Suppr超能文献

壁虎附肢黏附细胞生物学。

Cell biology of adhesive setae in gecko lizards.

机构信息

Dipartimento di Biologia Evoluzionistica Sperimentale, University of Bologna, via Selmi 3, 40126 Bologna, Italy.

出版信息

Zoology (Jena). 2009;112(6):403-24. doi: 10.1016/j.zool.2009.03.005. Epub 2009 Sep 26.

Abstract

Adhesive devices of digital pads of gecko lizards are formed by microscopic hair-like structures termed setae that derive from the interaction between the oberhautchen and the clear layer of the epidermis. The two layers form the shedding complex and permit skin shedding in lizards. Setae consist of a resistant but flexible corneous material largely made of keratin-associated beta-proteins (KA beta Ps, formerly called beta-keratins) of 8-22 kDa and of alpha-keratins of 45-60 kDa. In Gekko gecko, 19 sauropsid keratin-associated beta-proteins (sKAbetaPs) and at least two larger alpha-keratins are expressed in the setae. Some sKA beta Ps are rich in cysteine (111-114 amino acids), while others are rich in glycine (169-219 amino acids). In the entire genome of Anolis carolinensis 40 Ka beta Ps are present and participate in the formation of all types of scales, pad lamellae and claws. Nineteen sKA beta Ps comprise cysteine-rich 9.2-14.4 kDa proteins of 89-142 amino acids, and 19 are glycine-rich 16.5-22.0 kDa proteins containing 162-225 amino acids, and only two types of sKA beta Ps are cysteine- and glycine-poor proteins. Genes coding for these proteins contain an intron in the 5'-non-coding region, a typical characteristic of most sauropsid Ka beta Ps. Gecko KA beta Ps show a central amino acid region of high homology and a beta-pleated conformation that is likely responsible for the polymerization of Ka beta Ps into long and resistant filaments. The association of numerous filaments, probably over a framework of alpha-keratins, permits the formation of bundles of corneous material for the elongation of setae, which may be over 100 microm long. The terminals branching off each seta may derive from the organization of the cytoskeleton and from the mechanical separation of keratin bundles located at the terminal apex of setae.

摘要

壁虎的趾垫的粘性装置是由微小的毛发状结构称为刚毛组成的,这些刚毛源于 oberhautchen 和表皮的透明层之间的相互作用。这两层形成了脱皮复合物,并允许蜥蜴蜕皮。刚毛由一种具有弹性的角蛋白材料组成,主要由 8-22 kDa 的角蛋白相关β-蛋白(KAβPs,以前称为β-角蛋白)和 45-60 kDa 的α-角蛋白组成。在壁虎中,19 种蜥脚类动物角蛋白相关β-蛋白(sKAβPs)和至少两种较大的α-角蛋白在刚毛中表达。一些 sKAβPs 富含半胱氨酸(111-114 个氨基酸),而另一些则富含甘氨酸(169-219 个氨基酸)。在 Anolis carolinensis 的整个基因组中,有 40 种 KaβPs 存在,并参与所有类型的鳞片、趾垫和爪子的形成。19 种 sKAβPs 组成富含半胱氨酸的 9.2-14.4 kDa 蛋白质,由 89-142 个氨基酸组成,19 种是富含甘氨酸的 16.5-22.0 kDa 蛋白质,含有 162-225 个氨基酸,只有两种类型的 sKAβPs 是半胱氨酸和甘氨酸含量低的蛋白质。编码这些蛋白质的基因在 5'非编码区含有内含子,这是大多数蜥脚类动物 KaβPs 的典型特征。壁虎 KaβPs 显示出高度同源的中心氨基酸区域和β-折叠构象,这可能是 KaβPs 聚合成长而有抗性的纤维的原因。大量纤维的结合,可能是在α-角蛋白的框架上,允许形成角蛋白材料的束,用于刚毛的伸长,刚毛可能超过 100 微米长。每个刚毛分支的末端可能来自于细胞骨架的组织和位于刚毛末端顶点的角蛋白束的机械分离。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验