Phase I trial of a cisplatin‐albumin complex for the treatment of cancer of the head and neck.

Holding, J. D.; Lindup, W E; Laer, C. Van; Vreeburg, G. C. M.; Schilling, V.; Wilson, J. A.; Stell, P. M.

doi:10.1111/j.1365-2125.1992.tb04003.x

Cited by 50 publications

(32 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been postulated that cisplatin binding to proteins is the likely cause of many of the drugÕs side effects [6,7]. However, other reports suggest that Pt-serum albumin adducts may be important for the activity of the drug [8] because patients with low levels of serum albumin do not respond well to cisplatin-based chemotherapy [9]. In addition, Pt-ubiquitin adducts may suppress proteasome function inhibiting post-translational ubiquitination of proteins involved in the repair of DNA damage [10].…”

Section: Introductionmentioning

confidence: 98%

Water soluble cationic trans-platinum complexes which induce programmed cell death in the protozoan parasite Leishmania infantum

Nguewa

Fuertes

Iborra

et al. 2005

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 98%

Water soluble cationic trans-platinum complexes which induce programmed cell death in the protozoan parasite Leishmania infantum

Nguewa

Fuertes

Iborra

et al. 2005

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

“…The exact role of Pt-protein adducts in the mechanism of the action of the drug remains to be elucidated. It has been postulated that cisplatin binding to proteins is the likely cause of many of the drug's side effects [4,5]; however, other reports suggest that [Pt-human serum albumin] adducts may be important for the activity of the drug [6] since patients with low levels of human serum albumin do not respond well to cisplatin-based chemotherapy [7].…”

Section: Introductionmentioning

confidence: 99%

Ligand effects on the binding of cis- and trans-[PtCl2Am1Am2] to proteins

Najajreh

Peleg-Shulman

Moshel³

et al. 2003

J Biol Inorg Chem

View full text Add to dashboard Cite

As part of a systematic study of the basic principles that govern the formation and reactivity of Pt-protein adducts, we report the effect of substituting the amine ligand of cis- and trans-[PtCl(2)(NH(3))(2)] complexes with bulkier planar aromatic or nonplanar cyclic amine ligands on the binding properties of the complexes to ubiquitin and to horse heart myoglobin. The ligand replacement had a different effect on the cis or trans isomers investigated. In the cis-Pt complexes, replacing one or both amine ligands by piperidine or 4-picoline dramatically decreased the binding of the complexes to the proteins studied, whereas in the substituted trans-Pt complexes replacement of the amine by a piperidine or 4-picoline increased the binding rate. This behavior may have to do with the different preferred binding sites of the cis- and trans-Pt complexes. The bulkier cis- or trans-Pt complexes investigated also did not display a preference for Met1 of ubiquitin, possibly owing to steric constraints imposed by the substituted ligands. The introduction of a charged piperazine ligand significantly decreased the rate of binding to the protein, possibly owing to electrostatic interactions or hydrogen-bond formations with the surface of the protein. The binding of the complexes to ubiquitin and myoglobin does not disrupt the folding of the proteins as judged by electrospray ionization mass spectrometry.

show abstract

“…The hypothesis of HSA acting as a "drug reservoir" for the slow release of cisplatin has already been tested under clinical conditions [5][6][7] , though previous works had questioned this possibility 8 .…”

Section: Introductionmentioning

confidence: 99%

Effects of human serun albumin in some biological properties of rhodium(II) complexes

Espósito

Oliveira

Zyngier

et al. 2000

J. Braz. Chem. Soc.

View full text Add to dashboard Cite

were determined by spectrophotometry. In the case of the alkylcarboxylates, an inverse correlation of affinity with their liposolubilities was observed. Diffusion of the free or protein-bound complexes into Ehrlich cells in vitro seems to be primarily governed by the hydrophobic character of the complex. The complex [Rh 2 (tfc) 4 ] exhibited affinity towards the protein (K = 214.1) as well as cell partition both in the absence (32.1%) and presence (48.6%) of HSA. The compound HSA: [Rh 2 (tfc) 4 ] has had its antitumoral action in tumor-bearing Balb-c mice investigated, showing that HSA can be a drug reservoir for the rhodium complex.

show abstract

Phase I trial of a cisplatin‐albumin complex for the treatment of cancer of the head and neck.

Cited by 50 publications

References 21 publications

Water soluble cationic trans-platinum complexes which induce programmed cell death in the protozoan parasite Leishmania infantum

Water soluble cationic trans-platinum complexes which induce programmed cell death in the protozoan parasite Leishmania infantum

Ligand effects on the binding of cis- and trans-[PtCl2Am1Am2] to proteins

Effects of human serun albumin in some biological properties of rhodium(II) complexes

Contact Info

Product

Resources

About