Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members

Huang, Jing; Bridges, Lance C.; White, Judith M.

doi:10.1091/mbc.e05-03-0258

Cited by 87 publications

(77 citation statements)

References 35 publications

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“…ADAM 12 has proteolytic activity against insulin-like growth factor binding proteins 3 (IGFBP-3) (Shi et al, 2000) and insulin-like growth factor binding proteins 5 (IGFBP-5) and is probably responsible for at least part of the increased IGFBP-3 and IGFBP-5 protease activity seen in pregnancy (Giudice et al, 1990;Hossenlopp et al, 1990). ADAM 12 is involved in cell adhesion (Huang et al, 2005), myogenic and adipogenic transformation (Kawaguchi et al, 2003;Lafuste et al, 2005;Yi et al, 2005), apoptosis (Kveiborg et al, 2005), and cell fusion, and modulation of the local effect, and bioavailability of IGF-I and IGF-II, and other growth factors (Rosenfeld and Roberts, 1999). ADAM 12 is probably of importance for placental and fetal growth.…”

Section: Introductionmentioning

confidence: 99%

ADAM 12 as a second‐trimester maternal serum marker in screening for Down syndrome

et al. 2007

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Background ADAM 12 is a placenta-derived glycoprotein that is involved in growth and differentiation. The maternal serum concentration of ADAM 12 is a potential first-trimester maternal serum marker of Down syndrome (DS). Here we examine the potential of ADAM 12 as a second-trimester maternal serum marker of DS. Materials and MethodsThe concentration of ADAM 12 was determined in gestational week 14-19 in 88 DS pregnancies and 341 matched control pregnancies. Medians of normal pregnancies were established by polynomial regression and the distribution of log 10 MoM ADAM 12 values in DS pregnancies and controls determined. Correlations with alpha-fetoprotein (AFP) and free β-human chorionic gonadotrophin (free β-hCG) were established and used to model the performance of maternal serum screening with ADAM 12 in combination with other second-trimester serum markers. ResultsThe ADAM 12 maternal serum concentration was significantly increased with a median MoM of 1.85 and a mean log 10 MoM (SD) of 0.268 (0.2678) compared to a mean log 10 MoM (SD) of 0.013 (0.4318) in controls. ADAM 12 correlated with maternal weight and ethnicity (with the serum concentration increased in Afro-Caribbeans), but neither with maternal age nor gestational age, and only marginally with AFP (r(DS) = 0.078, r(controls) = 0.093) and free β-hCG (r(DS) = 0.073, r(controls) = 0.144. The increase in detection rate-for a false positive rate of 5%-by adding ADAM 12 to the double test (AFP + free β-hCG) was 4%, similar to that of adding uE3 to the double test.Conclusion ADAM 12 is an efficient second-trimester marker for DS. Further studies should be conducted to determine whether it may be a useful additonal or alternative marker to those currently used in the secondtrimester.

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Section: Introductionmentioning

confidence: 99%

ADAM 12 as a second‐trimester maternal serum marker in screening for Down syndrome

et al. 2007

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“…Several integrins are known to interact with ADAM disintegrin-like domain (55,56). EDC-motif D 468 within disintegrin-like loop sequence of ADAM17 was shown to be crucial in facilitating integrin-dependent cell adhesion (57). ADAM 17 was also found to interact with ␣ 5 ␤ 1 integrin in human dermal fibroblast cells (58) and to act as a specific ligand for the integrin ␣ 5 ␤ 1 in HeLa cells (59) and mediate cell migration (57).…”

Section: Discussionmentioning

confidence: 99%

“…EDC-motif D 468 within disintegrin-like loop sequence of ADAM17 was shown to be crucial in facilitating integrin-dependent cell adhesion (57). ADAM 17 was also found to interact with ␣ 5 ␤ 1 integrin in human dermal fibroblast cells (58) and to act as a specific ligand for the integrin ␣ 5 ␤ 1 in HeLa cells (59) and mediate cell migration (57). The biological relevance of these connections is reflected for example in the cleavage by ADAM17 of VCAM-1, .…”

Section: Discussionmentioning

confidence: 99%

Strain-induced Differentiation of Fetal Type II Epithelial Cells Is Mediated via the Integrin α6β1-ADAM17/Tumor Necrosis Factor-α-converting Enzyme (TACE) Signaling Pathway

Wang

Huang

Nayak

et al. 2013

Journal of Biological Chemistry

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Background: Mechanical forces are critical for normal fetal lung development. Results: Force applied to ␣ 6 ␤ 1 integrin activates TACE and sheds HB-EGF and TGF-␣. Conclusion: Mechanical strain enhances binding of ␣6␤1 integrin to TACE to promote fetal type II cell differentiation. Significance: Learning how mechanical forces regulate fetal lung development is critical for the discovery of approaches to accelerate lung maturation.

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“…The reports dealing with the functional interplay between ADAMs and integrins indicate that ADAMs can modulate, by inhibiting or supporting, cell migration mediated by integrins independently of their metalloprotease activity (37). These interactions may play an important role in promoting cell migration in physiological processes, such as during embryogenesis, as well as in cancer cell invasion.…”

Section: Discussionmentioning

confidence: 99%

Role of ADAM-9 Disintegrin-Cysteine-rich Domains in Human Keratinocyte Migration

Zigrino

Steiger

Fox

et al. 2007

Journal of Biological Chemistry

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ADAM-9 belongs to a family of transmembrane, disintegrincontaining metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. The aim of this study was to analyze the expression of ADAM-9 in skin and to assess the role of this proteolytic/adhesive protein in skin physiology. In normal skin, ADAM-9 expression was detected in both the epidermis and dermis and in vitro in keratinocytes and fibroblasts. Here we report that ADAM-9 functions as a cell adhesion molecule via its disintegrin-cysteine-rich domain. Using solid phase binding assays and antibody inhibition experiments, we demonstrated that the recombinant disintegrin-cysteine-rich domain of ADAM-9 specifically interacts with the ␤1 integrin subunit on keratinocytes. This was corroborated by co-immunoprecipitation. In addition, engagement of integrin receptors by the disintegrin-cysteine-rich domain resulted in ERK phosphorylation and increased MMP-9 synthesis. Treatment with the ERK inhibitor PD98059 inhibited MMP-9 induction. Furthermore, the presence of the soluble disintegrin-cysteine-rich domain did not interfere with cell migration on different substrates. However, keratinocytes adhering to the immobilized disintegrin-cysteine-rich domain showed increased motility, which was partially due to the induction of MMP-9 secretion. In summary, our results indicate that the ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with ␤1 integrins and modulates MMP synthesis.Degradation of the extracellular matrix is a prerequisite for tissue repair but also for cell migration and for release of bound factors and bioactive peptides. Different proteases have been implicated in these processes, such as the matrix metalloproteinase (MMP), 2 serine, cysteine, and aspartic protease families. In recent years, the family of proteases (a disintegrin and metalloproteinase (ADAM)) has drawn attention because the manifold proteolytic and adhesive activities of the different ADAM family members were attributed a pivotal role in physiological and pathological situations.The ADAM family includes ϳ30 members of proteins containing disintegrin-and metalloprotease-like domains. Most of the family members share a common well conserved domain structure, including a prodomain, metalloprotease, disintegrinlike, cysteine-rich, EGF-like, and a short cytoplasmic domain (reviewed in Refs. 1 and 2).Structurally, the ADAMs are most closely related to the P-III snake venom metalloproteases. However, in contrast to snake venom metalloproteases, most ADAMs possess EGF-like, transmembrane, and cytoplasmic domains. Half of the ADAM proteins are predicted to be active metalloproteinases, although the identification of specific substrates is still lacking for most of them. Various cell surface proteins are shed by ADAMs, such as IL-6 receptor, FAS-ligand, transforming growth factor-␣, tumor necrosis factor-␣, heparin-binding EGF, and L-selectin. The release of soluble forms of these proteins might lead to autocrine and di...

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Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members

Cited by 87 publications

References 35 publications

ADAM 12 as a second‐trimester maternal serum marker in screening for Down syndrome

ADAM 12 as a second‐trimester maternal serum marker in screening for Down syndrome

Strain-induced Differentiation of Fetal Type II Epithelial Cells Is Mediated via the Integrin α6β1-ADAM17/Tumor Necrosis Factor-α-converting Enzyme (TACE) Signaling Pathway

Role of ADAM-9 Disintegrin-Cysteine-rich Domains in Human Keratinocyte Migration

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