Lysosome-Associated Membrane Protein-1 (LAMP-1) Is the Melanocyte Vesicular Membrane Glycoprotein Band II

1993 ◽  
Vol 100 (2) ◽  
pp. 110-114 ◽  
Author(s):  
Bao-Kang Zhou ◽  
Raymond E. Boissy ◽  
Sharon Pifko-Hirst ◽  
Denis J. Moran ◽  
Seth J. Orlow
Keyword(s):  
Membrane Protein ◽  
Membrane Glycoprotein ◽  
Vesicular Membrane

scholarly journals Functional analyses of a novel vesicular membrane protein, TMEM141 during the growth stage in medaka (Oryzias latipes) larvae

2017 ◽  
Vol 145 ◽  
pp. S153
Author(s):  
Yasuhiro Tonoyama ◽  
Tamami Adachi ◽  
Atsushi Shimizu ◽  
Atsushi Takayanagi ◽  
Susumu Mitsuyama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Growth Stage ◽  
Oryzias Latipes ◽  
Vesicular Membrane ◽  
Functional Analyses

Platelet Agglutinating Protein p37 Causes Platelet Agglutination through its Binding to Membrane Glycoprotein IV

1991 ◽  
Vol 65 (01) ◽  
pp. 102-106 ◽  
Author(s):  
Eric C-Y Lian ◽  
Farooq A Siddiqui ◽  
G A Jamieson ◽  
Narendra N Tandon
Keyword(s):  
Monoclonal Antibodies ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Receptor Site ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Thrombocytopenic Purpura ◽  
Normal Platelet ◽  
Reducing Conditions ◽  
Rabbit Igg

SummaryA 37 kDa platelet agglutinating protein (PAP p37) has previously been shown to be present in a subset of patients with thrombotic thrombocytopenic purpura and has been purified from their plasma. Using solubilized platelet membrane proteins from normal donors, it was shown by Western blotting that r2sI-p37 bound to a membrane protein of 97 kDa (red/unred). Furthernore, the same protein was identified by reverse immunoblotting in which purified p37 was electrophoresed, transferred to the nitrocellulose sheet and incubated with solubilized normal platelet membrane proteins. The complex formed between p37 and the membrane protein was identified by autoradiography using polyclonal and monoclonal (OKM5) anti- GPIV antibodies, but was not detected by polyclonal antibody to GPIIIa. Similar studies with purified platelet GPIV under both reducing and non-reducing conditions demonstrated the binding of 125I-p37. Polyclonal and monoclonal antibodies to GPIV completely inhibited the platelet agglutination induced by TTP plasma containing p37, however, normal rabbit IgG, rabbit anti- GPIIIa IgG, and murine monoclonal anti-GPIIb/IIIa (10E5) antibodies had no effect. These data indicate that platelet GPIV is the receptor site for PAP p37.

scholarly journals Wheat germ agglutinin blocks the acrosome reaction in Strongylocentrotus purpuratus sperm by binding a 210,000-mol-wt membrane protein.

1984 ◽  
Vol 99 (5) ◽  
pp. 1598-1604 ◽  
Author(s):  
S B Podell ◽  
V D Vacquier
Keyword(s):  
Membrane Protein ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Acrosome Reaction ◽  
Strongylocentrotus Purpuratus ◽  
Membrane Glycoprotein ◽  
Entire Surface ◽  
Direct Measurements ◽  
Egg Jelly

Wheat germ agglutinin (WGA) binds to the entire surface of Strongylocentrotus purpuratus sperm, and inhibits the egg jelly-induced acrosome reaction. The binding was found to be species dependent and was completely inhibited by 5 mM N-acetyl-D-glucosamine. Blockage of the acrosome reaction by WGA was bypassed by a combination of the ionophores A23187 and monensin, although neither ionophore was effective individually. These experiments suggest that WGA blocks both Ca2+ uptake and Na+/H+ exchange in these sperm, which was confirmed by direct measurements of 45Ca2+ uptake and H+ efflux. The target of WGA in S. purpuratus sperm appears to be a membrane glycoprotein of Mr = 210,000. Treatment of this protein with neuraminidase or endo-beta-N-acetylglucosaminidase F abolished WGA binding.

scholarly journals Evidence for a nonlysosomal origin of the acrosome.

1996 ◽  
Vol 44 (4) ◽  
pp. 313-320 ◽  
Author(s):  
J A Martínez-Menárguez ◽  
H J Geuze ◽  
J Ballesta
Keyword(s):  
Membrane Protein ◽  
Secretory Protein ◽  
Synthetic Activity ◽  
Sperm Cells ◽  
Membrane Glycoprotein ◽  
Acrosomal Membrane ◽  
Golgi Region ◽  
Opposite Situation ◽  
Mannose 6 Phosphate ◽  
Lysosomal Membrane Glycoprotein

We studied the biogenesis of the acrosome in sperm cells in immunogold-labeled ultrathin cryosections of rat testis, using a variety of antibodies against endosomal/lysosomal marker protein and acrosin, the major secretory protein of sperm cells. As expected, acrosomes and proacrosomal vesicles in the trans-Golgi region contained abundant acrosin. Rat lysosomal membrane glycoprotein (lgp) 120 and mouse lysosome-associated membrane protein-1 were not detectable in the acrosomal membrane. Similarly, the late endosomal markers cation-dependent and -independent mannose 6-phosphate receptors were absent from the acrosome and proacrosomal vesicles. Therefore, acrosomes do not exhibit these endosomal/lysosomal features. Apart from (pro) acrosomal vesicles, both spermatocytes and spermatids contained classical lysosomes (positive for rat lgp 120, mouse lysosome-associated membrane protein-1, and cathepsin D) that were negative for acrosin. Quantitative analysis of the immunogold labeling showed that spermatocytes express more mannose 6-phosphate receptors and lgp 120 than spermatids, whereas the opposite situation existed for acrosin. These data indicate differential synthetic activity of lysosomal and acrosomal constituents in different states of sperm differentiation. Together, our observations argue against a lysosomal /endosomal origin of the acrosome.

Fibrinogen (FIBR) Binding Is Necessary For Incorporation Of 125I-Labeled Membrane Protein Into The Platelet Cytoskeleton

1981 ◽  
Author(s):  
M B Zucker ◽  
R A Grant
Keyword(s):  
Membrane Protein ◽  
Cytoskeletal Protein ◽  
Membrane Glycoprotein ◽  
Surface Molecules ◽  
Sds Page ◽  
Thrombin Activation ◽  
Triton X ◽  
Induced Aggregation

Platelets stimulated with ADP bind fibr specifically, and this ability correlates well with their ability to aggregate when they are shaken with ADP and fibr. Others found that platelets incubated with chymotrypsin (CT) bind and aggregate with fibr without stimulation by ADP; as with ADP-induced stimulation, these responses are inhibited by excess EDTA. Phillips et al. showed that thrombin activation produced a large Triton-insoluble cytoskeleton in the presence of either EDTA or CaCl2, but that 125I-labeled glycoprotein(s) IIb-III were incorporated into the cytoskeleton only when CaCl2 was present and aggregation occurred. This system cannot be used to assess the role of fibr in membrane glycoprotein incorporation, as exogenous fibr is not required for thrombin-induced aggregation. We therefore used CT-treated platelets labeled with 125I. They were suspended in calcium-poor Hepes-buffered Tyrode’s solution at 22°C for 30 min with 2.5 mM EDTA or 1 mM CaCl2 with or without 100 ug/ml fibr. Only samples with CaCl2 + fibr aggregated, and similar samples prepared with CT-treated platelets which had first been incubated with EDTA at 37°C for 15 min failed to aggregate despite recalcification. Cytoskeletons were prepared by adding an equal vol of 2% Triton X-100-5 mM EGTA-0.1 M Tris pH 7.4 and centrifuging 1 hr later. Cytoskeletal protein was 10-25% of total and did not vary with aggregability. CT-treated platelets showed more 125I bands than untreated labeled platelets. The two bands with highest Mr on SDS-PAGE were present only when the platelets aggregated during incubation, i.e., under conditions in which fibr is bound. Possibly the dimeric fibr molecule must link two surface molecules before they can attach to the cytoskeleton.

scholarly journals Abnormal carbohydrate composition of the major penetrating membrane protein of En(a-) human erythrocytes

1976 ◽  
Vol 155 (3) ◽  
pp. 701-703 ◽  
Author(s):  
M J Tanner ◽  
R E Jenkins ◽  
D J Anstee ◽  
J R Clamp
Keyword(s):  
Membrane Protein ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Membrane Glycoprotein ◽  
Carbohydrate Composition ◽  
A Cell ◽  
Normal Human

The major penetrating membrane glycoprotein (band 3) was isolated from En(a-) and normal human erythrocytes. The two proteins differed only in carbohydrate composition. Band 3 from En(a-) erythrocytes contained greater amounts of galactose and N-acetyl-glucosamine. The loss of the sialoglycoprotein sialotetrasaccharides in the En(a-) cell is not compensated by the appearance of these units in band 3 of En(a-) erythrocytes.

Effect of verapamil on cytoplasmic distribution of granules and microfilaments in amphibian urinary bladder

1988 ◽  
Vol 46 ◽  
pp. 324-325
Author(s):  
A.J. Mia ◽  
L.X. Oakford ◽  
T. Yorio
Keyword(s):  
Urinary Bladder ◽  
Water Flow ◽  
Morphological Changes ◽  
Granular Cell ◽  
Cytosolic Calcium ◽  
Calcium Storage ◽  
Amphibian Urinary Bladder ◽  
Vesicular Membrane ◽  
High Concentrations ◽  
Cytoskeletal System

The amphibian urinary bladder has been used as a ‘model’ system for studies of the mechanism of action of antidiuretic hormone (ADH) in stimulating transepithelial water flow. The increase in water permeability is accompanied by morphological changes that include the stimulation of apical microvilli, mobilization of microtubules and microfilaments and vesicular membrane fusion events . It has been shown that alterations in the cytosolic calcium concentrations can inhibit ADH transmembrane water flow and induce alterations in the epithelial cell cytomorphology, including the cytoskeletal system . Recently, the subapical granules of the granular cell in the amphibian urinary bladder have been shown to contain high concentrations of calcium, and it was suggested that these cytoplasmic constituents may act as calcium storage sites for intracellular calcium homeostasis. The present study utilizes the calcium antagonist, verapamil, to examine the effect of calcium deprivation on the cytomorphological features of epithelial cells from amphibian urinary bladder, with particular emphasis on subapical granule and microfilament distribution.

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

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