Myosin‐mediated cytoskeleton contraction and Rho GTPases regulate laminin‐5 matrix assembly

deHart, Gregory W.; Jones, Jonathan

doi:10.1002/cm.10161

Cited by 17 publications

(13 citation statements)

References 68 publications

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“…Moreover, inhibition of the small GTPases also inhibits assembly of laminin-311 fibers in the ma- trix of our alveolar epithelial cells. Indeed, the assembly of laminin-311 fibers in the matrix of alveolar epithelial cells involves the same molecules that regulate assembly of laminin-5 matrix in keratinocytes (deHart et al 2003;deHart and Jones 2004). In the latter instance, laminin-5 matrix assembly is perturbed by antagonists of various integrins and the small GTPases (deHart and Jones 2004).…”

Section: Discussionmentioning

confidence: 99%

Laminin-311 (Laminin-6) Fiber Assembly by Type I-like Alveolar Cells

DeBiase

Lane

Budinger

et al. 2006

J Histochem Cytochem.

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S U M M A R Y Two epithelial cell types cover the alveolar surface of the lung. Type II alveolar epithelial cells produce surfactant and, during development or following wounding, give rise to type I cells that are involved in gas exchange and alveolar fluid homeostasis. In culture, freshly isolated alveolar type II cells assume a more squamous (type I-like) appearance within 4 days after plating. They assemble numerous focal adhesions that associate with the actin cytoskeleton at the cell margins. These alveolar epithelial cells lose expression of type II cell markers including SP-C and after 4 days in culture express the type I cell marker T1a. Those cells that express T1a also deposit fibers of laminin-311 in their matrix. The latter appears to be related to their development of a type I phenotype because freshly isolated, primary type I cells also assemble laminin-311-rich fibers in vitro. A b1 integrin antibody antagonist inhibits the assembly of laminin-311 matrix fibers. Moreover, the formation of laminin fibers is dependent on the activity of the small GTPases and is perturbed by ML-7, a myosin light chain kinase inhibitor. In summary, our data indicate that assembly of laminin-311 fibers by lung epithelial cells is integrin and actin cytoskeleton dependent, and that these fibers are characteristic of type I alveolar cells. (J Histochem Cytochem 54:665 -672, 2006)

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Section: Discussionmentioning

confidence: 99%

Laminin-311 (Laminin-6) Fiber Assembly by Type I-like Alveolar Cells

DeBiase

Lane

Budinger

et al. 2006

J Histochem Cytochem.

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“…α3β1 integrin signaling is also involved in laminin-332 matrix assembly by normal and tumor cells [87,88]. This appears to involve Rho-GTPases, stress fiber and focal contact formation and is dependent on the protein T-lymphoma invasion and metastasis 1 (Tiam1) [87,88].…”

Section: Section 2 Part 3: Laminin-332 Signal Transduction In Cancermentioning

confidence: 99%

Laminin-332-Integrin Interaction: A Target For Cancer Therapy?

Tsuruta

Kobayashi²,

Imanishi³

et al. 2008

CMC

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For many years, extracellular matrix (ECM) was considered to function as a tissue support and filler. However, we now know that ECM proteins control many cellular events through their interaction with cell-surface receptors and cytoplasmic signaling pathways. For example, they regulate cell proliferation, cell division, cell adhesion, cell migration, and apoptosis. We focus in this review on a laminin isoform, laminin-332 (formerly termed laminin-5), a major component of the basement membrane (BM) of skin and other epithelial tissues. It is composed of 3 subunits (α3, β3, and γ2) and interacts with at least two integrin receptors expressed by epithelial cells (α3β1 and α6β4 integrin). Mutations in either laminin-332 or integrin α6β4 result in junctional epidermolysis bullosa, a blistering skin disease, while targeting of laminin-332 by autoantibodies in cicatricial pemphigoid leads to dysadhesion of epithelial cells from their underlying connective tissue. Abnormal expression of laminin-332 and its integrin receptors is also a hallmark of certain tumor types and is believed to promote invasion of colon, breast and skin cancer cells. Moreover, there is emerging evidence that laminin-332 and its protease degradation products are not only found at the leading front of several tumors but also likely induce and/or promote tumor cell migration. Thus, in this review, we focus specifically on the role of laminin-332 and its integrin receptors in adhesion, proliferation, and migration/invasion of cancer cells. Finally, we discuss strategies for the development of laminin-332-based antagonists for the treatment of malignant tumors.

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“…Since Rac1 activity is partially-dependent on Cdc42, such a defect might also be observable in the absence of Cdc42. Finally, dominant negative Cdc42 interfered with the normal deposition of laminin 5 into the matrix of a squamous cell carcinoma cell line (DeHart and Jones, 2004). These data suggested that Cdc42 might be involved in BM maintenance, however, no study has addressed this question directly.…”

Section: Introductionmentioning

confidence: 97%