Author:
Weber P.J.A.,Eckard C.P.,Gonser S.,Otto H.,Folkers G.,Beck-Sickinger A.G.
Abstract
AbstractThymopoietins (TMPOs) are a group of ubiquitously expressed nuclear proteins. They are suggested to play an important role in nuclear envelope organization and cell cycle control, as has been shown for lamina-associated polypeptides 2 α and β, which are the rat homologs of human TMPOα and TMPOβ, respectively. The recent isolation and characterization of seven mouse TMPO mRNA transcripts named TMPO-α, β, β', γ, ε, δ, and ζ, suggest that more than the three previously reported transcripts, α, β, and γ forms, may exist in humans. Here we report on the demonstration of putative human TMPOδ and ε by immunoblotting of human cell lines using a newly prepared polyclonal antiserum against the common N-terminal region of TMPO. Furthermore, we prepared the first truly TMPO-β-specific, affinity-purified polyclonal antiserum, using a part of the human analog of the β-specific domain of mouse TMPO 220–259 for immunization. We showed that human TMPOβ is highly expressed in all cancerous cells tested, while hardly any cross-reactivities with other proteins could be detected. In contrast to the high expression of human TMPOβ in the cancer-derived neuroblastoma cell lines SK-N-MC and SMS-KAN, we found very low expression of human TMPOβ in low-proliferative nerve tissue. These data led us to the assumption that expression of TMPOβ may correlate with the occurrence of cancer, and therefore may serve as a new tumor marker, or even as a new target for cancer therapy.
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Cited by
15 articles.
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