscu-PA. Our results demonstrate that in vivo LRP is responsible for more than 90% of the parenchymal liver cell mediated uptake of rscu-PA and for 60% of the Kupffer cell interaction. It is also suggested that u-PAR is involved in the Kupffer cell recognition of rscu-PA.


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