Snake venom metalloproteinases and disintegrins: interactions with cells

Kamiguti, Aura S.; Zuzel, Mirko; Theakston, R.D.G.

doi:10.1590/s0100-879x1998000700001

Cited by 103 publications

(69 citation statements)

References 74 publications

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“…Total RNA from Karpas 299 cells was extracted with Trizol reagent (Life Technologies, Karlsruhe, Germany), digested with RNase-free DNase I (Roche Diagnostics, Mannheim, Germany), and cDNA synthesis was performed using a SuperScript Preamplification System and oligo(dT) [12][13][14][15][16][17][18] primers (Life Technologies). For an amplification of the cDNA fragment encoding the catalytic, disintegrin, and cysteine-rich domain of TACE, total cDNA was subjected to 30 cycles of PCR using proofreading polymerase (Elongase Enzyme mix; Life Technologies).…”

Section: Cloning Of the Human Tace Ectodomain And Its Expression As Gmentioning

confidence: 99%

“…Due to their x-ray crystal structure, metalloproteinase-disintegrins are closely related to snake venom metalloproteinases (reprolysins) and are therefore regarded as members of the reprolysin family of metalloproteinases (13). Both snake venom proteinases and metalloproteinase-disintegrins exhibit membrane protein sheddase activity through their catalytic domain (11,12,14) and binding to cellular disintegrin receptors mediated by the disintegrin domain (15)(16)(17). Besides pro-TNF-␣, TACE cleaves the amyloid precursor protein (18) and mediates the shedding of L-selectin, the p75 TNFR, and TGF-␣ (16).…”

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confidence: 99%

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CD30 Shedding from Karpas 299 Lymphoma Cells Is Mediated by TNF-α-Converting Enzyme

Hansen¹,

Dietrich²,

Kisseleva³

et al. 2000

The Journal of Immunology

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CD30 is a costimulatory receptor on activated lymphocytes and a number of human lymphoma cells. Specific ligation of membrane-bound CD30 or cellular stimulation by PMA results in a metalloproteinase-mediated down-regulation of CD30 and release of its soluble ectodomain (sCD30). In this report, it is demonstrated that PMA-induced CD30 cleavage from Karpas 299 cells was mediated by a membrane-anchored metalloproteinase which was active on intact cells following 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate extraction of membrane preparations. Moreover, CD30 shedding was blocked by the synthetic hydroxamic acid-based metalloproteinase inhibitor BB-2116 (IC50, 230 nM) and the natural tissue inhibitor of metalloproteinases (TIMP)-3 (IC50, 30 nM), but not by the matrix metalloproteinase inhibitors TIMP-1 and TIMP-2. This inhibition profile is similar to that of the TNF-α- converting enzyme (TACE) and, indeed, mRNA transcripts of the membrane-bound metalloproteinase-disintegrin TACE could be detected in Karpas 299 cells. The ectodomain of TACE was expressed in bacteria as a GST fusion protein (GST-TACE) which cleaved CD30 from the surface of Karpas 299 cells and concomitantly increased the level of sCD30 in the cell supernatants. Hence, TACE does not only control the release of TNF-α, but also that of sCD30.

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Section: Cloning Of the Human Tace Ectodomain And Its Expression As Gmentioning

confidence: 99%

mentioning

confidence: 99%

CD30 Shedding from Karpas 299 Lymphoma Cells Is Mediated by TNF-α-Converting Enzyme

Hansen¹,

Dietrich²,

Kisseleva³

et al. 2000

The Journal of Immunology

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“…Vietnam, there were 68.810 new cases of cancer in 2000, increasing to 126.307 in 2010 and estimates that will be 189.000 in 2020 [3].…”

Section: Introductionmentioning

confidence: 99%

A Novel Anti-tumor Protein from Calloselasma Rhodostoma Venom in Vietnam

Trinh¹,

Thuc²

2016

Anat Physiol

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Aim: Vietnam is a tropical and agricultural country. Annually, there are 30,000 cases of snake bite. Two venomous snake families cause the big medical problem. In this, Calloselasma Rhodostoma (CR) is the most dangerous snake. Therefore, since 2001, the scientific research collaborations between Vietnam (VN) and University of Southern California (USC) were established. Since 2014 this project has been approved by VN government. The aims of the 1st project are to establish the technological process for purification of dsintegrin from CR venom of VN (CRd.VN), to determine the molecular weight, structure and its biological antitumor activities. Methods:The process of collection, lyophilisation of CR venom from VN. Protein concentration of CR venom was determined by BCA assay. High Performance Liquid Chromatography (HPLC), SDS-PAGE, Mass spectrometry (MS) analysis and sequencing by tryptic digestion were used for purification of CRd.VN and its molecular weight (MW) and structure. Standard cell biology methods were employed to characterize CRd's abilities (in vitro) to inhibit platelet aggregation, adhesion, migration and invasion of tumor cells. Its anti-cancer activity in a breast cancer (BC) murine model (in vivo) was tested.Results: Peak 7 of HPLC (CRd.VN), showed a single ~10 kDa band on SDS-PAGE gel. CRd.VN's MW, structure and the sequence are 7.33 kDa, a monomer containing 68 amino acids with an RGD motif (position 49-51) and 6 disulfide bonds. The anticancer activities of CRd.VN are very strong. Conclusion:We have shown that CRd.VN is a possible anti-tumor agent with clinical potential. However, further research is required on CRd recombinant production, preliminary pharmacokinetics/ toxicology properties and antitumor activities. The inhibition of angiogenesis is one of the most heavily explored treatment options for cancer, and snake venom disintegrins represent a library of molecules with different structures, potencies, and specificities and are good starting points for developing anti-angiogenesis therapeutics. Disintegrins first discovered in 1983 [11] and named in 1990 [12]. They are family of disulphide-rich, stable peptides, originally isolated from snake venom, also found in mammalian proteins (ADAMs). Disintegrins bind exclusively to activated integrins on cells, derived from multi-domain proteins by proteolytic processing, contain RGD (or alternate tri-peptide) motif at tip of a flexible 11-amino acid loop that is involved in integrin interaction. Range in size from small to medium to large and homo-and hetero-dimeric. Disintegrins hold a significant translational potential as anticancer agents based on their anti-angiogenic and anti-metastatic effects demonstrated in various experimental settings [13][14][15]. A Novel Anti-tumor Protein from Calloselasma Rhodostoma Venom in VietnamAlong with metalloproteases, disintegrins are important compounds in most Viperid and Crotalid venoms. Disintegrins represent a family of nontoxic and nonenzymatic low molecular weight (5-10 kDa) RGD-containing...

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“…These domains are involved in binding to integrins, the heterodimeric cell surface receptors involved not only in the interactions of cells with the surrounding matrix but also with neighboring cells (3). Most of the known ADAMs contain the integrin-binding amino acid sequence RGD (4) or instead ECD or DCD, which can compete with integrin-ligand interactions (4,5). ADAM-2 and ADAM-9 bind to -2 integrin through their disintegrin-like sequence ECD (6 -8), whereas ADAM-15 can interact with integrins on adjacent cells as observed with ␣␤3 and ␣5␤1 integrins on hematopoietic cells (9).…”

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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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Snake venom metalloproteinases and disintegrins: interactions with cells

Cited by 103 publications

References 74 publications

CD30 Shedding from Karpas 299 Lymphoma Cells Is Mediated by TNF-α-Converting Enzyme

CD30 Shedding from Karpas 299 Lymphoma Cells Is Mediated by TNF-α-Converting Enzyme

A Novel Anti-tumor Protein from Calloselasma Rhodostoma Venom in Vietnam

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

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