Intestinal epithelial restitution. Characterization of a cell culture model and mapping of cytoskeletal elements in migrating cells.

Nusrat, Asma; Delp, C; Madara, James L.

doi:10.1172/jci115741

Cited by 221 publications

(183 citation statements)

References 35 publications

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“…Because villin has a higher affinity for PIP 2 than PLC-␥ 1 , villin could sequester PIP 2 and release PIP 2 following tyrosine phosphorylation (in response to receptor activation) and thus play a role as a signal-generating actin-regulatory protein (33). (iii) Villin is localized to the leading edge of intestinal epithelial cells (73,74). Association of villin with PIP 2 could regulate actin assembly in the vicinity of the plasma membrane by inhibiting severing and capping, thus accelerating actin assembly, and by increasing actin bundling it can stabilize the cell surface protrusion, thus regulating cell shape change as well as cell motility.…”

Section: Discussionmentioning

confidence: 99%

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Kumar

Zhao

Tomar

et al. 2004

Journal of Biological Chemistry

101

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Section: Discussionmentioning

confidence: 99%

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Kumar

Zhao

Tomar

et al. 2004

Journal of Biological Chemistry

101

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“…In the gastrointestinal mucosa, cell proliferation and migration play a fundamental role in the organization and maintenance of tissue integrity (50). When damaged, the gastrointestinal mucosa has a remarkable ability to repair itself very rapidly.…”

Section: Discussionmentioning

confidence: 99%

Vasopressin-mediated mitogenic signaling in intestinal epithelial cells

Chiu

Santiskulvong

et al. 2002

American Journal of Physiology-Cell Physiology

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Here, we demonstrate that arginine vasopressin (AVP) induces multiple intracellular signal transduction pathways in rat intestinal epithelial IEC-18 cells via a V 1A receptor. Addition of AVP to these cells induces a rapid and transient increase in cytosolic Ca 2ϩ concentration and promotes protein kinase D (PKD) activation through a protein kinase C (PKC)-dependent pathway, as revealed by in vitro kinase assays and immunoblotting with an antibody that recognizes autophosphorylated PKD at Ser 916 . AVP also stimulates the tyrosine phosphorylation of the nonreceptor tyrosine kinase proline-rich tyrosine kinase 2 (Pyk2) and promotes Src family kinase phosphorylation at Tyr 418 , indicative of Src activation. AVP induces extracellular signal-related kinase (ERK)-1 (p44 mapk ) and ERK-2 (p42 mapk ) activation, a response prevented by treatment with mitogen-activated protein kinase kinase (MEK) inhibitors (PD-98059 and U-0126), specific PKC inhibitors (GF-I and Ro-31-8220), depletion of Ca 2ϩ (EGTA and thapsigargin), selective epidermal growth factor receptor (EGFR) tyrosine kinase inhibitors (tyrphostin AG-1478, compound 56), or the selective Src family kinase inhibitor PP-2. Furthermore, AVP acts as a potent growth factor for IEC-18 cells, inducing DNA synthesis and cell proliferation through ERK-, Ca 2ϩ -, PKC-, EGFR tyrosine kinase-, and Src-dependent pathways. arginine vasopressin; protein kinase D; protein kinase C; Src; proline-rich tyrosine kinase 2; intestinal epithelial proliferation THE SEQUENTIAL PROLIFERATION, lineage-specific differentiation, migration, and cell death of epithelial cells of the intestinal mucosa is a tightly regulated process that is modulated by a broad spectrum of regulatory peptides (8,36,70). The nontransformed IEC-6 and IEC-18 cells, derived from rat small intestinal crypt (56), have provided an in vitro model to examine intestinal epithelial cell migration, differentiation, and proliferation (16,27,58,70). Previous studies demonstrated that the proliferation and migration of these intestinal epithelial cells is regulated by a variety of polypeptide growth factors, including epidermal growth factor (EGF), insulin-like growth factor I, and hepatocyte growth factor, which act via single-pass transmembrane tyrosine kinase receptors (3,17,51). Neuropeptides and vasoactive peptides that signal through G protein-coupled receptors (GPCRs), characterized by seven-transmembrane helices, also act as potent cellular growth factors for a variety of cell types (63,64,66,67). However, the role of GPCRs and their ligands in intestinal epithelial cell signaling and proliferation remains poorly understood.The neurohypophysial nonapeptide arginine vasopressin (AVP), also known as antidiuretic hormone, is traditionally recognized for its role as a vasoconstrictor hormone acting on vascular smooth muscle cells and its antidiuretic effect via the renal collecting system. In addition to its function in the regulation of body fluid osmolality, vascular tone, and blood pressure, AVP acts as a growth-promo...

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“…ITF is a cytoprotective peptide secreted by intestinal goblet cells [16]. ITF has an important role during intestinal epithelial migration [12,17], a major step of the restitution process [32], but its mechanism of action remains unclear. Previous investigations showed that intestinal epithelial cells constitutively release NO in itro [33,34].…”

Section: Discussionmentioning

confidence: 99%

Intestinal trefoil factor binds to intestinal epithelial cells and induces nitric oxide production: priming and enhancing effects of mucin

Tan

Liu

Hsueh

et al. 1999

Biochemical Journal

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Intestinal trefoil factor (ITF or TFF3), NO and epitheliumassociated mucin have important roles in sustaining mucosal integrity in the gastrointestinal tract. In the present study we examined ITF-binding molecules on IEC-18 cells (an intestinal epithelial cell line) with the use of flow cytometry and localized these molecules on the cell surface by confocal microscopy. Furthermore, we studied the interaction of mucin and ITF and their co-operative effect on NO production by the epithelium.

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Intestinal epithelial restitution. Characterization of a cell culture model and mapping of cytoskeletal elements in migrating cells.

Abstract: Closure of superficial wounds in epithelia occurs by migration of cells shouldering the wound. We describe an in vitro model of such restitution using a human intestinal epithelial cell line,

Cited by 221 publications

References 35 publications

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Association of Villin with Phosphatidylinositol 4,5-Bisphosphate Regulates the Actin Cytoskeleton

Vasopressin-mediated mitogenic signaling in intestinal epithelial cells

Intestinal trefoil factor binds to intestinal epithelial cells and induces nitric oxide production: priming and enhancing effects of mucin

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