Differential expression of type I hair keratins.
Differential expression of type I hair keratins.
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I 型头发角蛋白的差异表达。
DOI：
10.1111/1523-1747.ep12874436
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Yu,DW
中科院分区：
文献类型：
--
作者：
Bertolino,AP;Checkla,DM;Heitner,S;Freedberg,IM;Yu,DW
毛囊为研究生长和分化提供了一个极好的系统。毛发角蛋白是这些事件的有用的组织特异性分子标记物。通过比较第二个小鼠I型毛发角蛋白cDNA克隆MHKA-2与我们先前描述的MHKA-1，我们已经能够对比最小（mHa4）和最大（mHa1）主要I型毛发角蛋白的核苷酸序列和相应的推导的氨基酸序列。两个核苷酸序列和两个推导的氨基酸序列具有高度同一性，但具有适合于产生特异性分子探针的不同片段。邻近中央螺旋结构域的氨基酸序列的比较已经证明了在I型毛发角蛋白非螺旋末端中的同源亚结构域，命名为H1和H2。虽然在羧基末端非螺旋结构域中只有56%的氨基酸同一性，但在该结构域中已确定了一个共同序列T----CGPC--R，表明该分子的这一部分可能具有共同的功能作用。此外，似乎mHa4可能与mHa1部分不同，因为缺失了H2亚结构域和保守序列之间的片段。用AmHa1（一种针对mHa1的单特异性多克隆抗体）和AE13（一种针对所有I型毛发角蛋白的特异性抗体）对小鼠和人毛囊进行染色，表明两个物种中个别I型毛发角蛋白的差异表达。这支持了我们的假设，即不同的功能需求是由头发角蛋白的多样性满足。
The hair follicle provides an excellent system in which to study growth and differentiation. Hair keratins are useful tissue-specific molecular markers for these events. By comparing a second mouse Type I hair keratin cDNA clone, MHKA-2, with our previously described MHKA-1, we have been able to contrast the nucleotide sequences and corresponding deduced amino acid sequences of the smallest (mHa4) and the largest (mHa1) major Type I hair keratins. Both nucleotide sequences and both deduced amino acid sequences share high identity but have distinct segments suitable for generation of specific molecular probes. Comparison of amino acid sequences adjacent to the central helical domains has demonstrated homologous subdomains, designated H1 and H2, in the Type I hair keratin nonhelical termini. Although there is only 56% amino acid identity in the carboxy-terminal nonhelical domains, a common sequence, T–––-CGPC––R, has been identified in this domain, suggesting a possible common functional role for this portion of the molecule. In addition, it appears that mHa4 may differ in part from mHa1 by deletion of a segment between the H2 subdomain and the conserved sequence. Staining of mouse and human hair follicles with AmHa1, a mono-specific polyclonal antibody for mHa1, and AE13, an antibody specific for all Type I hair keratins, suggests differential expression of individual Type I hair keratins in both species. This supports our hypothesis that distinct functional requirements are satisfied by the multiplicity of hair keratins.