In:
Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 54, No. 9 ( 2006-09), p. 1015-1020
Abstract:
Biological effects of substance P (SP) are mediated by the neurokinin-1 (NK 1 ) receptor that exists as a full-length and as a carboxy-terminally truncated isoform in humans. Although NK 1 receptor mRNA and binding sites have been detected in certain malignancies, little is known about the cellular and subcellular localization of NK 1 receptor protein in human neoplastic tissues. We developed and characterized a novel anti-peptide antibody to the carboxy-terminal region of the human full-length NK 1 receptor. Specificity of the anti-serum was demonstrated by (1) detection of a broad band migrating at molecular mass 70,000-90,000 Da in Western blots of membranes from NK 1 -expressing tissues; (2) cell-surface staining of NK 1 -transfected cells; (3) translocation of NK 1 receptor immunostaining after SP exposure; and (4) abolition of tissue immunostaining by preadsorption of the antibody with its immunizing peptide. Distribution of NK 1 receptors was investigated in 72 formalin-fixed, paraffin-embedded human tumors showing that NK 1 receptors were frequently expressed in glioblastomas and breast and pancreatic carcinomas. Immunoreactive NK 1 receptors were clearly confined to the plasma membrane and uniformly present on nearly all tumor cells. Development of this novel NK 1 receptor antibody allows the efficient localization of NK 1 receptor protein in human formalin-fixed, paraffin-embedded tissues. NK 1 receptor visualization with this simple and rapid immunohistochemical method will facilitate identification of tumors with a sufficient receptor overexpression for diagnostic or therapeutic intervention using SP analogs.
Type of Medium:
Online Resource
ISSN:
0022-1554
,
1551-5044
DOI:
10.1369/jhc.6A6966.2006
Language:
English
Publisher:
SAGE Publications
Publication Date:
2006
detail.hit.zdb_id:
1421306-0
SSG:
12
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