scholarly journals Role of the Lysosomal Membrane Protein, CLN3, in the Regulation of Cathepsin D Activity

2017 ◽  
Vol 118 (11) ◽  
pp. 3883-3890 ◽  
Author(s):  
Jaime Cárcel‐Trullols ◽  
Attila D. Kovács ◽  
David A. Pearce
Keyword(s):  
Membrane Protein ◽  
Cathepsin D ◽  
Lysosomal Membrane ◽  
Lysosomal Membrane Protein ◽  
Cathepsin D Activity

scholarly journals Antibodies to platelets in patients with anti-phospholipid antibodies

Blood ◽  
1991 ◽  
Vol 77 (12) ◽  
pp. 2655-2659 ◽  
Author(s):  
HJ Out ◽  
PG de Groot ◽  
M van Vliet ◽  
GC de Gast ◽  
HK Nieuwenhuis ◽  
...  
Keyword(s):  
Platelet Activation ◽  
Lysosomal Membrane ◽  
Immunofluorescence Method ◽  
Exact Role ◽  
Flow Cytofluorometry ◽  
Healthy Donors ◽  
Lysosomal Membrane Proteins ◽  
Lysosomal Membrane Protein ◽  
Platelet Autoantibodies

Abstract Binding of anti-phospholipid antibodies to circulating platelets and its consequences on platelet activation and aggregation was investigated in 11 patients with anti-phospholipid antibodies. Seven patients had mild thrombocytopenia. Nine healthy donors served as controls. Binding to platelets was investigated by performing enzyme- linked immunosorbent assays (ELISAs) with phospholipids as antigen on platelet eluates. Platelet activation was measured by flow cytofluorometry using monoclonal antibodies to an activation-specific lysosomal membrane protein. Findings in ELISA were compared with results of a conventional immunofluorescence method to detect platelet autoantibodies. In seven patients antibodies to negatively charged phospholipids were present in platelet eluates. In all thrombocytopenic patients and controls the platelets were not activated and aggregation was not impaired. There was a positive concordance of 50% between the results of immunofluorescence and ELISA. No apparent relation was found between the results of ELISA or immunofluorescence and platelet counts. It is concluded that anti-phospholipid antibodies can bind to circulating platelets. This binding is not associated with measurable aggregation abnormalities nor with platelet activation characterized by exposure of lysosomal membrane proteins. More studies are necessary to determine the exact role of anti-phospholipid antibodies in the pathogenesis of thrombocytopenia and thrombosis.

scholarly journals The lysosomal membrane protein LAMP2A promotes autophagic flux and prevents SNCA-induced Parkinson disease-like symptoms in the Drosophila brain

Autophagy ◽  
2018 ◽  
Vol 14 (11) ◽  
pp. 1898-1910 ◽  
Author(s):  
Abdul-Raouf Issa ◽  
Jun Sun ◽  
Céline Petitgas ◽  
Ana Mesquita ◽  
Amina Dulac ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Parkinson Disease ◽  
Lysosomal Membrane ◽  
Autophagic Flux ◽  
Drosophila Brain ◽  
Lysosomal Membrane Protein

Expression of the lysosomal membrane protein LMBD1 is essential for the initiation of gastrulation

2017 ◽  
Vol 120 (1-2) ◽  
pp. S117
Author(s):  
Frank Rutsch ◽  
Petra Pennekamp ◽  
Yvonne Nitschke ◽  
Chrishanthi Lowe ◽  
Boris Skryabin ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Lysosomal Membrane ◽  
Lysosomal Membrane Protein

scholarly journals Functional characterization of the lysosomal membrane protein TMEM192 in mice

Oncotarget ◽  
2017 ◽  
Vol 8 (27) ◽  
pp. 43635-43652 ◽  
Author(s):  
Thuy Linh Nguyen ◽  
Janna Schneppenheim ◽  
Sönke Rudnik ◽  
Renate Lüllmann-Rauch ◽  
Christian Bernreuther ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Functional Characterization ◽  
Lysosomal Membrane ◽  
Lysosomal Membrane Protein

Release of prostaglandin F2alpha during splanchnic artery occlusion shock

1976 ◽  
Vol 230 (3) ◽  
pp. 684-690 ◽  
Author(s):  
JT Flynn ◽  
GA Bridenbaugh ◽  
AM Lefer
Keyword(s):  
Cathepsin D ◽  
Amino Nitrogen ◽  
Artery Occlusion ◽  
Prostaglandin F2alpha ◽  
Arterial Blood ◽  
Nitrogen Concentrations ◽  
Splanchnic Artery ◽  
Hepatic Portal ◽  
Cathepsin D Activity

Prostaglandin F2alpha concentrations were determined in hepatic portal venous plasma of dogs during splanchnic artery occlusion (SAO) shock and in nonshock control dogs. Dogs subjected to SAO shock exhibited a dramatic decrease in mean arterial blood pressure and significant increases in portal venous PGF2alpha and amino-nitrogen concentrations, as well as in cathepsin D and MDF activities. Dogs treated with indomethacin prior to SAO shock did not exhibit a significant increase in portal venous PGF2alpha. Indomethacin had no effect on the increase of plasma amino-nitrogen and only slightly reduced portal venous cathepsin D activity during SAO shock. Nevertheless, indomethacin significantly attenuated the severity of the postrelease hypotension observed in SAO shock and diminished the plasma accumulation of MDF. These studies indicate that prostaglandins are released from the splanchnic region during SAO shock and that this release can be prevented by pretreatment with indomethacin. The role of endogenously released prostaglandins in SAO shock is not clear, but the magnitude of the increase warrants further study.

Comparative behavior of lysosomes and the pre-lysosome compartment (PLC) in in vivo cell fusion experiments

1991 ◽  
Vol 99 (3) ◽  
pp. 571-582 ◽  
Author(s):  
Y.P. Deng ◽  
G. Griffiths ◽  
B. Storrie
Keyword(s):  
Membrane Protein ◽  
Cell Fusion ◽  
Sindbis Virus ◽  
Single Cells ◽  
Mouse Cell ◽  
Lysosomal Membrane ◽  
Immunogold Electron Microscopy ◽  
Membrane Markers ◽  
Lysosomal Membrane Protein

Interspecies cell fusion was used to compare protein intermixing within the mannose 6-phosphate receptor (MPR)-enriched pre-lysosome compartment (PLC) and within the MPR-negative lysosomal compartment. Both compartments were positive for lysosomal glycoprotein (lgp) membrane markers but were morphologically distinct. In most experiments, rat-mouse cell syncytia were formed by u.v.-inactivated Sindbis virus-mediated fusion. By immunogold electron microscopy of syncytia, extensive intermixing of species-specific lysosomal membrane proteins was observed in both lysosomes and PLC. At 3 h post cell fusion, multiple-label immunogold studies showed that 82% of the lysosome-like structures positive for the rat lysosomal membrane protein LIMP-I were also positive for the mouse lysosomal membrane protein mLAMP-1. By immunofluorescence, LIMP-I and mLAMP-1 co-localized with a t1/2 of 30 min after cell fusion; although the lgp-positive organelle populations had evidently interchanged their proteins, the lysosomal structures remained small, punctate bodies distributed throughout the syncytoplasm as observed in single cells. In contrast, the initially separate units of the PLC congregated with a t1/2 of 1 h to form large, pre-lysosome complexes associated with individual nuclear clusters. At the electron-microscope level, gold markers endocytized by the rat and mouse parent cells in a 1 h uptake followed by a 16–20 h chase co-localized in these extended PLC complexes, as did the membrane markers mLAMP-1 and LIMP-I. The density of labeling for rat MPR in the extended PLCs was markedly decreased, consistent with membrane fusions and dilution of the antigen upon congregation of the PLC compartments from the donor cells. The extended PLC complex behaved as a late endocytic compartment, as shown by co-localization of the MPR and rhodamine-dextran following a 10 min dextran uptake and a 50 min chase. These differences in behavior between lysosomes and the PLC in rat-mouse cell syncytia suggest that the pathway(s) of protein intermixing with respect to the two organelles may be different.

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