Genetic polymorphism of high molecular weight urinary glycoproteins: A comparative study in normal individuals and breast cancer patients

Crocker, Glenn; Price, Michael R.

doi:10.1038/bjc.1987.132

Cited by 5 publications

(2 citation statements)

References 9 publications

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“…From analyses of individual urines, mo lecular weight polymorphisms have recently been described for immunologically related antigens of the epithelial membrane complex [22,23], which correspond to products of a hypervariable gene locus [23,24], As a con sequence, we cannot presently conclude that tumor-derived MA5 antigens are generally more highly sialylated than those of the MFGM. Our previous results [1], however, indicated that MA5 antigens of primary and metastatic breast tumors (total of 5 samples) possessed lower apparent molecular weights than MFGM-derived antigens.…”

Section: Discussionmentioning

confidence: 96%

Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Ishida¹,

Major²,

Ura³

et al. 1989

Tumor Biol

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Monoclonal antibody MA5 [ 1 ] recognizes an epitope present on the surface and in the cytoplasm of human breast cancer cells [2] and on the human milk fat globule membrane (MFGM). These immunoreactive determinants are found on tumor-associated glycoproteins with apparent molecular weights of 280 and 300 kdaltons, whereas the cross-related milk fat globule membrane antigen appears larger (330 kdaltons). Comparative electrophoretic migration analyses following neuraminidase digestion, as well as differential binding to various lectins, established that these molecules are extensively sialylated, and that the tumor antigens were sialylated to a greater extent than normal antigen. Immunoaffinity purification of this class of differentiation antigens from tumor and MFGM demonstrated similar size distributions, lectin affinities and buoyant densities as their respective crude antigens.

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Section: Discussionmentioning

confidence: 96%

Related Glycoproteins from Normal Secretory and Malignant Breast Cells

Ishida¹,

Major²,

Ura³

et al. 1989

Tumor Biol

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show abstract

“…The cDNA sequence of the protein core of the mammary mucin, MUCI, has been cloned and found to consist of unique amino and carboxyl sequences separated by a highly repetitive central portion containing 40-80 tandemly arranged copies of a 20 amino acid motif (APDTRPAPGSTAPPAHGVTS) (Marjolijn et al, 1990). As the number of repeats expressed by any individual is polymorphic, this region is referred to as VNTR (variable number tandem repeats), but there is no association between the number of repeats and susceptibility to malignancy (Crocker & Price, 1987). Mabs have been raised against naturally occurring mucin in human milk fat globule protein (HMFG) and against synthetic peptides representing portions of the repetitive region (Xing et al, 1989) and some of these antibodies have been found to be useful markers of progression of malignant disease and in imaging tumour deposits (Xing et al, 1989 (Xing et al, 1992 (Siddiqui et al, 1988) was subcloned into the bacterial expression vector pGEX-3X, in the correct reading frame and orientation (Smith & Johnson, 1988).…”

mentioning

confidence: 99%