Preparation and Application of Lectin–Gold Complexes

Benhamou, Nicole

doi:10.1016/b978-0-12-333927-0.50009-x

Cited by 59 publications

(34 citation statements)

References 82 publications

(112 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Baschong and Wrigley (1990) indicated that the centrifugation conditions usually reported for clearing small gold complexes are often too harsh and that smoother centrifugation conditions would lead to fewer losses due to aggregate packing in the centrifuge tube at the point of highest angular velocity. To improve the efficiency of clearance, the complex mixture may be diluted prior to centrifugation by one to several volumes of a buffered solution of protective protein such as BSA (Baschong, unpublished results), or centrifuged twice (Benhamou, 1989). Alternatively, complexes have been purified in sucrose or glycerol density gradients (Slot and Geuze, 1981), or by column size exclusion chromatography/gel filtration (Wang and Larrson, 1985;Slot et al, 1988; ϳ1 nm MPS-gold: Buining et al, 1997).…”

Section: Formation Of Protein Gold Complexes With Small Gold Colloidsmentioning

confidence: 99%

Preparation, use, and enlargement of ultrasmall gold particles in immunoelectron microscopy

Baschong

Stierhof

1998

Microsc. Res. Tech.

View full text Add to dashboard Cite

Section: Formation Of Protein Gold Complexes With Small Gold Colloidsmentioning

confidence: 99%

Preparation, use, and enlargement of ultrasmall gold particles in immunoelectron microscopy

Baschong

Stierhof

1998

Microsc. Res. Tech.

View full text Add to dashboard Cite

“…Cytochemical labeling was performed by the one-step and two-step postembedding methods as described by Benhamou (1986). The one-step method (direct labeling) was performed with HPL and RCA I lectins, and the two-step method (indirect labeling) with WGA and LFA lectins.…”

Section: Cytochemical Labelingmentioning

confidence: 99%

Ultrastructural and ultracytochemical features of secretory granules in the ampullary epithelium of the hamster oviduct

El-Mestrah¹,

Kan²

1999

Anat. Rec.

View full text Add to dashboard Cite

The epithelium of mammalian oviducts consists mainly of ciliated and non-ciliated secretory cells. In some mammals, secretory products originating from oviductal secretory cells have been shown to bind to the surface of, or accumulate within, ovulated eggs and/or developing embryos. These findings suggest that the secretions of the oviductal epithelial cells may play an important role in reproductive and developmental events that occur in the oviduct. In the present study, ultrastructural and cytochemical features of secretory cells in the hamster ampullary epithelium were shown by routine electron microscopy, lectin-gold cytochemistry and both conventional freeze-fracture and rapid-freezing techniques with special reference to the organizational aspects of their secretory granules. The use of ferrocyanide-reduced osmium tetroxide as a post-fixative in the Epon embedment of ampullary tissue samples also proved to be advantageous especially in revealing the carbohydrate contents of certain cellular compartments. The most conspicuous characteristic of the secretory cells, based on their staining property, was the presence of two types of secretory granules: those with a homogeneous electron-dense matrix and those with an electron-lucent matrix. Under favorable conditions, distinct features of the organizational arrangement of a crystalline lattice inside the secretory granules were also revealed. This well organized crystalline lattice shown in sections of Epon-embedded oviductal tissue was confirmed by examination of replicas of freeze-fractured oviducts prepared by the rapid-freezing technique. We also demonstrated with high resolution lectin-gold cytochemistry the intracellular distribution of lectin-binding glycoconjugates in the secretory cells of the hamster oviductal ampulla often in a linear array following the crystalline lattice. The results obtained in this study, taken together, provide insight into a possible link of the internal topographical features of oviductal secretory granules along with the cytochemical properties of their contents to the anticipated regulatory mechanism underlying their process of secretions.

show abstract

“…High-resolution cytochemical labeling techniques are available to cell biologists for subcellular localization of most types of biological macromolecules, from antigenic sites to carbohydrate residues, nucleic acids, and other substrate molecules, through their interaction with antibodies, lectins, and/or specific enzymes (Roth 1983;Bendayan 1981Bendayan ,1984Bendayan ,1995Londono and Bendayan 1988;Benhamou 1989). Taking advantage of the affinity properties that exist between macromolecules, we have used the protein-gold electron microscopic affinity cytochemical approach (Bendayan 1984) to localize the affinity binding sites of BSDL in pancreatic and duodenal tissues.…”

mentioning

confidence: 99%

The Affinity Binding Sites of Pancreatic Bile Salt-Dependent Lipase in Pancreatic and Intestinal Tissues

Bruneau

Lagadic‐Gossmann

Bendayan

2000

J Histochem Cytochem.

View full text Add to dashboard Cite

SUMMARYIn previous studies, we have shown that the bile salt-dependent lipase (BSDL) associates with the Grp94 molecular chaperone, an association that appears to play essential roles in the folding of BSDL. More recently, combined biochemical and immunocytochemical investigations were carried out to show that the transport of BSDL occurs via an association with the Grp94 all along the pancreatic secretory route (ER-Golgi-granules). The Grp94-BSDL complex is secreted with the pancreatic juice into the acinar lumen and reaches the duodenal lumen, where it is internalized by enterocytes. The dissociation of the complex could take place within the endosomal compartment because BSDL continues further on its way to the basolateral membrane of the enterocyte. To localize the affinity binding sites of pancreatic BSDL in pancreatic and duodenal tissues, we have used an affinity-gold ultrastructural technique. BSDL coupled to gold particles appears to interact with specific sites in tissue sections. This was confirmed by another indirect morphological approach using biotin-labeled BSDL and streptavidin-gold complexes on tissue sections. We have shown that BSDL associates with sites in the pancreatic secretory pathway compartments and in the microvilli, the endosomal compartment, and the basolateral membrane of enterocytes. By biochemical approaches, biotin-labeled BSDL displayed affinities with proteins of 180-190 kD in both pancreatic and duodenal tissues. We have also shown that the Grp94-BSDL complexes, which are insensitive to denaturing conditions, are present in pancreatic homogenate but not in duodenal lysate. Thus, BSDL is able to bind protein complexes formed by either BSDL-Grp94 or Grp94 dimers.

show abstract

Preparation and Application of Lectin–Gold Complexes

Cited by 59 publications

References 82 publications

Preparation, use, and enlargement of ultrasmall gold particles in immunoelectron microscopy

Preparation, use, and enlargement of ultrasmall gold particles in immunoelectron microscopy

Ultrastructural and ultracytochemical features of secretory granules in the ampullary epithelium of the hamster oviduct

The Affinity Binding Sites of Pancreatic Bile Salt-Dependent Lipase in Pancreatic and Intestinal Tissues

Contact Info

Product

Resources

About