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  • 1
    ISSN: 1059-910X
    Keywords: Transport ; Proteins ; Ions ; Micropuncture ; Tight junctions ; Permeability ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: To understand the process of sperm maturation, an understanding of interactions between the spermatozoa with the luminal fluid microenvironment and with the epididymal epithelium is necessary. The composition of epididymal luminal fluid of several species is well documented but the manner by which the epididymis contributes to the formation of this specialized milieu is not so well understood. A major role played by the epididymis is to finely regulate the movement of molecules into and out of the lumen. This ensures that as spermatozoa progress along the duct they are exposed to a continually changing, but optimal environment necessary for their maturation and survival. This review focusses on our current understanding of the contributions of the epididymal epithelium to the formation of a specialized luminal fluid microenvironment. The role of the blood-epididymis barrier, the composition of the epididymal luminal fluid, the permeability properties of the epididymal epithelium, and recent studies on a number of luminal fluid proteins and expression of the genes which encode these proteins are discussed. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-2592
    Keywords: HER2 ; neu ; TNF-α ; monoclonal antibody therapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The HER2 protooncogene encodes a 185-kDa transmembrane protein (p185HER2) with extensive homology to the epidermal growth factor (EGF) receptor. Clinical and experimental evidence supports a role for overexpression of the HER2 protooncogene in the progression of human breast, ovarian, and non-small cell lung carcinoma. These data also support the hypothesis that p185HER2 present on the surface of overexpressing tumor cells may be a good target for receptor-targeted therapeutics. The anti-p185HER2 murine monoclonal antibody (muMAb) 4D5 is one of over 100 monoclonals that was derived following immunization of mice with cells overexpressing p185HER2. The monoclonal antibody is directed at the extracellular (ligand binding) domain of this receptor tyrosine kinase and presumably has its effect as a result of modulating receptor function.In vitro assays have shown that muMAb 4D5 can specifically inhibit the growth of tumor cells only when they overexpress the HER2 protooncogene. MuMAb 4D5 has also been shown to enhance the TNF-α sensitivity of breast tumor cells that overexpress this protooncogene. Relevant to its clinical application, muMAb 4D5 may enhance the sensitivity of p185HER2-overexpressing tumor cells to cisplatin, a chemotherapeutic drug often used in the treatment of ovarian cancer.In vivo assays with a nude mouse model have shown that the monoclonal antibody can localize at the tumor site and can inhibit the growth of human tumor xenografts which overexpress p185HER2. Modulation of p185HER2 activity by muMAb 4D5 can therefore reverse many of the properties associated with tumor progression mediated by this putative growth factor receptor. Together with the demonstrated activity of muMAb 4D5 in nude mouse models, these results support the clinical application of muMAb 4D5 for therapy of human cancers characterized by the overexpression of p185HER2.
    Type of Medium: Electronic Resource
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