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Distinct glycosylation of serum proteins in patients with cancer: brief communication.

Concanavalin A and wheat germ agglutinin, lectins that interact with serum glycoprotein in a manner similar to the antigen--antibody reaction, were used as "antibodies" in a single radial immunodiffusion technique to test a coded serum panel (from the National Cancer Institute, Bethesda, Md., and the Mayo Clinic, Rochester, Minn.) containing a) 99 serum samples from patients with different types of malignant neoplasms of the gastrointestinal tract, prostate gland, and lung, b) 50 samples from patients with benign diseases of the same organs as those affected in the cancer patients, and c) 50 samples from apparently healthy smokers. The resulting precipitation rings were not correlated to serum protein concentration, and the differences (demonstrated by Student's t-test and with a generalization of the one-sided two-sample Kolmogorov-Smirnov statistic for evaluating diagnostic tests) established that serum glycoproteins are glycosylated differently in cancer patients than in people without cancer.

Blood Proteins↗

Novel immunohistochemical localization of 28,000 molecular-weight (Mr) calcium binding protein (calbindin-D28k) in enterochromaffin cells of the human appendix and neuroendocrine tumors (carcinoids and small-cell carcinomas) of the midgut and foregut.

Calbindin-D28k is a highly conserved 28,000 (dalton) molecular-weight (Mr) calcium binding protein with broad tissue distribution, yet cell-type-specific expression predominantly in subpopulations of central and peripheral nervous system neurons, distal tubular cells of the kidney, and enteric neuroendocrine cells. A polyclonal antiserum against rat renal calbindin-D28k and a monoclonal antibody to calbindin-D28k purified from chicken intestine (clone CL-300) were used for immunohistochemical evaluation of formalin-fixed, paraffin-embedded tissues from multiple areas of the human small and large intestines and 93 primary neoplasms of the gastrointestinal tract (foregut, midgut, and hindgut derivatives) and the lung (foregut derivative). Calbindin-D28k immunostaining was obtained in a minority of enterochromaffin (neuroendocrine) cells, predominantly of the appendix and small intestine, as well as in autonomic neurons of the neural plexuses. Focal cytoplasmic Golgi-type staining was obtained with monoclonal antibody CL-300 in the appendiceal surface epithelium and dendritic macrophages confined to the appendiceal lymphoid follicles. Epithelial progenitor cells in enteric crypts and absorptive, goblet, and Paneth cells were calbindin-D28k negative, while no immunoreactivity was demonstrated in the mucosae of the colon and rectum. Calbindin-D28k staining was consistently detected in subpopulations of neuroendocrine phenotypes in midgut (appendiceal/ileal) and foregut (bronchial) carcinoids and small-cell carcinomas, but was absent in adenocarcinomas, squamous cell carcinomas, leiomyomas/leiomyosarcomas, schwannomas, and lymphomas. Our observations suggest that calbindin-D28k is a novel adjuvant neuroendocrine marker that is potentially useful in diagnostic tumor immunohistochemistry.

Adult↗