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Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5.
Giannelli G, Falk-Marzillier J, Schiraldi O, Stetler-Stevenson WG, Quaranta V
(1997) Science 277: 225-8
MeSH Terms: Animals, Breast, Cell Adhesion, Cell Adhesion Molecules, Cell Division, Cell Line, Cell Movement, Cell Size, Collagenases, Epithelial Cells, Epithelium, Extracellular Matrix, Female, Fibrinolysin, Gelatinases, Humans, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9, Metalloendopeptidases, Mice, Phenylalanine, Protease Inhibitors, Rats, Recombinant Fusion Proteins, Skin Neoplasms, Thiophenes
Show Abstract · Added March 27, 2014
Structural changes in the extracellular matrix are necessary for cell migration during tissue remodeling and tumor invasion. Specific cleavage of laminin-5 (Ln-5) by matrix metalloprotease-2 (MMP2) was shown to induce migration of breast epithelial cells. MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling.
1 Communities
1 Members
0 Resources
26 MeSH Terms
An edgewise look at basal epithelial cells: three-dimensional views of the rat prostate, mammary gland and salivary gland.
Hayward SW, Brody JR, Cunha GR
(1996) Differentiation 60: 219-27
MeSH Terms: Actins, Animals, Basal Metabolism, Cell Size, Epithelial Cells, Female, Image Processing, Computer-Assisted, Immunohistochemistry, Keratins, Male, Mammary Glands, Animal, Pregnancy, Prostate, Rats, Rats, Sprague-Dawley, Salivary Glands
Show Abstract · Added December 10, 2013
Wholemount immunocytochemical staining was used to visualize basal and luminal epithelial-cell-specific cytokeratin and smooth muscle alpha-actin expression in the developing and adult rat prostate, in the pregnant rat mammary gland and adult rat salivary gland. The stained samples were examined using an Edge R400 3D microscope. Images were collected in both single-image and stereo-pair formats. Prostatic basal epithelial cells were found to have a cell body covering an area of 52-62 microns 2. The mean footprint size of basal cells was not significantly different between prostatic lobes. Basal epithelial cells were most dense in the anterior and most sparse in the ventral prostatic lobes. Basal epithelial cells had a large body with many processes, which spread around the duct and projected between luminal cells towards the lumen. These processes closely approached their counterparts from adjacent basal cells. In the developing prostate the differentiation of the basal cells from undifferentiated epithelial cords was observed at the region of ductal widening associated with canalization. Following castration prostatic basal epithelial cells became more closely packed, though the size of individual cells was not significantly changed. There was a two-to four-fold increase in basal cell density by 7 days after surgery. Most prostatic luminal cells were found to have hexagonal bases though some were pentagonal in shape. Luminal cells had a mean basal area of 50 microns 2. In the prostate immunocytochemical staining against smooth muscle alpha-actin revealed discrete bands of muscle surrounding individual prostatic ducts. In the mammary and salivary glands the epithelium was organized into an alveolar arrangement. In the salivary gland a single basal epithelial cell covered the top of each alveolus with processes arranged down the side of the structure. In the mammary gland several basal cells were draped over each alveolus. The mammary and salivary gland basal cells expressed smooth muscle alpha-actin, indicating their myoepithelial phenotype. The organization of the mammary and salivary gland basal cells placed them in an ideal position to squeeze the alveolar structures.
0 Communities
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16 MeSH Terms
The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts.
Reynolds AB, Daniel JM, Mo YY, Wu J, Zhang Z
(1996) Exp Cell Res 225: 328-37
MeSH Terms: 3T3 Cells, Animals, Cadherins, Catenins, Cell Adhesion Molecules, Cell Size, Cytoskeletal Proteins, DNA, Dendrites, Gene Expression, Mice, Mutation, Phenotype, Phosphoproteins, Protein Binding, Protein Structure, Tertiary, Repetitive Sequences, Nucleic Acid, Trans-Activators, beta Catenin
Show Abstract · Added March 5, 2014
p120cas (CAS) is a tyrosine kinase substrate whose phosphorylation has been implicated in cell transformation by Src and in ligand-induced signaling through the EGF, PDGF, and CSF-1 receptors. More recently, CAS has been shown to associate with E-cadherin and its cofactors (catenins), molecules that are involved in cell adhesion. Although both CAS and beta-catenin contain armadillo repeat domains (Arm domains), the amino acid identity between these proteins in this region is only 22%, and it is not yet clear whether CAS will emulate other catenins by associating with other members of the cadherin family. Here we report that in addition to binding E-cadherin, wild-type CAS associated with N-cadherin and P-cadherin. Transient transfection of cloned CAS isoforms into MDCK epithelial cells indicated that CAS1 and CAS2 isoforms are equally capable of binding to E-cadherin even though these cells preferentially express CAS2 isoforms. In addition, CAS colocalized with N-cadherin in NIH3T3 cells and analysis of CAS mutants in vivo indicated that the CAS-N-cadherin interaction requires an intact CAS Arm domain. The data suggest that CAS-cadherin interactions in general are dictated by the conserved armadillo repeats and are not heavily influenced by sequences added outside the Arm domain by alternative splicing. Interestingly, overexpression of CAS in NIH3T3 cells induced a striking morphological phenotype characterized by the presence of long dendrite-like processes. This branching phenotype was specific for CAS, since (i) overexpression of the structurally similar beta-catenin had little effect on cell morphology, and (ii) the branching was abolished by deletions in the CAS Arm domain. Our data indicate that, like other catenins, CAS is a cofactor for multiple members of the cadherin family. However, the dramatically distinct phenotype exhibited by fibroblasts overexpressing CAS, versus beta-catenin, support recent data suggesting that these catenins have fundamentally different and possibly opposing roles in cadherin complexes.
1 Communities
1 Members
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19 MeSH Terms
Cellular tensegrity: exploring how mechanical changes in the cytoskeleton regulate cell growth, migration, and tissue pattern during morphogenesis.
Ingber DE, Dike L, Hansen L, Karp S, Liley H, Maniotis A, McNamee H, Mooney D, Plopper G, Sims J
(1994) Int Rev Cytol 150: 173-224
MeSH Terms: Animals, Biomechanical Phenomena, Cell Division, Cell Movement, Cell Size, Cells, Cultured, Cytoskeleton, Embryonic and Fetal Development, Morphogenesis
Added May 22, 2014
0 Communities
1 Members
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9 MeSH Terms
Taxol-treated fibroblasts acquire an epithelioid shape and a circular pattern of actin bundles.
Pletjushkina OJ, Ivanova OJ, Kaverina IN, Vasiliev JM
(1994) Exp Cell Res 212: 201-8
MeSH Terms: 3T3 Cells, Actin Cytoskeleton, Actins, Animals, Cell Adhesion, Cell Size, Cytoskeleton, Demecolcine, Epithelial Cells, Intermediate Filaments, Mice, Microtubules, Myosins, Paclitaxel, Rats, Tubulin, Vimentin, Vinculin
Show Abstract · Added December 10, 2013
The effects of two microtubule-specific drugs, taxol and colcemid, upon the cell shape and cytoskeleton of several types of cultured fibroblastic cells were compared. While colcemid depolymerized completely the whole microtubular system, taxol induced decentralization of this system, leading to formation of numerous free microtubules filling the central cytoplasm. Morphometric determinations of two cell shape parameters, dispersion and elongation (G. Dunn and A. Brown, J. Cell Sci. (1986) 83, 313-340), have shown that, in all the tested cultures, taxol induced significantly larger decreases of average dispersion than colcemid; in addition, most taxol-treated cells, but not colcemid-treated ones, developed circumferential bundles of actin microfilaments instead of straight bundles. These results show that decentralization of the microtubular system, in contrast to its complete depolymerization, leads to the transformation of a polarized "fibroblast-like" cell morphology to an "epithelioid" morphology characterized by the smooth discoid cell shape and a circular actin pattern. Possible mechanisms of this transformation are briefly discussed.
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18 MeSH Terms
Rapid spreading and mature hemidesmosome formation in HaCaT keratinocytes induced by incubation with soluble laminin-5r.
Hormia M, Falk-Marzillier J, Plopper G, Tamura RN, Jones JC, Quaranta V
(1995) J Invest Dermatol 105: 557-61
MeSH Terms: Animals, Carcinoma, Cell Adhesion, Cell Line, Transformed, Cell Size, Culture Media, Conditioned, Extracellular Matrix Proteins, Humans, Immune Sera, Intercellular Junctions, Keratinocytes, Laminin, Neoplasm Proteins, Rats, Solubility, Tumor Cells, Cultured, Urinary Bladder Neoplasms, Wound Healing
Show Abstract · Added March 27, 2014
HaCaT cells, an immortalized keratinocyte line, incubated in plastic wells in the presence of conditioned medium from 804G cells adhered and spread rapidly in less than 30 min. In contrast, cells plated in fibroblast or keratinocyte conditioned medium adhered poorly and remained rounded at 30 min. Immunodepletion of 804G conditioned medium with polyclonal antisera to laminin-5r, but not control antisera, abolished rapid cell spreading. Electron microscopy of HaCaT cells spread by incubation in 804G conditioned medium, but not control medium, revealed mature hemidesmosomes after 24 h. Rapid spreading was also observed in wells precoated with 804G conditioned medium or 804G cell-deposited matrix, but not with fibronectin, vitronectin, or laminin-1. Immunoblotting of 804G conditioned medium with anti-laminin-5r antibodies unveiled polypeptides of 150, 140, 135, and 100 kDa, identical by electrophoretic mobility to immunoreactive polypeptides in 804G deposited matrix. Our results suggest that addition of laminin-5r in a soluble form is sufficient to promote rapid spreading and hemidesmosome assembly in keratinocytes. The mechanism of soluble laminin-5r action may include efficient surface "priming" for cell adhesion. Soluble laminin-5r may have a physiologic role in morphogenesis and repair of the epidermis and may be of use for therapeutic applications.
1 Communities
1 Members
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18 MeSH Terms