Accession Number : ADA346658


Title :   Cell-Matrix Interactions in Breast Carcinoma Invasion.


Descriptive Note : Annual rept. 15 Dec 96-14 Dec 97,


Corporate Author : NEW YORK UNIV MEDICAL CENTER NY


Personal Author(s) : Curatola, Anna M.


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a346658.pdf


Report Date : JAN 1998


Pagination or Media Count : 75


Abstract : The alpha 6 beta 4 integrin is a laminin 5 receptor expressed on the basal, basement membrane-apposed surface of ductal breast epithelial cells. In contrast to all other known integrins, alpha 6 beta 4 is concentrated in hemidesmosomes, adhesive junctions which connect the basement membrane to the intracellular keratin cytoskeleton. In virtually all cases of human breast cancer analyzed, alpha 6 beta 4 has been found to be diffusely distributed at the cell surface instead of being concentrated in hemidesmosomes. Our previous studies have indicated that alpha 6 beta 4 promotes the assembly of hemidesmosomes by interacting, via a specific region of the large unique cytoplasmic domain of the beta 4 subunit, with cytoskeletal elements of hemidesmosomes. We have observed that ligation of the EGF-R or EGF-R/Neu heterodimer promotes the association of the Src-family kinase Fyn with alpha 6 beta 4 and begun to map the sequences of Fyn and beta 4 required for the interaction. Ligation of the EGF-R or EGF-R/Neu heterodimer causes tyrosine phosphorylation of the beta 4 tail and disassembly of hemidesmosomes.


Descriptors :   *CELLS(BIOLOGY) , *BREAST CANCER , EPITHELIUM , MEMBRANES(BIOLOGY) , TISSUES(BIOLOGY) , ADHESION , NEOPLASMS , MUTATIONS , CYTOPLASM , MOLECULAR BIOLOGY , GENES , CARCINOGENS , VIRUSES , RECEPTOR SITES(PHYSIOLOGY) , MAMMARY GLANDS , TYROSINE , PHOSPHORYLATION.


Subject Categories : BIOCHEMISRTY
      GENETIC ENGINEERING AND MOLECULAR BIOLOGY
      MEDICINE AND MEDICAL RESEARCH


Distribution Statement : APPROVED FOR PUBLIC RELEASE