Disease relevance of Egfbp2

• In a previous study, we have shown that a kallikrein-like prorenin converting enzyme (PRCE C) is elevated in the submandibular gland tissue of a mouse line (BPH) that was genetically selected and inbred for high blood pressure in comparison to normotensive line (BPN) that was derived from the ancestors of BPH line [1].

High impact information on Egfbp2

• Interestingly, Klk-13, but not Klk-1, caused a proliferative response of splenic T cells from IQI/Jic mice from the age of 4 weeks onward [2].
• These results indicate that Klk-13 acts as an autoantigen and may increase T cells responsive to organs commonly expressing Klk-13, playing a pivotal role in the etiology of progression of disease in IQI/Jic mice [2].
• In addition, remarkably enhanced expression of Klk-13 was observed in the salivary glands of the mice in accordance with the development of inflammatory lesions [2].
• Western blot analysis using an antiserum against this enzyme gave rise to multiple bands in mouse submandibular glands, suggesting that PRECE is a member of a protease family [3].
• Mouse submandibular gland prorenin-converting enzyme (PRECE) consists of the two polypeptide chains of 17 and 10 kDa and cleaves mouse Ren-2 prorenin at a dibasic site to yield mature renin [3].

Biological context of Egfbp2

• Conditioned medium from Chinese hamster ovary cells transfected with an expression plasmid for PRECE had prorenin converting activity [3].
• The mGK-13 structure is similar to other members of the mammalian serine protease family, having five conserved disulfide bonds and an active site located in the cleft between two beta-barrel domains [4].
• A cDNA clone has been isolated that corresponds to the entire translated region of the mRNA coding for the epidermal growth factor-binding protein type B. The complete nucleotide sequence and the predicted amino acid sequence of the protein were elucidated [5].
• Substrate specificity of prorenin converting enzyme of mouse submandibular gland. Analysis using site-directed mutagenesis [6].
• Tissue distribution and characterization of prorenin-converting enzyme in mouse [7].

Anatomical context of Egfbp2

• Expression of an allozyme of prorenin-converting enzyme in the submandibular gland of DBA/2N mice [8].

Associations of Egfbp2 with chemical compounds

• A crystal structure of the serine protease, mouse glandular kallikrein 13 (mGK-13) has been determined at 2.6-A resolution [4].

Other interactions of Egfbp2

• Tissue kallikrein mK13 was confirmed to be a prorenin-converting enzyme; and mK9, which was earlier shown to be an EGF-binding protein, was found to cleave mouse Ren 2 prorenin specifically and convert it to mature renin with an activity of approximately 1/10 of that of mK13 [9].
• Amino acid sequencing showed this protein to be highly homologous to two tissue kallikreins, mK13 and mK26, also known as prorenin-converting enzymes PRECE and PRECE-2, respectively [8].
• The crystal structure of the mouse glandular kallikrein-13 (prorenin converting enzyme) [4].
• These results indicate that PRECE is involved in the maturation of two bioactive polypeptides expressed in mouse submandibular glands, Ren-2 renin and epidermal growth factor [3].
• The mGK-13 structure reveals for the first time an ordered kallikrein loop conformation containing a short 3(10) helix [4].

Analytical, diagnostic and therapeutic context of Egfbp2

• We have recently demonstrated, by protein and cDNA sequence analyses, that prorenin converting enzyme (PRECE) in the ICR mouse submandibular gland is identical to the epidermal growth factor-binding protein (EGF-BP) type B, the mGK-13 gene product identified in Balb/c mouse [10].

References