High impact information on LOC397939

• A comparative analysis of the Xenopus and mammalian proteins revealed a striking regional conservation with an overall sequence identity of 48% for SgII and 61% for SgIII [1].
• Surprisingly, and in contrast to what holds for POMC and the convertases, mRNAs for secretogranin II and III (SgII, SgIII) and 7B2 were not only expressed during neural development, but could already be detected in unfertilized mature oocytes, the first cleavage stages and in blastula-stage embryos [2].
• When cells were treated with the fungal metabolite brefeldin A or with the specific vacuolar H+-ATPase inhibitor bafilomycin A1, the processing of SgII and the release of its cleavage products were strongly inhibited, indicating that its processing commenced in the later compartments of the secretory pathway [3].
• Granin proteins (chromogranin A and secretogranin II C23-3 and C26-3) in the endocrine pancreas of amphibians [4].
• The occurrence, distribution and possible cellular colocalizations of chromogranin A (CgA) and of two synthetic secretogranin II peptides (SgIIC23-3 and SgIIC26-3) with serotonin, somatostatin, neurotensin, pancreatic polypeptide and bombesin have been investigated immunohistochemically in the amphibian gut [5].

Other interactions of LOC397939

• However, in SgII and especially in SgIII, a substantial portion of the potential dibasic cleavage sites is not conserved, arguing against the idea that these granins serve solely as peptide precursors [1].

Analytical, diagnostic and therapeutic context of LOC397939

• Pulse-chase incubations in combination with immunoprecipitation analysis showed that SgII was synthesised as an 84-kDa precursor protein which was processed to fragments of 69, 54, 34, 21 and 15 kDa [3].

References