ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3

Loechel, Frosty; Fox, Jay W.; Murphy, Gillian; Albrechtsen, Reidar; Wewer, Ulla M.

doi:10.1006/bbrc.2000.3835

Cited by 293 publications

(213 citation statements)

References 30 publications

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“…ADAM-12 has been demonstrated to cleave insulin-like growth factor binding proteins 3 and 5, pro-heparin-binding epidermal growth factor, and the ECM components gelatin, type IV collagen, and fibronectin (43)(44)(45)(46), and may therefore be significant in painful tendinopathy, both as a regulator of cytokine activity and as a mediator of ECM degradation. ADAM-12 is also reported to support cell attachment and influence cell spreading and migration (47)(48)(49).…”

Section: Discussionmentioning

confidence: 99%

“…Since fibrocartilagenous transformation and endochondral ossification Compared with the normal tendon group, the levels of TIMP-3 mRNA were lower in the painful tendon group. TIMP-3 is believed to be the primary endogenous inhibitor of the aggrecanase ADAMTS proteinases (23,55) and the ADAM-12 and -17 proteinases (21,22,43), and a decrease in TIMP-3 might therefore be predicted to influence the activity of these proteinases. TIMP-3 has also been demonstrated to possess an antiangiogenic activity (56,57), and a lower TIMP-3 expression in pathologic tissue may correlate with the increased incidence of vascular invasion that has been reported in chronic pathologic conditions in the tendon (1,58).…”

Section: Discussionmentioning

confidence: 99%

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Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

Jones¹,

Corps²,

Pennington³

et al. 2006

Arthritis & Rheumatism

259

284

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Objective. To profile the messenger RNA (mRNA) expression for the 23 known genes of matrix metalloproteinases (MMPs), 19 genes of ADAMTS, 4 genes of tissue inhibitors of metalloproteinases (TIMPs), and ADAM genes 8, 10, 12, and 17 in normal, painful, and ruptured Achilles tendons.Methods. Tendon samples were obtained from cadavers or from patients undergoing surgical procedures to treat chronic painful tendinopathy or ruptured tendon. Total RNA was extracted and mRNA expression was analyzed by quantitative real-time reverse transcription-polymerase chain reaction, normalized to 18S ribosomal RNA.Results. In comparing expression of all genes, the normal, painful, and ruptured Achilles tendon groups each had a distinct mRNA expression signature. Three mRNA were not detected and 14 showed no significant difference in expression levels between the groups. Statistically significant (P < 0.05) differences in mRNA expression, when adjusted for age, included lower levels of MMPs 3 and 10 and TIMP-3 and higher levels of ADAM-12 and MMP-23 in painful compared with normal tendons, and lower levels of MMPs 3 and 7 and TIMPs 2, 3, and 4 and higher levels of ADAMs 8 and 12, MMPs 1, 9, 19, and 25, and TIMP-1 in ruptured compared with normal tendons.Conclusion. The distinct mRNA profile of each tendon group suggests differences in extracellular proteolytic activity, which would affect the production and remodeling of the tendon extracellular matrix. Some proteolytic activities are implicated in the maintenance of normal tendon, while chronically painful tendons and ruptured tendons are shown to be distinct groups. These data will provide a foundation for further study of the role and activity of many of these enzymes that underlie the pathologic processes in the tendon.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

Jones¹,

Corps²,

Pennington³

et al. 2006

Arthritis & Rheumatism

259

284

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“…Several ADAMs are expressed by adult and developing skeletal muscles, including ADAM1, 4, 9, and 15 that are ubiquitous, and ADAM12, also called meltrin-␣, whose expression is less widespread (Yagami-Hiromasa et al, 1995;Loechel et al, 2000;Kratzschmar et al, 1996;Weskamp et al, 1996;Kurisaki et al, 1998). In rodents, constitutive muscle expression of ADAM12 starts at the embryonic stage when myotubes are formed (Kurisaki et al, 1998), persists at the neonatal stage (Yagami-Hiromasa et al, 1995;Borneman et al, 2000;Kronqvist et al, 2002), and ceases in adulthood (Borneman et al, 2000;Kronqvist et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, some ADAMs contain a hydrophobic sequence in a cysteine-rich region that may represent a fusion peptide, suggesting that this subclass of ADAMs might participate to plasma membrane merging (Huovila et al, 1996). Some ADAMs have been implicated in most mammalian cell fusion processes, including ADAM1, 2, and 3 in fertilization (Blobel et al, 1992;Huovila et al, 1996;Wolfsberg and White, 1996;Hooft, 1998) and ADAM12 in osteoclast (Abe et al, 1999;Choi et al, 2001) and macrophage-derived multinucleated giant cell formation (Abe et al, 1999), in trophoblast syncytialization (Huovila et al, 1996;Gilpin et al, 1998;Shi et al, 2000), and in myogenesis (Yagami-Hiromasa et al, 1995).Several ADAMs are expressed by adult and developing skeletal muscles, including ADAM1, 4, 9, and 15 that are ubiquitous, and ADAM12, also called meltrin-␣, whose expression is less widespread (Yagami-Hiromasa et al, 1995;Loechel et al, 2000;Kratzschmar et al, 1996;Weskamp et al, 1996;Kurisaki et al, 1998). In rodents, constitutive muscle expression of ADAM12 starts at the embryonic stage when myotubes are formed (Kurisaki et al, 1998), persists at the neonatal stage (Yagami-Hiromasa et al, 1995;Borneman et al, 2000;Kronqvist et al, 2002), and ceases in adulthood (Borneman et al, 2000;Kronqvist et al, 2002).…”

mentioning

confidence: 99%

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Lafuste

Sonnet

Chazaud

et al. 2005

MBoC

Self Cite

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Knowledge on molecular systems involved in myogenic precursor cell (mpc) fusion into myotubes is fragmentary. Previous studies have implicated the a disintegrin and metalloproteinase (ADAM) family in most mammalian cell fusion processes. ADAM12 is likely involved in fusion of murine mpc and human rhabdomyosarcoma cells, but it requires yet unknown molecular partners to launch myogenic cell fusion. ADAM12 was shown able to mediate cell-to-cell attachment through binding ␣ 9 ␤ 1 integrin. We report that normal human mpc express both ADAM12 and ␣ 9 ␤ 1 integrin during their differentiation. Expression of ␣ 9 parallels that of ADAM12 and culminates at time of fusion. ␣ 9 and ADAM12 coimmunoprecipitate and participate to mpc adhesion. Inhibition of ADAM12/␣ 9 ␤ 1 integrin interplay, by either ADAM12 antisense oligonucleotides or blocking antibody to ␣ 9 ␤ 1 , inhibited overall mpc fusion by 47-48%, with combination of both strategies increasing inhibition up to 62%. By contrast with blockade of vascular cell adhesion molecule-1/␣ 4 ␤ 1 , which also reduced fusion, exposure to ADAM12 antisense oligonucleotides or anti-␣ 9 ␤ 1 antibody did not induce detachment of mpc from extracellular matrix, suggesting specific involvement of ADAM12-␣ 9 ␤ 1 interaction in the fusion process. Evaluation of the fusion rate with regard to the size of myotubes showed that both ADAM12 antisense oligonucleotides and ␣ 9 ␤ 1 blockade inhibited more importantly formation of large (>5 nuclei) myotubes than that of small (2-4 nuclei) myotubes. We conclude that both ADAM12 and ␣ 9 ␤ 1 integrin are expressed during postnatal human myogenic differentiation and that their interaction is mainly operative in nascent myotube growth. INTRODUCTIONAdult skeletal muscle regeneration after injury results from activation, proliferation, and fusion of mononucleated myogenic precursor cells (mpc) (Hawke and Garry, 2001). The mpc fusion results from an ordered sequence of events, including clustering and alignment of cells, establishment of close cell-to-cell contacts, and plasma membrane merging (Doberstein et al., 1997;Taylor, 2003). Various membrane proteins have been implicated in myotube formation, including N-and M-cadherins, neural cell adhesion molecule (NCAM), and vascular cell adhesion molecule (VCAM), ␣ 4 ␤ 1 and other integrins, and a disintegrin and metalloproteinases (ADAMs) (Abmayr et al., 2003). ADAMs form a family of Ͼ30 transmembrane glycoproteins with a unique domain organization, including a prodomain, a proteolytic domain (metalloprotease), an adhesion integrin-binding site formed by both disintegrin and cysteine-rich domains, an epidermal growth factor-like domain, a transmembrane domain, and a signaling cytoplasmic tail (Huovila et al., 1996;Primakoff and Myles, 2002;White, 2003). In addition, some ADAMs contain a hydrophobic sequence in a cysteine-rich region that may represent a fusion peptide, suggesting that this subclass of ADAMs might participate to plasma membrane merging (Huovila et al., 1996). Some ADAMs have been implicated i...

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“…ADAM-12 is shown to be involved in cell-cell and cell-matrix interactions, leading to myogenesis (2) and adipogenesis (3), and to promote EGF receptor signaling by shedding of the heparin-binding EGF (HB-EGF) from the membrane-anchored inactive precursor pro-HG-EGF form (4) and release of insulin-like growth factor binding proteins 3 and 5 (IGFBP-3 and IGFBP-5; refs. 5,6). Although biological significance of ADAM-12 is yet to be fully understood, an increase in the level of ADAM-12 is detected during several pathologies (7).…”

mentioning

confidence: 99%

Transforming Growth Factor-β1–Mediated Activation of NF-κB Contributes to Enhanced ADAM-12 Expression in Mammary Carcinoma Cells

Ray

Dhar²,

Ray³

2010

Molecular Cancer Research

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A disintegrin and metalloproteinase-12 (ADAM-12), a member of multifunctional family of proteins, is upregulated in many cancers, including breast, lung, liver, prostate, gastric, and bladder. The multidomain structure, composed of a prodomain, a metalloproteinase, disintegrin-like, epidermal growth factor-like, cysteinerich and transmembrane domains, and a cytoplasmic tail, allows ADAM-12 to promote matrix degradation, cell-cell adhesion, and intracellular signaling capacities and thereby to play a critical role in cancer growth and metastasis. Despite ample evidence linking increased ADAM-12 expression with cancer, the mechanisms controlling its upregulation are still unknown. In the present study, transforming growth factor-β1 (TGF-β1) is shown to increase ADAM-12 mRNA expression in MDA-MB-231 breast carcinoma cells. We have identified a promoter element responsible for TGF-β1-mediated ADAM-12 induction. We show interaction of NF-κB with ADAM-12 promoter and that high level of NF-κB activity in breast carcinoma cells results in the upregulation of ADAM-12 expression. Site-directed mutagenesis of the NF-κB element in ADAM-12 promoter and inhibition of NF-κB activity by Bay-11-7085 and MG-132 significantly reduced TGF-β1-mediated increase of ADAM-12 promoter-driven gene expression. Transfection of cells with a dominant-negative mutant form of IκBα (IκBαΔN), which inhibits activation of NF-κB, significantly reduced transcription from ADAM-12 promoter-reporter in TGF-β1-stimulated MDA-MB-231 cancer cells. In correlation, overexpression of NF-κB induced ADAM-12 expression in a dose-dependent manner. DNA-binding and ChIP assays indicated that p65 subunit of NF-κB binds to ADAM-12 promoter. Together, our study identified a cellular mechanism for induction of ADAM-12, which involves NF-κB and its activation by TGF-β1.

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ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3

Cited by 293 publications

References 30 publications

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Transforming Growth Factor-β1–Mediated Activation of NF-κB Contributes to Enhanced ADAM-12 Expression in Mammary Carcinoma Cells

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ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3

Cited by 293 publications

References 30 publications

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

Transforming Growth Factor-β1–Mediated Activation of NF-κB Contributes to Enhanced ADAM-12 Expression in Mammary Carcinoma Cells

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation