4.6 Article

Soluble fragment of P-cadherin adhesion protein found in human milk

Journal

JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 85, Issue 1, Pages 180-184

Publisher

WILEY
DOI: 10.1002/jcb.10126

Keywords

metalloproteinase; Listeria; epithelial cells; mammary gland; myoepithelial cells; protein in serum and urine

Funding

  1. NATIONAL CANCER INSTITUTE [R21CA087230] Funding Source: NIH RePORTER
  2. NCI NIH HHS [R21 CA87230, U01 CA6277] Funding Source: Medline

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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. (C) 2002 Wiley-Liss, Inc.

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