Figure 2 Expression of APMCF1 in normal and malignant human tissues. Expression of APMCF1 in normal and malignant human tissues was detected by immunohistochemistry. (A) esophagus carcinoma; (B) colon carcinoma; (C) gastric carcinoma; (D) liver carcinoma; (E) breast carcinoma; (F) lung carcinoma; (G) testis seminoma; (H) brain; (I) gastric mucosa. Bar = 50 μm. We also detect the specific expression pattern of APMCF1 in several common carcinomas including
liver, colon, esophagus, lung selleckchem and breast carcinomas in a large sample (Table 2). The positive ratios of APMCF1 in liver, colon, esophagus, lung and breast carcinomas were 96%, 80%, 57%, 58% and 34% respectively. Discussion Small GTP-binding proteins (G proteins) are monomeric G proteins with GTPase structure in amino acid sequence structure and molecular masses of 20–40 kDa, currently existing in eukaryotes from yeast to human and containing more than 100 members. Based on both their sequence homology and function, they have been subdivided into at least six Pitavastatin solubility dmso families: Ras, Rho, Rab, Sar1/Arf, Ran, and Rad/Gem [7, 8]. They regulate a wide variety of cell functions in response to diverse stimuli, such as cell growth, apoptosis, lipid metabolism, cytoarchitecture,
membrane trafficking, and transcriptional regulation [9–12]. However, uncontrolled activation of these multifunctional proteins (i.e. point mutations or overexpression) Interleukin-2 receptor cause them insensitive to regulatory signals, leading to uncontrolled proliferation, enhanced angiogenesis, inhibition of apoptosis, and
genetic instability, all of which result in tumor development [12–14]. Their cellular oncogenes were then identified, and their mutations were furthermore found in some human carcinomas [15–17]. The predicted protein of APMCF1 contained a GTPase domain closely related to ADP-ribosylation factor family (ARF) and Sar1p-like members of the Ras-family of small GTPases, suggesting it was a new member of small GTP-binding proteins and also a human homolog of SRβ . The SR is a heterodimeric complex assembled by the two GTPases SRα and SRβ . The eukaryotic signal recognition particle (SRP) and its receptor (SR) play a central role in co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). In eukaryotes, this process is tightly controlled by the concerted action of three G proteins, the 54-kD subunit of SRP, SRα and SRβ [19–22]. All SRβ members in species other than human are cytoplasmic proteins. The subcellular location in present study based on APMCF1-GFP fusion protein identified that APMCF1 has a cytosol distribution pattern which also concoined it was a human homolog of SRβ. There is little information about the JNK-IN-8 function of AMPCF1 so far.