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Retinoic acid‐binding protein in experimental and human colon tumors
Author(s) -
Sani Brahma P.,
Condon Stephen M.,
Brockman R. Wallace,
Weiland Louis H.,
Schutt Allan J.
Publication year - 1980
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(19800315)45:5+<1199::aid-cncr2820451326>3.0.co;2-d
Subject(s) - retinoic acid , binding protein , microbiology and biotechnology , rectum , colorectal cancer , ligand (biochemistry) , isoelectric point , medicine , pathology , biochemistry , cancer research , biology , cancer , receptor , enzyme , gene
Retinoic acid‐binding protein is present in metastatic murine colon tumors as well as in Lewis lung tumors and in lungs and brains of mice bearing these tumors; however, this protein is below the limits of detection in weakly‐metastatic carcinomas and in normal lung, colon, or brains. These observations are interesting since they concern the possibility of measuring the binding protein levels of colon tumors in clinical specimens as biochemical markers in human malignancy. A total of thirty‐three human colon tumors and related materials were analyzed for the presence of the binding protein. The interfering serum albumin, which nonspecifically binds retinoic acid, was eliminated by affinity chromatography. Of the twenty colon, cecum, and rectum tumors analyzed, 80% contained the binding protein in detectable amounts, and 20% showed nondetectable or marginally detectable amounts. Twenty‐two percent of the human colon segments isolated from patients suspected for colon tumors contained the binding protein in readily detectable amounts, whereas 78% revealed nondetectable to marginally detectable amounts. The retinoic acid‐binding protein of human colon tumor shared the same ligand specificity, thiol functions in ligand‐binding, and sedimentation coefficient as the binding protein isolated from chick embryo skin. However, the human protein exhibited altered isoelectric pH.