1997
DOI: 10.1016/s1071-5576(97)00016-6
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Human endometrial transforming growth factor-α: A transmembrane, surface epithelial protein that transiently disappears during the midsecretory phase of the menstrual cycle

Abstract: Western blot data were consistent with the hypothesis that the extracellular segment of TGF-alpha is cleaved from the transmembrane precursor in vivo, as has been demonstrated in other tissues. Immunohistochemistry demonstrated that the TGF-alpha antigens are concentrated in the luminal surface epithelium and decline and disappear in the early to midsecretory phase. These findings suggest that the most active period of membrane-bound TGF-alpha cleavage corresponds with the interval during which preimplantation… Show more

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Cited by 11 publications
(2 citation statements)
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“…When the polyclonal anti-human or rat recombinant TGF-α antibodies were used to probe the blots (Figure 3A, showing representative results with the rabbit anti-human recombinant TGF-α IgG), TGF-α immunoreactivity was shown as a 6-kD band with the recombinant peptide (Figure 3A, Lane 2), and three bands with human colon protein of predominantly 6 kD, and around 15-18 and 25-28 kD in molecular weight (Figure 3A, lane 3). The two larger molecular species probably represent precursor peptides of TGF-α which were also shown in some previous studies (Hansard et al 1997; Hoffmann et al 1997; Tureaud et al 1997; Wang et al 1997). Using this antibody, no TGF-α immunoreactivity was found in colon protein samples from knockout mice (Figure 3A, Lane 4), but one band of around 25-28 kD was revealed in the sample from wild-type mice (Figure 3A, Lane 5).…”
Section: Resultssupporting
confidence: 82%
See 1 more Smart Citation
“…When the polyclonal anti-human or rat recombinant TGF-α antibodies were used to probe the blots (Figure 3A, showing representative results with the rabbit anti-human recombinant TGF-α IgG), TGF-α immunoreactivity was shown as a 6-kD band with the recombinant peptide (Figure 3A, Lane 2), and three bands with human colon protein of predominantly 6 kD, and around 15-18 and 25-28 kD in molecular weight (Figure 3A, lane 3). The two larger molecular species probably represent precursor peptides of TGF-α which were also shown in some previous studies (Hansard et al 1997; Hoffmann et al 1997; Tureaud et al 1997; Wang et al 1997). Using this antibody, no TGF-α immunoreactivity was found in colon protein samples from knockout mice (Figure 3A, Lane 4), but one band of around 25-28 kD was revealed in the sample from wild-type mice (Figure 3A, Lane 5).…”
Section: Resultssupporting
confidence: 82%
“…In human colon extract (Figure 3B, Lane 5), apart from the presence of the immunoglobulin IgG 2a light chain (around 30 kD) and heavy chain (around 50 kD), which correspond to the bands of the normal mouse IgG 2a control (Figure 3B, Lane 10), there was a band of around 25-28 kD. This 25-28-kD band, also seen in some previous studies (Hansard et al 1997; Hoffmann et al 1997; Wang et al 1997), could be assumed to be a TGF-α precursor. After human colon was fixed in either formalin (Figure 3B, Lane 8) or in Methacarn (Figure 3B, Lane 9) and processed for paraffin embedding, the immunoreactive material in the protein extracts by this monoclonal antibody appeared to be around 31 and 66 kD in size, the identities of which remain to be determined.…”
Section: Resultssupporting
confidence: 81%