scholarly journals Detecting distant relatives of mammalian LPS-binding and lipid transport proteins

1998 ◽  
Vol 7 (7) ◽  
pp. 1643-1646 ◽  
Author(s):  
Lesa J. Beamer ◽  
Daniel Fischer ◽  
David Eisenberg
Keyword(s):  
Transport Proteins ◽  
Lipid Transport ◽  
Lps Binding

scholarly journals Bactericidal/permeability-increasing protein in the reproductive system of male mice may be involved in the sperm–oocyte fusion

Reproduction ◽  
2013 ◽  
Vol 146 (2) ◽  
pp. 135-144 ◽  
Author(s):  
Kun Li ◽  
Yue Liu ◽  
Xiaoyu Xia ◽  
Li Wang ◽  
Meige Lu ◽  
...  
Keyword(s):  
Transport Proteins ◽  
Seminal Vesicles ◽  
Lipid Transport ◽  
Human Neutrophils ◽  
Gram Negative Bacteria ◽  
Male Mice ◽  
Gram Negative ◽  
Major Function ◽  
The Family ◽  
Lps Binding

Bactericidal/permeability-increasing protein (BPI) is a 455-residue (∼55 kDa) protein found mainly in the primary (azurophilic) granules of human neutrophils. BPI is an endogenous antibiotic protein that belongs to the family of mammalian lipopolysaccharide (LPS)-binding and lipid transport proteins. Its major function is to kill Gram-negative bacteria, thereby protecting the host from infection. In addition, BPI can inhibit angiogenesis, suppress LPS-mediated platelet activation, increase DNA synthesis, and activate ERK/Akt signaling. In this study, we found thatBpiwas expressed in the testis and epididymis but not in the seminal vesicles, prostate, and solidification glands. BPI expression in the epididymis increased upon upregulation of testosterone, caused by injection of GNRH. In orchidectomized mice, BPI expression was significantly reduced, but its expression was restored to 30% of control levels in orchidectomized mice that received supplementary testosterone. The number of sperm fused per egg significantly decreased after incubation with anti-BPI antiserum. These results suggest that BPI may take part in the process of sperm–oocyte fusion and play a unique and significant role in reproduction.

scholarly journals PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes

2019 ◽  
Vol 116 (45) ◽  
pp. 22619-22623 ◽  
Author(s):  
Andrés Guillén-Samander ◽  
Xin Bian ◽  
Pietro De Camilli
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Hot Spots ◽  
Transport Proteins ◽  
Lipid Transport ◽  
Domain Family ◽  
Late Endosomes ◽  
Dependent Interaction

Contacts between the endoplasmic reticulum (ER) and other membranes are hot spots for protein-mediated lipid transport between the 2 adjacent bilayers. Compiling a molecular inventory of lipid transport proteins present at these sites is a premise to the elucidation of their function. Here we show that PDZD8, an intrinsic membrane protein of the ER with a lipid transport module of the SMP domain family, concentrates at contacts between the ER and late endosomes/lysosomes, where it interacts with GTP-Rab7. These findings suggest that PDZD8 may cooperate with other proteins that function at the ER–endo/lysosome interface in coordinating endocytic flow with lipid transport between endocytic membranes and the ER.

Relevance of hereditary defects in lipid transport proteins for the pathogenesis of cholesterol gallstone disease

2004 ◽  
Vol 39 (241) ◽  
pp. 60-69 ◽  
Author(s):  
G. P. vanBerge-Henegouwen ◽  
N. G. Venneman ◽  
P. Portincasa ◽  
A. Kosters ◽  
K. J. van Erpecum ◽  
...  
Keyword(s):  
Cholesterol Gallstone ◽  
Gallstone Disease ◽  
Transport Proteins ◽  
Lipid Transport

scholarly journals Dysregulated Lipid Transport Proteins Correlate With Pathogenesis and Outcome in Severe Alcoholic Hepatitis

2019 ◽  
Vol 3 (12) ◽  
pp. 1598-1625 ◽  
Author(s):  
Jaswinder Singh Maras ◽  
Sukanta Das ◽  
Adil Bhat ◽  
Ashish Kumar Vyas ◽  
Gaurav Yadav ◽  
...  
Keyword(s):  
Alcoholic Hepatitis ◽  
Transport Proteins ◽  
Lipid Transport ◽  
Severe Alcoholic Hepatitis

scholarly journals A firehose for phospholipids

2020 ◽  
Vol 219 (5) ◽  
Author(s):  
William A. Prinz ◽  
James H. Hurley
Keyword(s):  
Transport Proteins ◽  
Lipid Transport ◽  
Cellular Membranes ◽  
Contact Sites

All lipid transport proteins in eukaryotes are thought to shuttle lipids between cellular membranes. In this issue, Li et al. (2020. J. Cell Biol.https://doi.org/10.1083/jcb.202001161) show that Vps13 has a channel-like domain that may allow lipids to flow between closely apposed membranes at contact sites.

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