Sequence and Biological Activity of Catrocollastatin-C: A Disintegrin-Like/Cysteine-Rich Two-Domain Protein fromCrotalus atroxVenom

Shimokawa, Ken‐ichi; Shannon, John D.; Jia, Li-Guo; Fox, Jay W.

doi:10.1006/abbi.1997.0133

Cited by 94 publications

(68 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Based on data in a number of studies, this may vary between different ECD-containing disintegrin proteins. Studies of two snake disintegrins, atrolysin A and catrocollastatin, suggest the cysteine in the ECD could be disulfide-bonded, since synthetic peptides with the cysteine constrained in a disulfide bond inhibit platelet aggregation (16,20), although catrocol- ZP-free eggs were incubated in medium containing 10 M (0.5 mg/ml) of the indicated BAP-presented disintegrin loop peptide or in no BAPpresented peptide (amino acid sequences indicated on the y axis) for 60 min. The eggs were then washed twice and fixed.…”

Section: Analysis Of the Fertilin ␤ Disintegrin Domainmentioning

confidence: 99%

“…2 The interactions of snake venom metalloproteases and ADAMs with their target cell surfaces appear to be more complicated than are those of the small disintegrins. In some cases, the peptide sequence aligning near the predicted disintegrin loop appears to mediate molecular interactions (6,16,19,20). However, in other instances, domains other than the disintegrin loop appear to be involved (7,(21)(22)(23).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Identification of Key Functional Amino Acids of the Mouse Fertilin β (ADAM2) Disintegrin Loop for Cell-Cell Adhesion during Fertilization

Zhu¹,

Bansal²,

Evans³

2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

Fertilin ␤ (also known as ADAM2) is a cell adhesion molecule on the surface of mammalian sperm that participates in sperm-egg membrane binding. Fertilin ␤ is a member of the molecular family known as ADAMs or MDCs. These proteins have a disintegrin domain with homology to integrin ligands found in snake venoms; several of these snake proteins have an RGD tripeptide presented on an extended "disintegrin loop." However, fertilin ␤ lacks an RGD tripeptide and instead has the consensus sequence X(D/E)ECD (QDECD in mouse fertilin ␤) in its putative disintegrin loop, and there is controversy over which amino acids comprise the active site of the fertilin ␤ disintegrin loop. We have used point-mutated versions of the sequence AQDECDVT and two bioassays to identify the key functional amino acids of this sequence from the mouse fertilin ␤ disintegrin domain. Amino acid substitutions for the terminal aspartic acid residue of the QDECD sequence result in dramatically reduced activities in the two assays for protein function, implicating the terminal aspartic acid residue as critical for protein function. Substitutions for the glutamic acid and the cysteine residues in the QD-ECD sequence result in slight reductions in activity, whereas substitution of the first aspartic acid has virtually no effect. These data suggest that the conserved ECD sequence of the mouse fertilin ␤ disintegrin loop, especially the terminal D residue, contributes more to the protein's activity than does the QDE sequence that aligns with the RGD tripeptide in other disintegrins.The interactions of gamete plasma membranes are mediated by multiple cell adhesion molecules on the surfaces of the sperm and egg. One of these cell adhesion molecules is the mammalian sperm protein fertilin ␤ (previously known as PH-30; also known as ADAM2). The involvement of fertilin ␤ in sperm-egg adhesion during fertilization is well established based on studies with synthetic peptides, antibodies, recombinant proteins, and the subfertile phenotype of male fertilin ␤ knock-out mice (summarized in Ref. 1). Of particular interest is the domain of fertilin ␤ that has homology to a family of integrin ligands originally identified in snake venoms. This domain of fertilin ␤, known as the disintegrin domain, has been implicated in the interactions of fertilin ␤ with the egg membrane in a variety of species (2-9).A large number of disintegrin domain-containing proteins have been identified. These include members of the molecular family known as ADAMs (for A disintegrin and A metalloprotease) or MDCs (for metalloprotease/disintegrin/cysteine-rich) (10, 11), of which fertilin ␤ is a member. Disintegrin domains are also present in a number of snake venom proteins, which are called simply disintegrins, reprolysins, or snake venom metalloproteases. These snake venom polypeptides range in size from small peptide chains of Ͻ50 amino acids to multidomain proteins of several hundred amino acids that are similar in domain structure to ADAM proteins, having a metalloprotease domain and a cy...

show abstract

Section: Analysis Of the Fertilin ␤ Disintegrin Domainmentioning

confidence: 99%

mentioning

confidence: 99%

Identification of Key Functional Amino Acids of the Mouse Fertilin β (ADAM2) Disintegrin Loop for Cell-Cell Adhesion during Fertilization

Zhu¹,

Bansal²,

Evans³

2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Há ainda diversos outros componentes ativos previamente identificados na peçonha de serpentes do gênero Crotalus, como desintegrinas (SHIMOKAWA et al, 1997(SHIMOKAWA et al, , 1998SÁNCHEZ et al, 2006), peptídeos potencializadores de bradicinina (HIGUCHI et al, 2006;GOMES et al, 2007); peptídeos natriuréticos (EVANGELISTA et al, 2008), metaloproteases CHEN & RAEL, 1997;KOMORI et al, 2011;WU et al, 2001), proteínas semelhantes à lectinas tipo-C (FRANCISCHETTI et al, 1997;TOYAMA et al, 2001;HAMAKO et al, 2007) e L-aminoácido oxidases (WELLNWE & MEISTER 1960;TORII et al, 1997;TOYAMA et al, 2006;VARGAS et al, 2012). Estes componentes, no entanto, são pouco estudados para as serpentes crotálicas sul-americanas por estarem presentes na peçonha em menores proporções em relação às toxinas predominantes.…”

Section: A Peçonha Ofídicaunclassified

Expressão e caracterização de uma protease de interesse biotecnológico clonada da glândula de peçonha de Crotalus durissus collilineatus

Boldrini-França¹

View full text Add to dashboard Cite

“…Proteínas nativas e recombinantes, compostas pelos domínios tipodisintegrina e rico em cisteínas de metaloproteinases hemorrágicas de venenos, são potentes inibidores da agregação plaquetária por bloquearem a ligação do colágeno tipo I à integrina  2  1 das plaquetas e ainda inibir a adesão de células da linhagem MG63 de osteosarcoma SHIMOKAWA et al, 1997;SOUZA et al, 2000).…”

Section: Domínios Não Catalíticos Das Metaloproteinasesunclassified

“…2003), e a bothropasina (ASSAKURA et al, 2003), do veneno da B. jararaca, e a catrocollastatina, do veneno de C. atrox (SHIMOKAWA et al, 1997). Tanto a jararhagina-C, como a catrocollastatina C, inibem a agregação plaquetária induzida pelo colágeno (USAMI et al, 1994;SHIMOKAWA et al, 1997).…”

Section: Domínios Não Catalíticos Das Metaloproteinasesunclassified

Estudo sobre a função dos domínios não catalíticos do HF3, uma metaloproteínase do veneno da serpente Bothrops jararaca, na sua interação com alvos celulares e plasmáticos.

Santos¹

View full text Add to dashboard Cite

show abstract

Sequence and Biological Activity of Catrocollastatin-C: A Disintegrin-Like/Cysteine-Rich Two-Domain Protein fromCrotalus atroxVenom

Cited by 94 publications

References 19 publications

Identification of Key Functional Amino Acids of the Mouse Fertilin β (ADAM2) Disintegrin Loop for Cell-Cell Adhesion during Fertilization

Identification of Key Functional Amino Acids of the Mouse Fertilin β (ADAM2) Disintegrin Loop for Cell-Cell Adhesion during Fertilization

Expressão e caracterização de uma protease de interesse biotecnológico clonada da glândula de peçonha de Crotalus durissus collilineatus

Estudo sobre a função dos domínios não catalíticos do HF3, uma metaloproteínase do veneno da serpente Bothrops jararaca, na sua interação com alvos celulares e plasmáticos.

Contact Info

Product

Resources

About