Ibaraki K, Kozak C A, Wewer U M, Albrechtsen R, Young M F
Bone Research Branch, National Institute of Dental Research National Institutes of Health (NIH), Bethesda, Maryland 20892, USA.
Mamm Genome. 1995 Oct;6(10):693-6. doi: 10.1007/BF00354289.
Tetranectin is a plasminogen-binding tetrameric protein originally isolated from plasma. Expression of tetranectin appears ubiquitous, although particularly high expression is noted in the stroma of malignant tumors and during mineralization. To dissect the molecular basis of tetranectin gene regulation, mouse tetranectin cDNA was cloned from a 16-day-old mouse embryo library. Sequence analysis revealed a 992-bp cDNA with an open reading frame of 606 bp, which is identical in length to the human tetranectin cDNA. The deduced amino acid sequence showed high homology to the human cDNA with 76% identity and 87% similarity at the amino acid level. Sequence comparisons between mouse and human tetranectin and some C-type lectins confirmed a complete conservation in the position of six cysteines as well as numerous other amino acid residues, indicating an essential structure for potential function(s) of tetranectin. The sequence analysis revealed a difference in both sequence and size of the noncoding regions between mouse and human cDNAs. Northern analysis of the various tissues from mouse, rat, and cow showed the major transcript(s) to be approximately 1 kb, which is similar in size to that observed in human. Although additional minor bands of 1.5 and 3.3 kb were found in Northern blots, RT-PCR (reverse transcription polymerase chain reaction) analysis failed to provide evidence that these minor bands are products of the tetranectin gene. Finally, the genetic map location for this gene, Tna, was determined to be on distal mouse Chromosome (Chr) 9 by analysis of two sets of multilocus crosses.
纤连蛋白是一种最初从血浆中分离出来的与纤溶酶原结合的四聚体蛋白。纤连蛋白的表达似乎无处不在，尽管在恶性肿瘤的基质中以及矿化过程中观察到其表达特别高。为了剖析纤连蛋白基因调控的分子基础，从小鼠胚胎文库中克隆了小鼠纤连蛋白cDNA。序列分析显示一个992bp的cDNA，其开放阅读框为606bp，长度与人纤连蛋白cDNA相同。推导的氨基酸序列与人cDNA具有高度同源性，在氨基酸水平上同一性为76%，相似性为87%。小鼠和人纤连蛋白与一些C型凝集素之间的序列比较证实了六个半胱氨酸以及许多其他氨基酸残基位置的完全保守，表明纤连蛋白潜在功能的基本结构。序列分析显示小鼠和人cDNA的非编码区在序列和大小上都存在差异。对小鼠、大鼠和牛的各种组织进行的Northern分析表明，主要转录本约为1kb，大小与人中观察到的相似。尽管在Northern印迹中发现了1.5kb和3.3kb的额外小条带，但逆转录聚合酶链反应（RT-PCR）分析未能提供证据表明这些小条带是纤连蛋白基因的产物。最后，通过分析两组多位点杂交，确定该基因Tna的遗传图谱位置在小鼠9号染色体远端。
