Anti-Laminin Receptor Antibody Targeting of Liposomes With Encapsulated Doxorubicin to Human Breast Cancer Cells In Vitro

Rahman, Aquilur; Panneerselvam, M.; Guirguis, Raouf; Castronovo, Vincenzo; Sobel, Mark E.; Abraham, Katalin G.; Daddona, Peter E.; Liotta, Lance A.

doi:10.1093/jnci/81.23.1794

Cited by 17 publications

(4 citation statements)

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“…Immunofluorescence studies with antipeptide G antibodies confirmed that peptide G was expressed on the cancer cell surface (CASTRONOVO et al 1991 b). In addition, a monoclonal antibody to a 37LRP-derived sequence overlapping the peptide G region competed with laminin for binding to living human metastatic breast cancer cells in vitro (RAHMAN et al 1989). These data confirmed the hypothesis that the 37LRP contained a membrane-associated domain and a cellsurface laminin-binding region, characteristics that one would expect of the 67LR.…”

Section: Membrane-associatedand Laminin-binding Domains In the 37lrpsupporting

confidence: 70%

The 67-kDa Laminin Receptor and Tumor Progression

Montuori

Sobel²

1996

Attempts to Understand Metastasis Formation I

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Section: Membrane-associatedand Laminin-binding Domains In the 37lrpsupporting

confidence: 70%

The 67-kDa Laminin Receptor and Tumor Progression

Montuori

Sobel²

1996

Attempts to Understand Metastasis Formation I

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“…Human a-thrombin, polyclonal antibodies to glycocalicin (Harmon & Jamieson, 1986) and GPIV (Tandon et al, 1989a) and polyclonal antibody to the laminin receptor of pooled human breast carcinoma tissue (Wewer et al, 1986) had been previously produced in our laboratories. Monoclonal IgM antibodies 3D1 and 6G4 to synthetic peptide (Leu-33-.His) of the 67 kDa laminin receptor had been prepared as described (Rahman et al, 1989). Fab fragments were prepared using immobilized papain and Protein A according to the protocol of the manufacturer (Pierce Chemical Co., Rockford, IL, U.S.A.).…”

Section: Methodsmentioning

confidence: 99%

Interaction of human platelets with laminin and identification of the 67 kDa laminin receptor on platelets

Tandon

Holland

Kralisz

et al. 1991

Biochemical Journal

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A microtitre adhesion assay has been developed to define parameters affecting the adherence of washed platelets to laminin. Adherence was optimally supported by Mg2+ and was inhibited by Ca2+ and by anti-laminin Fab fragments, but significant adhesion (75-90% of control) was found both in heparinized plasma containing physiological levels of bivalent cations and in plasma anti-coagulated with EGTA. Adherence was unaffected by platelet activation with ADP but was decreased by 50% by treatment with alpha-thrombin (1 unit/ml, 5 min). Adherence was unaffected by monospecific polyclonal antibodies to glycoprotein (GP) Ib and GPIV, and was normal with platelets from two patients with Glanzmann's thrombasthaenia, indicating that GPIb, the GPIIb/IIIa complex and GPIV are not involved in platelet-laminin interaction. Affinity chromatography of Triton-solubilized membranes on laminin-Sepharose followed by elution with 0.2 M-glycine/HCl (pH 2.85) identified a major band with a molecular mass of 67 kDa in the reduced and of 53 kDa in the unreduced form. This protein gave a positive reaction on Western blotting with a monospecific polyclonal antibody raised against the high-affinity laminin receptor isolated from human breast carcinoma tissue. The adhesion of platelets to laminin was inhibited by two monoclonal IgM antibodies specific to the LR-1 domain of the 67 kDa receptor. The binding protein was surface-oriented, as shown by flow cytofluorimetry and by the fact that it could be iodinated in intact platelets, but it was not labelled by the periodate-borotritide procedure, suggesting that it did not contain terminal sialic acid. The laminin-derived peptides Tyr-Ile-Gly-Ser-Arg and Cys-Asp-Pro-Gly-Tyr-Ile-Gly-Ser-Arg-NH2, which constitute a complementary binding domain in laminin for the 67 kDa receptor, themselves supported platelet adhesion, bound to the receptor and inhibited the adhesion of platelets to laminin. In addition, Fab fragments of anti-Tyr-Ile-Gly-Ser-Arg antibody inhibited platelet adhesion to laminin. These results demonstrate that the high-affinity 67 kDa laminin receptor previously identified in a range of normal and transformed cells and its complementary Tyr-Ile-Gly-Ser-Arg binding domain play an important role in the interaction of platelets with laminin.

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“…Wewer et al first indicated that anti-67LR/37LBP antisera raised against a 20-mer peptide partial sequence blocked the surface interaction of melanoma cells with endogenous laminin, resulting in the inhibition of laminin-mediated cell attachment and migration. 12) Rahman et al 27) have reported that anti-67LR/ 37LBP antibody-coupled liposomes encapsulating an anticancer drug selectively killed breast cancer cells. Iwamoto et al 28) demonstrated that synthetic YIGSR peptide, derived from the sequence of the laminin B1 chain and reported to be a binding site for 67LR/37LBP, 29) inhibited experimental metastasis of B16 melanoma.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Experimental Metastasis of Human Fibrosarcoma Cells by Anti‐recombinant 37‐kDa Laminin Binding Protein Antibody

Narumi

Inoue

Tanaka

et al. 1999

Japanese Journal of Cancer Research

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The laminin binding protein of 37 kDa (37LBP) is regarded as a precursor protein of the high-affinity 67-kDa laminin receptor (67LR). Expression of 67LR/37LBP is well correlated with biological aggressiveness of cancer, particularly with invasive and metastatic potential. To investigate in detail the role of 37LBP in cancer cells, we synthesized recombinant 37LBP (r37LBP) as a fusion protein and generated an IgG-type polyclonal antibody P4G against r37LBP. Western blot analysis with P4G showed a single band of 67LR under both nonreducing and reducing conditions using cell extract of human fibrosarcoma cells HT1080. It was shown that P4G inhibited cell attachment to immobilized laminin in a dose-dependent manner. Further, the intravenous injection of HT1080 cells pretreated with P4G, compared with that of cells pretreated with normal rabbit serum, resulted in a reduced number of experimental metastases (3.3 ± ± ± ±5.1 vs. 58.0 ± ± ± ±38.0 nodules per mouse, respectively) (P< < < <0.005). These results suggest that P4G inhibits the colonization and growth of HT1080 cells in the lungs of mice, and that the blocking of r37LBP with the specific antibody P4G may offer a potential strategy for preventing cancer metastasis. Key words: Laminin receptor -Fusion protein -Antibody -Cell attachment -Cancer metastasisLaminin, a high-molecular-weight glycoprotein (Mr= 850,000-1,000,000), is regarded as one of the main components of the basement membrane structure. Since laminin plays an important role in the control of cell functions through the various binding sites of extracellular matrix components (proteoglycans, heparin, and collagen), an interaction between laminin and laminin receptor/binding protein on the cell surface is crucial for cancer-related processes such as proliferation, migration, adhesion, phagocytosis, and metastasis. 1, 2)The 37-kDa laminin binding protein (37LBP) has been described as a precursor protein of the non-integrin 67-kDa laminin receptor (67LR). [3][4][5] Previous reports have demonstrated the up-regulated expression of 37LBP in various human cancer cells and tissues such as colon , 5) breast, 6) ovary, 7) and lung. 8) In these cancers, a direct positive correlation was demonstrated between the expression of 37LBP in the primary tumor and the metastatic potential of the lesion. 9-11) These findings suggest that increased expression of the 37LBP gene participates in the acquisition of the metastatic phenotype.In the present study, we report a polyclonal antibody that was generated against recombinant 37LBP (r37LBP). The resultant antibody P4G immunoreacted with 67LR and inhibited cell adhesion of H1080, a cell line of human fibrosarcoma, to immobilized laminin in a dose-dependent manner. In addition, pulmonary metastases of HT1080 cells in Balb/c nu/nu mice were dramatically inhibited by pretreatment of the cells with P4G. These results demonstrate that 37LBP is the functional domain of 67LR and suggest that the blocking of 37LBP with a specific antibody may constitute a potential future thera...

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Anti-Laminin Receptor Antibody Targeting of Liposomes With Encapsulated Doxorubicin to Human Breast Cancer Cells In Vitro

Cited by 17 publications

References 0 publications

The 67-kDa Laminin Receptor and Tumor Progression

The 67-kDa Laminin Receptor and Tumor Progression

Interaction of human platelets with laminin and identification of the 67 kDa laminin receptor on platelets

Inhibition of Experimental Metastasis of Human Fibrosarcoma Cells by Anti‐recombinant 37‐kDa Laminin Binding Protein Antibody

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