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Cancer-associated SCM-recognition, immunedefense suppression, and serine protease protection peptide. Part I. Isolation, amino acid sequence, homology, and origin

Cercek, L.; Cercek, B.

Cancer Detection and Prevention 16(5-6): 305-319

1992

ISSN/ISBN: 0361-090X
PMID: 1473120
Document Number: 400096
The isolation of a cancer-associated, SCM-recognition, immunedefense-suppressing, and serine protease-protecting (CRISPP) peptide from the blood plasma of cancer patients is described. The amino acid sequences were determined on preparations from 12 different cancers. The peptide is composed in 9 cancer of 29 and in 3 cancers of 35 amino acid residues with molecular weight of 3410 and 4007 Da, respectively. A consensus, synthetic 29 amino acid CRISPP peptide (CRISPP-S) has the same cancer SCM-recognition (CR) activity and SCM-response modifying effects as the natural peptide. The "cancer SCM-recognition epitope" of the CRISPP peptide was determined. Anti-CRISPP-S antibodies were raised and used in immunoassays to confirm the presence of the CRISPP peptides in cancer blood plasmas, in supernatants of cancer cell growth media and in cultured human cancer cells. The amino terminal end sequences of peptides isolated from growth media of cultured breast and colon cancer cells corresponded to amino acid sequences of CRISPP peptides isolated from cancer blood plasmas of subjects with the respective cancers. The CRISPP peptides are between 83 to 100% homologous to the alpha-1-protease inhibitor amino acid sequence located at the carboxy terminal end between residues 358 and 393. The genetic origin of the CRISPP peptides and their selective advantage to cancer cell survival are discussed.

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