Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities.
Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities.
复制标题
具有黑色素瘤粘附和肝素结合活性的纤连蛋白肽的定位和化学合成。
DOI:
10.1021/bi00404a044
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发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Furcht,LT
中科院分区:
文献类型:
--
作者:
McCarthy,JB;Chelberg,MK;Mickelson,DJ;Furcht,LT
Department of Laboratory Medicine and Pathology, The University of Minnesota, Minneapolis, Minnesota 55455 Received May 27, 1987; Revised Manuscript Received September 23, 1987 abstract: Tumor cell adhesion to the extracellular matrix is an important consideration in tumor metastasis. Recent results show that multiple adhesion-promoting domains for melanoma cells can be purified from proteolytic digests of fibronectin [McCarthy, J. B., Hagen, S. T., & Furcht, L. T.(1986) J. Cell Biol. 102, 179-188]. Monoclonal antibodies were generated against a tryptic/catheptic 33K heparin binding fragment of fibronectin derived from the carboxyl terminal of the A chain. This region contains a tumor cell adhesion-promoting domain (s). The amino-terminal sequence was determined for this fragment, as well as a tryptic 3 IK fragment which is located to the carboxyl-terminal side of the 33K heparin binding fragment in A chains of fibronectin. The partial sequence data demonstrate that arginyl-glycyl-aspartyl-serine (RGDS) or the related arginyl-glutamyl-aspartyl-valine (REDV) is not present in the 33K heparin binding fragment, confirming earlier results which demonstrated that cells adhere to this fragment by an RGDS-independent mechanism. Two monoclonal antibodies, termed AHB-1 and AHB-2, recognized epitopes common to heparin binding fragments derived from the carboxyl terminus of both the A and B chains of fibronectin. Monoclonal antibody AHB-2 inhibited melanomaadhesion to the 33K heparin binding fragment of fibronectin in a concentration-dependent manner, whereas monoclonal antibody AHB-1 had no effect on adhesion to this fragment. Neither monoclonal antibody inhibited adhesion to intact fibronectin. However, monoclonal AHB-2 potentiated the inhibitory effect of suboptimal levels of exogenous RGDS on cell adhesion to intact fibronectin. AHB-2 recognized an epitope common to both the A-and B-chain carboxyl-terminal heparin binding region of fibronectin. Thus, synthetic peptides of this region were prepared in order to further localize the cell adhesion-promotingactivity of this portion of the molecule. Two peptides were identified which promoted melanoma cell adhesion in a concentration-dependent manner. These peptides also bound [3H] heparin in a solid phase binding assay. The studies support the concept that melanoma adhesion to intact fibronectin occurs as a result of multiple distinct adhesion-promoting domains, which interact with multiple, functionally discrete receptors on the surface of melanoma cells. e invasion and metastasis of tumor cells is a complex process which involves numerous tumor-and host-related factors. One important approach for understanding the biology of metastasizing tumor cells is to develop tools which can be used to study the molecular basis of cell adhesionto components of the extracellular matrix. Work from several labo-ratories has shown that adhesion to the extracellular matrix is an integral part of the metastatic process. For example, coinjection of metastatic tumorcells with antibodies against laminin has been shown to inhibit the formation of pulmonary metastatic nodules (Terranova et al., 1982). More recently, isolated tumor cell adhesion-promoting fragments of laminin (Barsky et al., 1984) or synthetic adhesion-disrupting peptides from fibronectin (Furcht et al., 1985; Humphries et al., 1986) have been shown to inhibit the metastatic behavior of tumor cells when these cells were incubated ex vivo in the presence of these reagents prior to injection into mice. These and many other results suggest a role for tumor cell adhesion to molecules in plasma, basement membranes, or extracellular …
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DOI:
--
发表时间:
1986
期刊:
Journal of immunology (Baltimore, Md. : 1950)
影响因子:
--
作者:
Gerberick,GF;Jaffe,HA;Willoughby,JB;Willoughby,WF
通讯作者:
Willoughby,WF
DOI:
10.1164/arrd.1987.135.6.1300
发表时间:
2015-05
期刊:
The American review of respiratory disease
影响因子:
--
作者:
J. Brieland;R. Kunkel;J. Fantone
通讯作者:
J. Brieland;R. Kunkel;J. Fantone
影响因子:
4.4
作者:
M. Cohen;J. Ryan;R. Root
通讯作者:
R. Root
DOI:
--
发表时间:
1985
期刊:
Journal of immunology (Baltimore, Md. : 1950)
影响因子:
--
作者:
Myers,MA;McPhail,LC;Snyderman,R
通讯作者:
Snyderman,R
DOI:
--
发表时间:
1983
期刊:
The American journal of pathology
影响因子:
--
作者:
Ward,PA;Duque,RE;Sulavik,MC;Johnson,KJ
通讯作者:
Johnson,KJ