Literature DB >> 17377743

Proline prodrug of melphalan targeted to prolidase, a prodrug activating enzyme overexpressed in melanoma.

Sachin Mittal1, Xueqin Song, Balvinder S Vig, Gordon L Amidon.   

Abstract

PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.
MATERIALS AND METHODS: Hydrolysis, cell uptake, and cell proliferation studies of melphalan and the L: - and D: -proline prodrugs of melphalan, prophalan-L: and prophalan-D: , respectively, were conducted in the cancer cell lines using established procedures.
RESULTS: The bioactivation of prophalan-L: in the cancer cell lines exhibited high correlation with their prolidase expression levels (r (2) = 0.86). There were no significant differences in uptake of melphalan and its prodrugs. The cytotoxicity of prophalan-L: (GI(50)) in cancer cells also showed high correlation with prolidase expression (r (2) = 0.88), while prophalan-D: was ineffective at comparable concentrations. A prolidase targeting index (ratio of melphalan to prophalan-L: cytotoxicity normalized to their uptake) was computed and showed high correlation with prolidase expression (r (2) = 0.82).
CONCLUSIONS: The data corroborates the specificity of prophalan-L: activation by prolidase as well as prolidase-targeted cytotoxicity of prophalan-L: in cancer cell lines. Hence, prophalan-L: , a stable prodrug of melphalan, exhibits potential for efficiently targeting melanoma with reduced systemic toxicity.

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Year:  2007        PMID: 17377743     DOI: 10.1007/s11095-007-9249-9

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.580


  19 in total

1.  Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase.

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Review 3.  Drug-targeting strategies in cancer therapy.

Authors:  P S Huang; A Oliff
Journal:  Curr Opin Genet Dev       Date:  2001-02       Impact factor: 5.578

Review 4.  Current therapy for malignant melanoma.

Authors:  S S Legha
Journal:  Semin Oncol       Date:  1989-02       Impact factor: 4.929

5.  Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs.

Authors:  Sachin Mittal; Xueqin Song; Balvinder S Vig; Christopher P Landowski; Insook Kim; John M Hilfinger; Gordon L Amidon
Journal:  Mol Pharm       Date:  2005 Jan-Feb       Impact factor: 4.939

6.  Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2.

Authors:  R Humerickhouse; K Lohrbach; L Li; W F Bosron; M E Dolan
Journal:  Cancer Res       Date:  2000-03-01       Impact factor: 12.701

Review 7.  Systemic treatments for advanced cutaneous melanoma.

Authors:  C M Anderson; A C Buzaid; S S Legha
Journal:  Oncology (Williston Park)       Date:  1995-11       Impact factor: 2.990

8.  Utilization of peptide carrier system to improve intestinal absorption: targeting prolidase as a prodrug-converting enzyme.

Authors:  J P Bai; M Hu; P Subramanian; H I Mosberg; G L Amidon
Journal:  J Pharm Sci       Date:  1992-02       Impact factor: 3.534

9.  Human kidney prolidase--purification, preincubation properties and immunological reactivity.

Authors:  I Myara; C Cosson; N Moatti; A Lemonnier
Journal:  Int J Biochem       Date:  1994-02

Review 10.  Proline-dependent structural and biological properties of peptides and proteins.

Authors:  A Yaron; F Naider
Journal:  Crit Rev Biochem Mol Biol       Date:  1993       Impact factor: 8.250

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  3 in total

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Review 3.  Current Understanding of the Emerging Role of Prolidase in Cellular Metabolism.

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Journal:  Int J Mol Sci       Date:  2020-08-17       Impact factor: 5.923

  3 in total

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