The vacuolar-type ATPase from insect plasma membrane: immunocytochemical localization in insect sensilla

1991 ◽  
Vol 266 (2) ◽  
pp. 265-273 ◽  
Author(s):  
Ulla Klein ◽  
Bernhard Zimmermann
Keyword(s):  
Plasma Membrane ◽  
Immunocytochemical Localization ◽  
Insect Sensilla

Immunocytochemical localization of p65 with one-nanometer gold particles following silver development

1989 ◽  
Vol 47 ◽  
pp. 1042-1043
Author(s):  
Richard W. Burry ◽  
Diane M. Hayes
Keyword(s):  
Plasma Membrane ◽  
Bovine Serum Albumin ◽  
Calf Serum ◽  
Specific Protein ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Gold Particles ◽  
Pass Through ◽  
Label Distribution ◽  
Phosphate Buffered Saline

Electron microscopic (EM) immunocytochemistry localization of the neuron specific protein p65 could show which organelles contain this antigen. Antibodies (Ab) labeled with horseradish peroxidase (HRP) followed by chromogen development show a broad diffuse label distribution within cells and restricting identification of organelles. Particulate label (e.g. 10 nm colloidal gold) is highly desirable but not practical because penetration into cells requires destroying the plasma membrane. We report pre-embedding immunocytochemistry with a particulate marker, 1 nm gold, that will pass through membranes treated with saponin, a mild detergent.Cell cultures of the rat cerebellum were fixed in buffered 4% paraformaldehyde and 0.1% glutaraldehyde (Glut.). The buffer for all incubations and rinses was phosphate buffered saline with: 1% calf serum, 0.2% saponin, 0.1% gelatin, 50 mM glycine 1 mg/ml bovine serum albumin, and (not in the HRP labeled cultures) 0.02% sodium azide. The monoclonal #48 to p65 was used with three label systems: HRP, 1 nm avidin gold with IntenSE M development, and 1 nm avidin gold with Danscher development.

scholarly journals GRAMP 100: a membrane protein concentrated on secretory granule membranes and the apical cell surface in exocrine acinar cells.

1992 ◽  
Vol 40 (12) ◽  
pp. 1827-1835 ◽  
Author(s):  
S M Laurie ◽  
M B Mixon ◽  
J D Castle
Keyword(s):  
Plasma Membrane ◽  
Apical Cell ◽  
Reduced Form ◽  
Electron Microscopic Level ◽  
Apical Plasma Membrane ◽  
Cell Fractionation ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Common Component ◽  
Rat Parotid

Using a monoclonal antibody (SG10A6) raised against secretion granule membranes of the rat parotid gland, we have identified an antigen that is a common component of both exocrine pancreatic and parotid granule membranes. SG10A6 (an IgM) immunoprecipitates antigen that migrates as a single band (M(r) approximately 80 KD unreduced; M(r) approximately 100 KD reduced) and immunoblots at least two polypeptides that are similar to the reduced and nonreduced immunoprecipitated antigen. This granule-associated membrane polypeptide (GRAMP 100; named for the apparent M(r) in reduced form) is also a prominent component of plasma membrane fractions. Immunocytochemical localization at the electron microscopic level demonstrates the presence of GRAMP 100 on granule membranes, especially condensing vacuoles and exocytotic figures, and the apical plasma membrane. Lower levels of antigen are detected on basolateral plasma membrane and on peri-Golgi membranes that may be part of the endosomal system. Both the cell fractionation and immunocytochemical localization indicate that GRAMP 100 differs in distribution from GRAMP 92 and 30K SCAMPs, two other components of exocrine granule membranes identified with monoclonal antibodies. To date, no polypeptides have been identified with this approach that are exclusive components of exocrine granule membranes.

Immunocytochemical localization of thymus-leukemia (TL) antigen on cryosections of thymocytes

1990 ◽  
Vol 48 (3) ◽  
pp. 372-373
Author(s):  
Cheryl Hartfield ◽  
Bruce Loveland ◽  
Alasdair McDowall ◽  
Kirsten Fischer Lindahl
Keyword(s):  
Plasma Membrane ◽  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Mhc Class I ◽  
Subcellular Fractions ◽  
Class I ◽  
Mouse Strains ◽  
Immunocytochemical Localization ◽  
Isolated Mitochondria ◽  
Histocompatibility Complex

TL antigens are class I molecules of the major histocompatibility complex (MHC). They are present on the surface of cortical thymocytes of certain mouse strains. A recent study finds that a mitochondrially-encoded peptide (MTF) is presented on the cell surface by the MHC class I HMT molecule, which is encoded by a gene closely linked to that encoding TL. These results make it relevant to re-examine earlier reports that TL antigens can be found on mitochondria. In 1978, Jeng et al. demonstrated by classical resin embedding that, in addition to the plasma membrane, isolated mitochondria from TL+ cells could also be labeled with anti-TL alloantiserum and a hemocyanin conjugate. This finding was unexpected, as there was no precedent for the presence of any class I molecules on the surface of mitochondria. However, contamination of subcellular fractions with other cellular constituents is unavoidable, and a control for plasma membrane contamination was not reported by Jeng et al.

Trypanosoma cruzi and American Leishmania spp: Immunocytochemical localization of a laminin-like protein in the plasma membrane

1986 ◽  
Vol 61 (2) ◽  
pp. 168-175 ◽  
Author(s):  
Antonio Bretaña ◽  
JoséLuis Avila ◽  
Marianela Arias-Flores ◽  
Marisol Contreras ◽  
Félix Jacobo Tapia
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Immunocytochemical Localization ◽  
Leishmania Spp

scholarly journals Immunocytochemical localization of P170 at the plasma membrane of multidrug-resistant human cells.

1987 ◽  
Vol 35 (12) ◽  
pp. 1451-1456 ◽  
Author(s):  
M C Willingham ◽  
N D Richert ◽  
M M Cornwell ◽  
T Tsuruo ◽  
H Hamada ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Multidrug Resistant ◽  
Human Cells ◽  
Immunocytochemical Localization

Regular Papers / Articles OrdinairesIntine wall modifications during germination of Zygophyllum fabago (Zygophyllaceae) pollen grains

2003 ◽  
Vol 81 (12) ◽  
pp. 1267-1277 ◽  
Author(s):  
Teresa Castells ◽  
Juan A Seoane-Camba ◽  
María Suárez-Cervera
Keyword(s):  
Plasma Membrane ◽  
Pollen Grains ◽  
High Density ◽  
Hydration Process ◽  
Immunocytochemical Localization ◽  
Germination Process ◽  
Acidic Polysaccharides ◽  
Allergenic Proteins ◽  
Germinated Pollen

The composition of the inner layer (intine) of mature, activated, and germinated Zygophyllum fabago L. (Zygophyllaceae) pollen grains was studied. Cytochemical techniques showed neutral and acidic polysaccharides to be the major component of the thin and unlayered intine. The intine lacks lipids, with only scattered lipid globules being observed near the plasma membrane. Immunocytochemical localization of esterified and unesterified pectins in the intine was performed to determine the behaviour (permeability and elasticity) of germinal apertures. The high density of unesterified pectins in the intine of Z. fabago may be related to harmomegathic changes, which increase the elasticity of the intine during hydration and germination processes. A new layer was deposited in germinated pollen grains, recognized by 1,3-β-glucan (callose) antibodies; this layer plays a role in keeping the grains swollen during the germination process and probably forms a selective barrier to control the movement of substances through the pollen walls. Indeed, the composition of the Z. fabago intine was related to both the hydration process preceding germination and the passage of allergenic proteins through it.Key words: callose, germination, intine, pectins, pollen grains, Zygophyllum fabago.

scholarly journals Immunocytochemical localization of pectinesterases in hyphae of Phytophthora infestans

1987 ◽  
Vol 65 (12) ◽  
pp. 2607-2613 ◽  
Author(s):  
Helga Förster ◽  
Kurt Mendgen
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Phytophthora Infestans ◽  
Protein A ◽  
Immunocytochemical Localization ◽  
Hyphal Cell ◽  
Gold Particles ◽  
Different Types ◽  
Ultrathin Sections ◽  
Lowicryl K4m

Evidence for the localization of extracellular pectinesterases was obtained in hyphae of Phytophthora infestans with the antibody – protein A – gold technique. Hyphae were fixed in 1% formaldehyde and 0.5% glutaraldehyde, and the immunocytochemical localization was done on ultrathin sections of tissue embedded at low temperature in Lowicryl K4M. Gold particles were mainly present over three different types of vesicles and over dictyosomes. In older parts of the hyphae, the plasma membrane was heavily labeled. This might suggest that the hyphal cell wall in subapical regions is not as permeable as in the hyphal tips.

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