Thesis (Ph. D.)--University of Virginia, 2002. / Includes bibliographical references (leaves 178-194). Also available online through Digital Dissertations.

Thesis supervisor: Joshua A. Weiner. Includes bibliographic references (p. 108-126).

Thesis supervisor: Charles A. Yeaman. Includes bibliographic references (p. 128-139).

Thesis (Ph. D.)--University of Wisconsin--Madison, 1981. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Cell adhesion molecules enhance Interactions between adjacent cells In order to mediate a large variety of functions of the Immune system. An antibody against the murine lymphocyte surface antigen MALA-2 has previously been shown to Inhibit mixed lymphocyte response. A λgt10 cDNA library from NS-1 cells was screened and a cDNA clone, K3-1.1, was previously isolated. It had significant homology to the human ICAM-1 gene. This thesis covers the isolation of a second cDNA clone, K4-1.1, and its comparison to K3-1.1 In terms of expression, function and distribution. The two clones are identical in sequence with the exception of the 5’ ends. Expression of these two clones was examined using a transient expression system of COS cell transfection. Cell surface expression of the K3-1.1 clone could not be detected by FACS analysis. Even when the 5' untranslated region of the K3-1.1 clone (which has 10 potential translation start sites) was removed, protein could not be detected at the cell surface, intracellularly, or extracellularly. However, K4-1.1 expression was detected at the cell surface. Northern blot analysis reveals that there are two distinct messages which are likely to be represented by the two clones. When the northern blot was probed with the 5' end of the K3-1.1 clone, only one of the messages was detected. This together with the result of Southern blot analysis suggests that the two messages are likely the result of alternate splicing. In order to examine the interactions of the murine ICAM-1 with the surface of other cells, an expression system which would produce large amounts of a secreted soluble form was established. The soluble protein was purified from the supernatant of transfected cells by an antibody-affinity column and used in preliminary binding assays. / Medicine, Faculty of / Medical Genetics, Department of / Graduate

No description available.

Abstract not available

Thesis (Ph. D. in Cancer Biology)--Vanderbilt University, May 2007. / Title from title screen. Includes bibliographical references.

Cell adhesion to extracellular matrices (ECM) is essential to numerous physiological and pathological processes. Cell adhesion is initiated by binding of the transmembrane integrin family of receptors to an ECM ligand such as fibronectin (FN). Once bound, integrins cluster together and form focal adhesions (FA). FAs serve as structural links and signal transduction elements between the cell and its extracellular environment. While a great deal of progress has been made in identifying the biochemical components that comprise focal adhesions and the roles they play in migration, cell spreading, and signaling, the contributions of these proteins to mechanical interactions between the cell and its environment remain poorly understood. A FA adhesion protein of particular importance is vinculin. When localized to focal adhesions, vinculin forms a ternary complex with talin and 1-integrin. This 1-integrin-talin-vinculin complex plays a central role in the regulation of FA assembly and cell spreading and migration. Nevertheless, the specific contribution to adhesive force generation of the 1-integrin-talin-vinculin complex remains poorly understood. The objective of this project was to analyze the role of vinculin in the cell adhesion strengthening process. Our central hypothesis is that vinculin modulates adhesion strength via regulating the size and/or composition of the integrin-talin-vinculin complex. We used a novel combination of biochemical reagents and engineering techniques along with quantitative and sensitive adhesion strength measurements to provide new insights into how the structure of vinculin contributes to cell adhesion strength.

Diss. (sammanfattning) Stockholm : Karol. inst., 2002. / Härtill 5 uppsatser.