pp32 overexpression induces nuclear pleomorphism in rat prostatic carcinoma cells.

Nuclear pleomorphism is an important diagnostic factor in tumour pathology. Traditionally, nuclear pleomorphism is evaluated qualitatively or semiquantitatively, often as a component of tumour grade; the molecular basis of nuclear pleomorphism, however, remains unclear. In this study, we investigated the quantitative effects on nuclear morphology of overexpressing pp32, a recently described nuclear phosphoprotein highly expressed in self-renewing and neoplastic cell populations.

Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci.

pp32 is a nuclear protein found highly expressed in normal tissues in those cells capable of self-renewal and in neoplastic cells. We report the cloning of cDNAs encoding human and murine pp32. The clones encode a 28.

Inhibition of fatty acid synthesis delays disease progression in a xenograft model of ovarian cancer.

One of the key limiting factors in the treatment of advanced stage human epithelial malignancies is the lack of selective molecular targets for antineoplastic therapy. A substantial subset of human ovarian, endometrial, breast, colorectal, and prostatic cancers exhibit increased endogenous fatty acid biosynthesis and overexpress certain enzymes in the pathway. Cell lines derived from these tumors use endogenously synthesized fatty acids for cellular functions, whereas normal cells and tissues appear to utilize dietary lipids preferentially.

Intermolecular homologies of human interferon-alpha.

Human interferon-alpha 2 (IFN) was analyzed by homology search computer program with the use of protein primary structures data bases. Results indicate that four domains with heightened ability to form homology pairs with different proteins exist in the IFN molecule. These domains occupy regions 35-56, 72-85, 97-110 and 124-136, mainly between the alpha-helical cylinders on the tertiary structure models.

[Determination of the amino acid composition of cartilage and creatine phosphokinase isoenzymes with the use of phenylthiocarbamyl amino acid derivatives].

A method for estimation of amino acid composition and collagen-specific amino acids was developed. The assay was based on the precolumn reaction of amino acids with phenylisothiocyanate. The phenylthiocarbamyl derivatives were analyzed by means of reverse-phase chromatography on octadecyl sorbents, which involved gradient elution with ethanol and sodium or ammonium acetate.