In vitro binding of Candida albicans yeast cells to human fibronectin

1984 ◽  
Vol 30 (2) ◽  
pp. 221-227 ◽  
Author(s):  
Katherine G. Skerl ◽  
Richard A. Calderone ◽  
Esther Segal ◽  
T. Sreevalsan ◽  
W. Michael Scheld
Keyword(s):  
Candida Albicans ◽  
Epithelial Cells ◽  
Mammalian Cells ◽  
Fluorescent Antibody ◽  
In Vitro Assay ◽  
Yeast Cells ◽  
Vitro Assay ◽  
Vaginal Epithelial Cells ◽  
Human Fibronectin

The binding of Candida albicans yeast cells to human fibronectin (Fn), a major glycoprotein of mammalian cells, was studied using an in vitro assay. Adherence was quantitated in microtiter dishes coated with Fn to which radiolabeled yeast cells were added. Under optimum conditions of the assay, i.e., 1 mM CaCl2 and 70 μg Fn protein, approximately 40% of the radiolabeled yeast cells adhered to the Fn. Adherence to Fn was greater at 30 °C than at 4 °C and was greater with viable yeast cells than with heat-killed cells. Candida albicans (two strains) and C. tropicalis adhered to Fn to a greater extent than C. pseudotropicalis, C. krusei, or Saccharomyces cerevisiae. Pretreatment of C. albicans with chymotrypsin, pronase, or papain, but not pepsin, decreased adherence to Fn. Blocking experiments using mannan, sugars, or amino sugars were carried out by preabsorbing the Fn with each of the above-mentioned compounds. Candida mannan blocked adherence of C. albicans to Fn. The mannan effect was dose dependent. However, adherence of C. albicans to Fn was not significantly reduced by mannose, glucose, or several other sugars. The role of FN as a receptor for the binding of C. albicans yeast cells to buccal and vaginal epithelial cells was investigated also using an in vitro assay. We determined, using indirect fluorescent antibody techniques, that both buccal and vaginal epithelial cells possessed Fn. In addition, yeast cells, when pretreated with Fn, showed reduced adherence with buccal and vaginal cells when compared with nontreated cells. These studies may indicate a role for Fn in the adherence of C. albicans to buccal and vaginal epithelial cells.

scholarly journals THE DETECTION OF A VIRAL INTERFERING SUBSTANCE IN THE SHOPE PAPILLOMA AND THE Vx7 AND Vx2 CARCINOMAS

1967 ◽  
Vol 126 (5) ◽  
pp. 887-897
Author(s):  
Deborah Pavan Langston ◽  
Leslie H. Sobin
Keyword(s):  
Nucleic Acid ◽  
Fluorescent Antibody ◽  
In Vitro Assay ◽  
Moderate Activity ◽  
Protein Extract ◽  
Viral Nucleic Acid ◽  
Vitro Assay ◽  
Protein Coat

In vivo assay of Shope papilloma protein extract and in vitro assay of extracts from Shope papilloma, Vx7 and Vx2 carcinomas showed strong interferon-like activity in the papilloma and moderate activity in the carcinomas. The interpretation is that the presence of viral nucleic acid in all three tumors stimulated the production of this substance even though fluorescent antibody studies reveal the protein coat only in the papilloma and Vx7.

scholarly journals Identification and Functional Characterization of a Novel Nuclear Localization Signal Present in the Yeast Nab2 Poly(A)+ RNA Binding Protein

1998 ◽  
Vol 18 (3) ◽  
pp. 1449-1458 ◽  
Author(s):  
Ray Truant ◽  
Robert A. Fridell ◽  
R. Edward Benson ◽  
Hal Bogerd ◽  
Bryan R. Cullen
Keyword(s):  
Nuclear Localization ◽  
Nuclear Import ◽  
Nuclear Localization Signal ◽  
Nuclear Export ◽  
Mammalian Cells ◽  
Rna Binding ◽  
Yeast Cells ◽  
Vitro Assay ◽  
Localization Signal

ABSTRACT The nuclear import of proteins bearing a basic nuclear localization signal (NLS) is dependent on karyopherin α/importin α, which acts as the NLS receptor, and karyopherin β1/importin β, which binds karyopherin α and mediates the nuclear import of the resultant ternary complex. Recently, a second nuclear import pathway that allows the rapid reentry into the nucleus of proteins that participate in the nuclear export of mature mRNAs has been identified. In mammalian cells, a single NLS specific for this alternate pathway, the M9 NLS of heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1), has been described. The M9 NLS binds a transport factor related to karyopherin β1, termed karyopherin β2 or transportin, and does not require a karyopherin α-like adapter protein. A yeast homolog of karyopherin β2, termed Kap104p, has also been described and proposed to play a role in the nuclear import of a yeast hnRNP-like protein termed Nab2p. Here, we define a Nab2p sequence that binds to Kap104p and that functions as an NLS in both human and yeast cells despite lacking any evident similarity to basic or M9 NLSs. Using an in vitro nuclear import assay, we demonstrate that Kap104p can direct the import into isolated human cell nuclei of a substrate containing a wild-type, but not a defective mutant, Nab2p NLS. In contrast, other NLSs, including the M9 NLS, could not function as substrates for Kap104p. Surprisingly, this in vitro assay also revealed that human karyopherin β1, but not the Kap104p homolog karyopherin β2, could direct the efficient nuclear import of a Nab2p NLS substrate in vitro in the absence of karyopherin α. These data therefore identify a novel NLS sequence, active in both yeast and mammalian cells, that is functionally distinct from both basic and M9 NLS sequences.

scholarly journals Cell cycle expression of RNA duplex unwindase activity in mammalian cells.

1988 ◽  
Vol 8 (2) ◽  
pp. 770-777 ◽  
Author(s):  
R W Wagner ◽  
K Nishikura
Keyword(s):  
Cell Cycle ◽  
Burkitt Lymphoma ◽  
Mammalian Cells ◽  
Somatic Cells ◽  
Mouse Fibroblast ◽  
In Vitro Assay ◽  
3T3 Cells ◽  
Vitro Assay ◽  
Gel Retardation Assay

An RNA duplex unwindase activity has been found by using an in vitro assay with various types of mammalian, somatic cells, including HeLa, mouse plasmacytoma, and Burkitt lymphoma. The unwindase activity is very low in mouse fibroblast 3T3 cells arrested into quiescence, but increases when the cells are released into renewed growth by serum. In addition, a gel retardation assay proved to be specific and sensitive for detection of RNA duplex-unwindase complexes.

An adapted in vitro assay to assess Campylobacter jejuni interaction with intestinal epithelial cells: Taking into stimulation with TNFα

2018 ◽  
Vol 149 ◽  
pp. 67-72 ◽  
Author(s):  
Ramila Cristiane Rodrigues ◽  
Anne-Lise Pocheron ◽  
Jean-Michel Cappelier ◽  
Odile Tresse ◽  
Nabila Haddad
Keyword(s):  
Epithelial Cells ◽  
Campylobacter Jejuni ◽  
Intestinal Epithelial Cells ◽  
In Vitro Assay ◽  
Intestinal Epithelial ◽  
Vitro Assay

A simple quantitative in vitro assay for thymocyte adhesion to thymic epithelial cells using a fluorescein diacetate

1993 ◽  
Vol 157 (1-2) ◽  
pp. 117-123 ◽  
Author(s):  
Yasuyuki Maeda ◽  
Kazuo Tanaka ◽  
Yasuhiro Koga ◽  
Xin-Ying Zhang ◽  
Masafumi Sasaki ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
In Vitro Assay ◽  
Fluorescein Diacetate ◽  
Thymic Epithelial Cells ◽  
Vitro Assay

Cultured gill epithelial cells from tilapia (Oreochromis niloticus): a new in vitro assay for toxicants

2005 ◽  
Vol 71 (1) ◽  
pp. 61-72 ◽  
Author(s):  
Bingsheng Zhou ◽  
Wenhua Liu ◽  
Rudolf S.S. Wu ◽  
Paul K.S. Lam
Keyword(s):  
Epithelial Cells ◽  
Oreochromis Niloticus ◽  
In Vitro Assay ◽  
Vitro Assay

scholarly journals Synthesis and Biological Evaluation of Haloalkyl Phosphate Triester Derivatives of araA and araC

1992 ◽  
Vol 3 (2) ◽  
pp. 79-84 ◽  
Author(s):  
C. McGuigan ◽  
B. C. N. M. Jones ◽  
S. M. Tollerfield ◽  
P. A. Riley
Keyword(s):  
Epithelial Cells ◽  
Antiviral Drug ◽  
Biological Evaluation ◽  
In Vitro Assay ◽  
Vitro Assay ◽  
Free Nucleotides ◽  
Synthesis And Biological Evaluation ◽  
Derivatives Of

Novel phosphate triester derivatives of the antiviral drug araA and the anti-leukaemic agent araC have been prepared as membrane-soluble pro-drugs of the bio-active free nucleotides. In particular, novel trichloro- and trifluoroethyl phosphates have been prepared using phosphorochloridate chemistry, and are fully characterized. An in vitro assay indicates inhibition, by each of the compounds, of thymidine incor-portion by mammalian epithelial cells. It is notable that the trichloroethyl derivative is most active in each case, and in the case of araC its activity appears to exceed that of the parent nucleoside.

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