scholarly journals Study of the transit of an integral membrane protein from secretory granules through the plasma membrane of secreting rat basophilic leukemia cells using a specific monoclonal antibody.

1986 ◽  
Vol 102 (2) ◽  
pp. 516-522 ◽  
Author(s):  
J S Bonifacino ◽  
P Perez ◽  
R D Klausner ◽  
I V Sandoval
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Membrane Protein ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Secretory Granules ◽  
Integral Membrane Protein ◽  
Rat Basophilic Leukemia Cells ◽  
Rbl Cells ◽  
Basophilic Leukemia

The monoclonal antibody 5G10 reacted specifically with an 80-kD integral membrane protein in rat basophilic leukemia (RBL) cells. Immunofluorescence microscopy studies of RBL cells, fixed and permeabilized, revealed that the 80-kD protein was located in the membrane of cytoplasmic vesicles. The vesicles were identified as secretory granules by their content in immunoreactive serotonin. Expression of the 5G10 antigen on the surface of unstimulated RBL cells was low. However, RBL cells stimulated to secrete with anti-dinitrophenyl IgE followed by dinitrophenyl-bovine serum albumin or with the Ca2+ ionophore A-23187 displayed an increased expression of the antigen on their surface. Surface exposure of the 5G10 antigen was maximal at 5 min after stimulation of secretion. Removal of dinitrophenyl-bovine serum albumin from the incubation medium resulted in internalization of 50% of the antigen within 10 min.

Monoclonal antibody-based cross-reactive sandwich ELISA for the detection of Salmonella spp. in milk samples

2015 ◽  
Vol 7 (21) ◽  
pp. 9047-9053 ◽  
Author(s):  
Xiaoling Wu ◽  
Wenbin Wang ◽  
Liqiang Liu ◽  
Hua Kuang ◽  
Chuanlai Xu
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sandwich Elisa ◽  
Periodate Oxidation ◽  
Salmonella Spp ◽  
Milk Samples

An immunogen consisting ofSalmonellalipopolysaccharide and bovine serum albumin was prepared by periodate oxidation.

Pregnancy-blocking progesterone antibody targets specifically the uterus through its progesterone-binding sites

1990 ◽  
Vol 4 (3) ◽  
pp. 283-291 ◽  
Author(s):  
M.-W. Wang ◽  
A. Whyte ◽  
R. B. Heap ◽  
M. J. Taussig
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Passive Immunization ◽  
Uterine Epithelium ◽  
High Affinity ◽  
Specific Targeting

ABSTRACT Passive immunization with a mouse monoclonal antibody against progesterone, designated DB3, blocks pregnancy in several species. We have previously reported that DB3 localizes in the mouse uterine epithelium shortly before normal implantation. This phenomenon is pregnancy dependent and specific for the progesterone antibody. In this study we demonstrate that DB3 is present in the lumen of the uterus 36 h after an i.p. injection; this correlates with the time of maximum antibody reaction on the uterine epithelium. Incubation of DB3 with free progesterone, progesterone-hemisuccinate or progesterone—bovine serum albumin before administration prevented its localization on the epithelium, indicating that the localization requires free progesterone-binding sites and thus probably depends upon progesterone binding. In addition, studies in vitro show that DB3 can effectively bind to progesterone carried by high-affinity progesterone-binding protein purified from coypu plasma. We suggest that specific targeting of DB3 may be through progesterone associated with a progesterone-binding molecule on the membrane of the uterine epithelia. This may be an important part of the mechanism of antibody action against implantation.

Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells

1989 ◽  
Vol 92 (4) ◽  
pp. 701-712
Author(s):  
J.S. Bonifacino ◽  
L. Yuan ◽  
I.V. Sandoval
Keyword(s):  
Membrane Protein ◽  
Secretory Granules ◽  
Integral Membrane Protein ◽  
Integral Membrane Proteins ◽  
Multivesicular Bodies ◽  
Pituitary Cells ◽  
Coated Pits ◽  
Golgi System ◽  
Rbl Cells ◽  
Natural Killer Lymphocytes

The 80K (80 × 10(3) Mr) integral membrane protein, first described in the secretory granules of rat basophilic leukaemia (RBL) cells, is also localized to lysosomes in these cells. The protein displays the same distribution in natural killer lymphocytes (RNK-7), wherein it codistributes with cytolysin in secretory granules. In contrast, the protein is absent from the endocrine and exocrine secretory granules of rat pancreatic acinar and pituitary cells, respectively, where it is confined to lysosomes. The protein colocalizes with lysosomal integral membrane proteins in all the cells studied, indicating that is largely restricted to secretory granules with lysosomal properties (LSG) and lysosomes. The protein expressed on the surface of secreting RBL cells is internalized by endocytosis via coated pits, and found in coated vesicles, endosomes, multivesicular bodies and Golgi system, before being recycled to LSG and partly delivered to lysosomes. The recycled protein is re-expressed on the surface of cells stimulated to secrete a second time.

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