Disease relevance of C21orf45

• The rat glioblastoma cell line B28 was stably transfected with human L1 [1].
• Neither anti-Ran-1 nor the monoclonal antibody bound to neurons, fibroblasts or glial cells in newborn rat cerebellum cultures, the rat muscle cell line L6, the transformed rat fibroblast cell line Rat 1, the rat brain tumor cell line B28 or the mouse Schwannoma cell line TR6B [2].
• [B28 Asp]-human insulin (insulin aspart, CAS 116094-23-6, X14) is a rapidly absorbed analogue of human insulin currently undergoing development for the treatment of diabetes mellitus [3].

High impact information on C21orf45

• Insulin aspart (B28 asp-insulin): a fast-acting analog of human insulin: absorption kinetics and action profile compared with regular human insulin in healthy nondiabetic subjects [4].
• OBJECTIVE: To evaluate the efficacy of the insulin analog lispro (Lys B28, Pro B29) in severe insulin resistance caused by human insulin antibodies [5].
• Insulin's natural tendency to form dimers and hexamers is significantly reduced in a mutant insulin B28 Pro --> Asp, which has been designed as a monomeric, rapid-acting hormone for therapeutic purposes [6].
• The structure of a cross-linked derivative of B28 Asp insulin, containing an Ala-Lys dipeptide linker between residues B30 Ala and A1 Gly, has also determined [6].
• Two structures of B28 Asp insulin have been determined from crystals grown in the presence of phenol and m-cresol [6].

Biological context of C21orf45

• An eight amino acid sequence, CAKGDWNC, from disintegrin barbourin, was introduced into an inactive human proinsulin molecule between the B28 and A2 sites to construct a chimeric, anti-thrombosis recombinant protein [7].
• Pressure was applied at acupuncture points Gv4, Gv15, Gv20, B23, B28, B32, H7, H9, St36, Sp4, Sp6, Sp12, Ren2, Ren3, Ren6, K3 and K5 [8].
• Other residues situated at the interface between the 2 monomers were found to make favorable but smaller contributions to the dimerization: Tyr B16, Val B12, and Pro B28, and to an even lesser extent, Gly B23 [9].

Anatomical context of C21orf45

• Co-localization of pp5644 and FASP1 in cytoplasm in Hela cells could further support the interaction [10].

Associations of C21orf45 with chemical compounds

• To determine the conformational properties of the C-terminal region of the insulin B-chain relative to the helical core of the molecule, we have investigated the fluorescence properties of an insulin analog in which amino acids B28 and B29 have been substituted with a tryptophan and proline residue respectively, ([WB28,PB29]insulin) [11].
• Replacement of HB10 with aspartic acid increased stability while substitutions at B28 and/or B29 were either comparable to insulin or had decreased stability [12].
• The natural sequence in human insulin at this position is proline at B28 and lysine at B29 [13].

Other interactions of C21orf45

• The pp5644-interacting protein FAPP1 (phosphatidylinositol-four-phosphate adaptor protein1) associated protein-1, called FASP1, was obtained by using yeast two-hybrid system [10].

Analytical, diagnostic and therapeutic context of C21orf45

• The interaction between pp5644 and FASP1 was experimentally confirmed by GST pull-down assay in vitro and co-immunoprecipitation assay in vivo [10].
• In the antibacterial bioassay, the stems and the roots of H. capitellata showed moderate activity against the 4 tested bacteria while the leaves showed moderate activity towards B. subtilis B28, MRSA and P. aeruginosa only [14].

References