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脊椎动物细胞与发育生物学中的膜锚定丝氨酸蛋白酶。

Membrane-anchored serine proteases in vertebrate cell and developmental biology.

机构信息

Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA.

出版信息

Annu Rev Cell Dev Biol. 2011;27:213-35. doi: 10.1146/annurev-cellbio-092910-154247. Epub 2011 Jun 29.

DOI:10.1146/annurev-cellbio-092910-154247
PMID:21721945
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3391589/
Abstract

Analysis of vertebrate genome sequences at the turn of the millennium revealed that a vastly larger repertoire of enzymes execute proteolytic cleavage reactions within the pericellular and extracellular environments than was anticipated from biochemical and molecular analysis. Most unexpected was the unveiling of an entire new family of structurally unique multidomain serine proteases that are anchored directly to the plasma membrane. Unlike secreted serine proteases, which function primarily in tissue repair, immunity, and nutrient uptake, these membrane-anchored serine proteases regulate fundamental cellular and developmental processes, including tissue morphogenesis, epithelial barrier function, ion and water transport, cellular iron export, and fertilization. Here the cellular and developmental biology of this fascinating new group of proteases is reviewed. Particularly highlighted is how the study of membrane-anchored serine proteases has expanded our knowledge of the range of physiological processes that require regulated proteolysis at the cell surface.

摘要

在千年之交对脊椎动物基因组序列进行分析后发现,细胞周围和细胞外环境中执行蛋白水解切割反应的酶的种类远远超过了生化和分子分析的预期。最令人意外的是,揭示了一整类结构独特的新型多结构域丝氨酸蛋白酶,它们直接锚定在质膜上。与主要在组织修复、免疫和营养吸收中发挥作用的分泌型丝氨酸蛋白酶不同,这些膜结合的丝氨酸蛋白酶调节基本的细胞和发育过程,包括组织形态发生、上皮屏障功能、离子和水转运、细胞铁输出和受精。本文综述了这组引人入胜的新型蛋白酶的细胞和发育生物学。特别强调的是,研究膜结合的丝氨酸蛋白酶如何扩展了我们对需要在细胞表面进行调控蛋白水解的生理过程范围的认识。

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本文引用的文献

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Transport via the transcytotic pathway makes prostasin available as a substrate for matriptase.通过胞吞作用途径运输可使脯氨酰蛋白酶原作为组织蛋白酶 M 的底物。
J Biol Chem. 2011 Feb 18;286(7):5793-802. doi: 10.1074/jbc.M110.186874. Epub 2010 Dec 10.
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Suppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 protein.急性铁缺乏时肝脏铁调素表达的抑制与组织蛋白酶 2 蛋白的增加有关。
Blood. 2011 Feb 3;117(5):1687-99. doi: 10.1182/blood-2010-06-287292. Epub 2010 Nov 29.
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Iron-deficiency anemia from matriptase-2 inactivation is dependent on the presence of functional Bmp6.由于组织蛋白酶-2失活引起的缺铁性贫血依赖于功能性 Bmp6 的存在。
Blood. 2011 Jan 13;117(2):647-50. doi: 10.1182/blood-2010-07-295147. Epub 2010 Oct 12.
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A novel TMPRSS6 mutation that prevents protease auto-activation causes IRIDA.一个新的 TMPRSS6 突变阻止了蛋白酶的自动激活导致了 IRIDA。
Biochem J. 2010 Nov 1;431(3):363-71. doi: 10.1042/BJ20100668.
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Thyroxine treatments do not correct inner ear defects in tmprss1 mutant mice.甲状腺素治疗无法纠正tmprss1突变小鼠的内耳缺陷。
Neuroreport. 2010 Sep 15;21(13):897-901. doi: 10.1097/WNR.0b013e32833dbd2d.
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Identification of the matriptase second CUB domain as the secondary site for interaction with hepatocyte growth factor activator inhibitor type-1.鉴定组织蛋白酶丝氨酸蛋白酶 2 的第二个 CUB 结构域是与肝细胞生长因子激活物抑制剂 1 相互作用的次要位点。
J Biol Chem. 2010 Oct 22;285(43):33394-33403. doi: 10.1074/jbc.M110.115816. Epub 2010 Aug 3.
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Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome.丝氨酸蛋白酶组织抑制剂(matriptase)在 Netherton 综合征小鼠模型中启动表皮前激肽释放酶的激活和疾病发生。
Nat Genet. 2010 Aug;42(8):676-83. doi: 10.1038/ng.629. Epub 2010 Jul 25.
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Apical serine protease activity is necessary for assembly of a high-resistance renal collecting duct epithelium.顶端丝氨酸蛋白酶活性对于形成高电阻的肾集合管上皮是必需的。
Acta Physiol (Oxf). 2010 Dec;200(4):347-59. doi: 10.1111/j.1748-1716.2010.02170.x.
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Processing of pro-B-type natriuretic peptide: furin and corin as candidate convertases.脑啡肽酶和羧基肽酶 M 作为候选转化酶参与脑利钠肽前体的加工。
Clin Chem. 2010 Jul;56(7):1166-76. doi: 10.1373/clinchem.2010.143883. Epub 2010 May 20.
10
Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro.缺乏两种精子丝氨酸蛋白酶(ACR 和 PRSS21)的小鼠是不育的,但突变精子在体外是不育的。
Biol Reprod. 2010 Sep;83(3):359-69. doi: 10.1095/biolreprod.109.083089. Epub 2010 May 19.