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Updated: Jun 2, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Expression and regulation of the 67-kda laminin-binding protein and its precursor gene in lymphoid-cells
1NCI,MOLEC ONCOL LAB,POB B,FREDERICK,MD 21702. NCI,PATHOL LAB,MOLEC PATHOL SECT,BETHESDA,MD 20892. MED UNIV S CAROLINA,CTR MOLEC & STRUCT BIOL,CHARLESTON,SC 29425. MED UNIV S CAROLINA,HOLLINGS CANC CTR,CHARLESTON,SC 29425. FREDERICK CANC RES & DEV CTR,PROGRAM RESOURCES INC DYNCORP,FREDERICK,MD 21702.
Abstract:
The 67-kDa laminin-binding protein is a non-integrin laminin-binding protein that mediates cancer cell adhesion and migration. The expression of the 67-kDa laminin-binding protein and of its putative precursor, a 37-kDa polypeptide, was studied in peripheral T-cells and T-lymphoma cell lines. Immunofluorescence experiments detected antigen in both the cytosol and on the cell membrane. On immunoblots of T-cell protein extracts, both the 37-kDa precursor and the mature 67-kDa protein were present. The mRNA for the precursor was expressed in both immature and mature thymocytes. In three independent T-lymphoma cell lines, the mRNA levels were decreased after prolonged stimulation with phorbol esters. Since the latter directly activate protein kinase C, it appears that regulation of the 37-kDa precursor in T-cells may be mediated by the signal transduction cascade associated with protein kinase C activation.
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