title: Soluble fragment of P-cadherin adhesion protein found in human milk.
abstract: Classical cadherins such as E- and P-cadherin are transmembrane proteins that mediate specific cell-to-cell adhesion and are important to tissue development and function. Cadherin function can be modulated by various means, including proteolytic cleavage of the extracellular adhesion domain from the cells' surface, yielding large soluble fragments termed (soluble) sE- or sP-cadherin. In people with certain carcinomas, sE-cadherin can be detected at elevated levels in the serum and sometimes can serve as a prognostic marker. Soluble E-cadherin also is found in urine of patients with bladder cancer. In addition to being present in bodily fluids of cancer patients, sE- and sP-cadherin are present in the serum of healthy people, suggesting that shedding of cadherins is a normal event. Here, we report high levels of 80 kDa sP-cadherin in human milk. In the lactating mammary gland tissue, P-cadherin appears to be a protein secreted by epithelial cells, rather than an adhesion protein. This is in contrast to the non-lactating mammary gland where P-cadherin is restricted to myoepithelial cells, and is present at sites of cell-cell contact.
authors.affiliation: The Lankenau Institute for Medical Research, 100 Lancaster Avenue, Wynnewood, Pennsylvania 19096, USA.
authors.forename: Alejandro Peralta
authors.initials: AP
authors.lastname: Soler
authors.forename: Jose
authors.initials: J
authors.lastname: Russo
authors.forename: Irma H
authors.initials: IH
authors.lastname: Russo
authors.forename: Karen A
authors.initials: KA
authors.lastname: Knudsen
mesh_terms: D001940:Breast / Q000378:metabolism; D015820:Cadherins / Q000032:analysis*; D004847:Epithelial Cells / Q000378:metabolism; D005260:Female; D006801:Humans; D007774:Lactation / Q000502:physiology; D008895:Milk, Human / Q000737:chemistry*; D010446:Peptide Fragments / Q000032:analysis; D012995:Solubility; D014018:Tissue Distribution
chemical_list: D015820:Cadherins; D010446:Peptide Fragments