A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin.
A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin.
复制标题
编码富含半胱氨酸的阳离子肽的新型小鼠基因家族。
DOI：
10.1016/s0021-9258(19)38746-0
复制
发表时间：
1990
期刊：
影响因子：
--
通讯作者：
J. Lualdi
中科院分区：
文献类型：
--
作者：
A. Ouellette;J. Lualdi
Cryptdin是小鼠小肠中的潘氏细胞皮质抑素/防御素。为了帮助确定的肠道作用的cryptdin，cryptdin相关序列（CRS）的mRNA已被表征的发育调控，序列同源性，推定的编码功能，并在骨髓细胞中的出现。Cryptdin，CRS 1C和CRS 4C mRNA从不同的基因转录，在小肠中以相等的丰度出现，并在产后第2周和第3周期间一致出现在小肠中。在成年小鼠骨髓中检测不到Cryptdin和CRS 1C mRNA，但对CRS 4C mRNA的5 '或3'非翻译区具有特异性的探针与中等丰度的1.05-β-淀粉酶骨髓mRNA杂交，而小肠中的0.75-β-淀粉酶mRNA高度丰度。对应于推断的cryptdin、CRS 1C和CRS 4C mRNA的前原编码区的核苷酸序列包含高度保守的200个碱基对的92%序列相似性区域（CSE.2），但mRNA在其他方面不同源。推导的CRS 1C和CRS 4C多肽是分泌的、阳离子的、富含脯氨酸和半胱氨酸的含有Cys-Pro-X重复序列的肽的明显前体。然而，与cryptdin不同，所提出的CRS 1C和CRS 4C成熟肽区域缺乏防御素的结构基序特征。试图找到推定的CRS肽和现有的蛋白质序列之间的同源性一直是不成功的，导致我们推测，CRS 1C和CRS 4C代表了一个新的家庭nondefensin抗菌肽在小鼠小肠。
Cryptdin is a Paneth cell corticostatin/defensin in the mouse small bowel. To help define the intestinal role of cryptdin, cryptdin-related sequence (CRS) mRNAs have been characterized with respect to developmental regulation, sequence homology, putative coding function, and occurrence in myeloid cells. Cryptdin, CRS1C, and CRS4C mRNAs are transcribed from separate genes, occur at equivalent abundance in small intestine, and appear in the small bowel in concert during the 2nd and 3rd weeks postpartum. Cryptdin and CRS1C mRNAs are not detectable in adult mouse bone marrow, but probes specific for the 5'- or the 3'-untranslated regions of CRS4C mRNA hybridize to a moderately abundant 1.05-kilobase bone marrow mRNA in contrast to a highly abundant 0.75-kilobase mRNA in small intestine. Nucleotide sequences corresponding to the deduced prepro-coding regions of cryptdin, CRS1C, and CRS4C mRNAs contain a highly conserved 200-base pair region of 92% sequence similarity (CSE.2), but the mRNAs are not homologous otherwise. The deduced CRS1C and CRS4C polypeptides are apparent precursors of secreted, cationic, proline- and cysteine-rich peptides that contain Cys-Pro-X repeats. Unlike cryptdin, however, the proposed CRS1C and CRS4C mature peptide regions lack the structural motif characteristic of defensins. Attempts to find homologies between the putative CRS peptides and existing protein sequences have been unsuccessful, leading us to speculate that CRS1C and CRS4C represent a new family of nondefensin antimicrobial peptides in the mouse small bowel.