0000000000672601

AUTHOR

L. Basiricò

A new form of tumor and fetal collagen that binds laminin.

Human breast and colon carcinoma tissues contain a form of collagen, not described before, composed of alpha 1 chains of similar size (approximately 100 kDa) but different charge. The three constitutive chains, separated by two-dimensional electrophoresis, are a unique acidic component, undetectable in other collagen types, with an apparent isoelectric point of 4-5, and two more basic components displaying the same electrophoretic behavior as alpha 1(III) and alpha 1(I), respectively. The acidic chain is structurally distinct from alpha 1(I) and displays a cyanogen bromide-derived fragment of similar size to CB5(III). This collagen in its native state is resistant to trypsin and metalloprot…

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Absence of regular alpha2(I) collagen chains in colon carcinoma biopsy fragments.

The extracellular matrix (ECM) is known to play an active role in numerous biological processes such as differentiation, apoptosis and cancer. Extensive alterations of epithelial basement membranes and of interstitial ECM are known to occur during the progression of most invasive carcinomas. Collagen, which represents the major component of the interstitial ECM, is primarily involved in the stromal changes at the site of tumor cell invasion. We have previously described the occurrence in breast and colon cancer ECM of an oncofetal form of collagen, characterized by an acidic chain distinct from those of type I and III collagen. In the present paper, we bring evidence that alpha2(I) collagen…

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Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences.

We have recently identified an oncofetal-laminin binding collagen (OF/LB) composed of three alpha chains, with the apparent molecular mass of about 100 kDa each, but bearing different pI. One of the chains appears markedly acidic in a bidimensional electrophoretic system, where the NEPHGE is used as first dimension separating gel, while the two more basic chains have similar migration as alpha 1(III) and alpha 1(I) collagen chains, respectively. Sequence analyses have been performed on CNBr-peptides, derived from pepsinized triple helical molecules and on tryptic fragments obtained after in gel digestion of the acidic band. The research of sequence homology with computerized databases indic…

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A contribution to breast cancer cell proteomics: detection of new sequences

Ductal infiltrating carcinoma (DIC) of the breast is the most common and potentially aggressive form of cancer. Knowledge of proteomic profiles, attained both in vivo and in vitro, is fundamental to acquire as much information as possible on the proteins expressed in these pathologic conditions. We used the breast cancer cell line 8701-BC, established from a primary DIC, with the aim of contributing to the databases on mammary cancer cells, which in turn will be very useful for the identification of differentially expressed proteins in normal and neoplastic cells. Within an analysis window comprising about 1750 discernible spots, we have at present catalogued 84 protein spots. The proteins …

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