Calcium-binding proteins in human carcinoma cell lines.

Abstract

Elevated levels of Ca2+-binding proteins are reported in transformed cells and thought to be involved in their uncontrolled proliferation and often increased motility.Therefore, three cell-lines [LICR(Lond)-HN 1, -HN 2, and -HN 6] derived from human carcinomas displaying various degrees of locomotive activity were investigated for the presence of parvalbumin and related Ca2+-binding proteins. By applying different immunohistochemical methods in conjunction with a monospecific anti-parvalbumin antiserum, an intense staining was seen in cells displaying translocative motility. Often in these cells, an association with filamentous structures located in the nuclear region was observed. Unique Ca2 -binding proteins, absent from comparable normal tissue, were found in the malignant cell lines when analyzed by two-dimensional polyacrylamide gel electrophoresis and high-performance liquid chromatography. From these tumor cells a protein (Mr, 12,000; pI, 4.8) was isolated that crossreacted with antiparvalbumin antiserum. Peptide maps of this protein revealed a further structural homology to parvalbumin (Mr,12,000; pl, 4.9). In analogy to muscle, where there is evidence for a regulatory role of parvalbumin in the contraction-relaxation cycle, we speculate that this protein is tumor-associated and connected to the motile behavior of carcinoma cells.

Immunocytochemical detection of the onco‐developmental protein oncomodulin in pre‐neoplastic and neoplastic hepatocellular lesions during hepatocarcinogenesis in rats

“…A role for this protein in the regulation of cell motility has been suggested in epidermoid carcinoma cell lines (Pfyffer et a/., 1984;Heizmann and Berchtold, 1987) that exhibit invasive FIGURE 5 -Enlargement of an area in Figure 3a, showing inter-cell variations in intensity of intracytoplasmic immunozning. M o s t x n o t all, cells in the nodule stain homogeneously in the cytoplasm (arrows).…”

“…A role for this protein in the regulation of cell motility has been suggested in epidermoid carcinoma cell lines (Pfyffer et a/., 1984;Heizmann and Berchtold, 1987) that exhibit invasive Figure 4a, representative of the heterogeneous staining pattern for oncomodulin observed in hepatocellular carcinomas. The immunostaining is intracytoplasmic in all cells but may be homogeneously distributed or restricted to regions of the cytoplasm, then occasionally in contiguous regions of 2 adjacent cells.…”

Expression of the Ca2+-binding protein, parvalbumin, during embryonic development of the frog, Xenopus laevis

“…It can be inferred from parvalbumin's absence in oocytes, eggs, and early embryos that the protein plays no major role in oogenesis, egg fertilization, early cleavage, or gastrulation. Parvalbumin might have been expected to be expressed in the early embryo since a number of human and rodent carcinomas express parvalbumin-like Ca2+-binding proteins (30,31,38). It has been speculated that these proteins may be involved in cell replication (3) and motility (38).…”

“…Recently a set of Ca2+-binding proteins have been found to be developmentally regulated in sea urchin embryos. During sea urchin embryogenesis, the Spec proteins are synthesized de novo and accumulate in presumptive dorsal ectoderm cells (28,38). These proteins are related in primary sequence to the troponin C superfamily (7), which includes calmodulin, troponin C, myosin light chains, and parvalbumin.…”

Parvalbumin in Cat Brain: Isolation, Characterization, and Localization

“…The large shift in hydrophobicity that occurs when parvalbumins are separated by HPLC in the presence or absence of Ca2+ions is characteristic for Ca2+-binding proteins (Klee et al, 1981;Berchtold et al, 1983;Pfyffer et al, 1984). Like the rat parvalbumin ( Fig.…”